4-α- and 14-β-gluco-oligosaccharides, non-reducing gluco-oligosaccharides and L-arabinose, which are not substrates of EC 1.1.3.10. Sugars are oxidized in their pyranose but not in their furanose form.Continued from EC 1.1.2 and EC 1.1.3
Sections
EC 1.1.4 With a disulfide as acceptor
EC 1.1.5 With a quinone or similar compound as acceptor
EC 1.1.7 With an iron-sulfur protein as acceptor
EC 1.1.98 With other, known, physiological acceptors
EC 1.1.99 With unknown physiological acceptors
[EC 1.1.4.2 Transferred entry: vitamin-K-epoxide reductase (warfarin-insensitive). Now EC 1.17.4.5, vitamin-K-epoxide reductase (warfarin-insensitive) (EC 1.1.4.2 created 1989, deleted 2014)]
Accepted name: glucose 1-dehydrogenase (PQQ,quinone)
Reaction: D-glucose + ubiquinone = D-glucono-1,5-lactone + ubiquinol
Other name(s): quinoprotein glucose dehydrogenase; membrane-bound glucose dehydrogenase; mGDH; glucose dehydrogenase (PQQ-dependent); glucose dehydrogenase (pyrroloquinoline-quinone); quinoprotein D-glucose dehydrogenase
Systematic name: D-glucose:ubiquinone oxidoreductase
Comments: Integral membrane protein containing PQQ as a cofactor. It also contains bound ubiquinone and Mg2+ or Ca2+. Electron acceptor is membrane ubiquinone but usually assayed with phenazine methosulfate. Like in all other quinoprotein alcohol dehydrogenases the catalytic domain has an 8-bladed 'propeller' structure. It occurs in a wide range of bacteria. Catalyses a direct oxidation of the pyranose form of D-glucose to the lactone and thence to D-gluconate in the periplasm. Oxidizes other monosaccharides including the pyranose forms of pentoses.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 81669-60-5
References:
1. Yamada, M., Sumi, K., Matsushita, K., Adachi, O. and Yamada, Y. Topological analysis of quinoprotein glucose-dehydrogenase in Escherichia coli and its ubiquinone-binding site. J. Biol. Chem. 268 (1993) 12812-12817. [PMID: 8509415]
2. Dewanti, A.R. and Duine, J.A. Reconstitution of membrane-integrated quinoprotein glucose dehydrogenase apoenzyme with PQQ and the holoenzyme's mechanism of action. Biochemistry 37 (1998) 6810-6818. [PMID: 9578566]
3. Duine, J.A., Frank, J. and Van Zeeland, J.K. Glucose dehydrogenase from Acinetobacter calcoaceticus: a 'quinoprotein'. FEBS Lett. 108 (1979) 443-446. [PMID: 520586]
4. Ameyama, M., Matsushita, K., Ohno, Y., Shinagawa, E. and Adachi, O. Existence of a novel prosthetic group, PQQ, in membrane-bound, electron transport chain-linked, primary dehydrogenases of oxidative bacteria. FEBS Lett. 130 (1981) 179-183. [PMID: 6793395]
5. Cozier, G.E. and Anthony, C. Structure of the quinoprotein glucose dehydrogenase of Escherichia coli modelled on that of methanol dehydrogenase from Methylobacterium extorquens. Biochem. J. 312 (1995) 679-685. [PMID: 8554505]
6. Cozier, G.E., Salleh, R.A. and Anthony, C. Characterization of the membrane quinoprotein glucose dehydrogenase from Escherichia coli and characterization of a site-directed mutant in which histidine-262 has been changed to tyrosine. Biochem. J. 340 (1999) 639-647. [PMID: 10359647]
7. Elias, M.D., Tanaka, M., Sakai, M., Toyama, H., Matsushita, K., Adachi, O. and Yamada, M. C-terminal periplasmic domain of Escherichia coli quinoprotein glucose dehydrogenase transfers electrons to ubiquinone. J. Biol. Chem. 276 (2001) 48356-48361. [PMID: 11604400]
8. James, P.L. and Anthony, C. The metal ion in the active site of the membrane glucose dehydrogenase of Escherichia coli. Biochim. Biophys. Acta 1647 (2003) 200-205. [PMID: 12686133]
9. Elias, M.D., Nakamura, S., Migita, C.T., Miyoshi, H., Toyama, H., Matsushita, K., Adachi, O. and Yamada, M. Occurrence of a bound ubiquinone and its function in Escherichia coli membrane-bound quinoprotein glucose dehydrogenase. J. Biol. Chem. 279 (2004) 3078-3083. [PMID: 14612441]
10. Mustafa, G., Ishikawa, Y., Kobayashi, K., Migita, C.T., Elias, M.D., Nakamura, S., Tagawa, S. and Yamada, M. Amino acid residues interacting with both the bound quinone and coenzyme, pyrroloquinoline quinone, in Escherichia coli membrane-bound glucose dehydrogenase. J. Biol. Chem. 283 (2008) 22215-22221. [PMID: 18550551]
Accepted name: glycerol-3-phosphate dehydrogenase
Reaction: sn-glycerol 3-phosphate + a quinone = glycerone phosphate + a quinol
Glossary: glycerone phosphate = dihydroxyacetone phosphate = 3-hydroxy-2-oxopropyl phosphate
Other name(s): α-glycerophosphate dehydrogenase; α-glycerophosphate dehydrogenase (acceptor); anaerobic glycerol-3-phosphate dehydrogenase; DL-glycerol 3-phosphate oxidase (misleading); FAD-dependent glycerol-3-phosphate dehydrogenase; FAD-dependent sn-glycerol-3-phosphate dehydrogenase; FAD-GPDH; FAD-linked glycerol 3-phosphate dehydrogenase; FAD-linked L-glycerol-3-phosphate dehydrogenase; flavin-linked glycerol-3-phosphate dehydrogenase; flavoprotein-linked L-glycerol 3-phosphate dehydrogenase; glycerol 3-phosphate cytochrome c reductase (misleading); glycerol phosphate dehydrogenase; glycerol phosphate dehydrogenase (acceptor); glycerol phosphate dehydrogenase (FAD); glycerol-3-phosphate CoQ reductase; glycerol-3-phosphate dehydrogenase (flavin-linked); glycerol-3-phosphate:CoQ reductase; glycerophosphate dehydrogenase; L-3-glycerophosphate-ubiquinone oxidoreductase; L-glycerol-3-phosphate dehydrogenase (ambiguous); L-glycerophosphate dehydrogenase; mGPD; mitochondrial glycerol phosphate dehydrogenase; NAD+-independent glycerol phosphate dehydrogenase; pyridine nucleotide-independent L-glycerol 3-phosphate dehydrogenase; sn-glycerol 3-phosphate oxidase (misleading); sn-glycerol-3-phosphate dehydrogenase; sn-glycerol-3-phosphate:(acceptor) 2-oxidoreductase; sn-glycerol-3-phosphate:acceptor 2-oxidoreductase
Systematic name: sn-glycerol 3-phosphate:quinone oxidoreductase
Comments: This flavin-dependent dehydrogenase is an essential membrane enzyme, functioning at the central junction of glycolysis, respiration and phospholipid biosynthesis. In bacteria, the enzyme is localized to the cytoplasmic membrane [6], while in eukaryotes it is tightly bound to the outer surface of the inner mitochondrial membrane [2]. In eukaryotes, this enzyme, together with the cytosolic enzyme EC 1.1.1.8, glycerol-3-phosphate dehydrogenase (NAD+), forms the glycerol-3-phosphate shuttle by which NADH produced in the cytosol, primarily from glycolysis, can be reoxidized to NAD+ by the mitochondrial electron-transport chain [3]. This shuttle plays a critical role in transferring reducing equivalents from cytosolic NADH into the mitochondrial matrix [7,8]. Insect flight muscle uses only CoQ10 as the physiological quinone whereas hamster and rat mitochondria use mainly CoQ9 [4]. The enzyme is activated by calcium [3].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9001-49-4
References:
1. Ringler, R.L. Studies on the mitochondrial α-glycerophosphate dehydrogenase. II. Extraction and partial purification of the dehydrogenase from pig brain. J. Biol. Chem. 236 (1961) 1192-1198. [PMID: 13741763]
2. Schryvers, A., Lohmeier, E. and Weiner, J.H. Chemical and functional properties of the native and reconstituted forms of the membrane-bound, aerobic glycerol-3-phosphate dehydrogenase of Escherichia coli. J. Biol. Chem. 253 (1978) 783-788. [PMID: 340460]
3. MacDonald, M.J. and Brown, L.J. Calcium activation of mitochondrial glycerol phosphate dehydrogenase restudied. Arch. Biochem. Biophys. 326 (1996) 79-84. [PMID: 8579375]
4. Rauchová, H., Fato, R., Drahota, Z. and Lenaz, G. Steady-state kinetics of reduction of coenzyme Q analogs by glycerol-3-phosphate dehydrogenase in brown adipose tissue mitochondria. Arch. Biochem. Biophys. 344 (1997) 235-241. [PMID: 9244403]
5. Shen, W., Wei, Y., Dauk, M., Zheng, Z. and Zou, J. Identification of a mitochondrial glycerol-3-phosphate dehydrogenase from Arabidopsis thaliana: evidence for a mitochondrial glycerol-3-phosphate shuttle in plants. FEBS Lett. 536 (2003) 92-96. [PMID: 12586344]
6. Walz, A.C., Demel, R.A., de Kruijff, B. and Mutzel, R. Aerobic sn-glycerol-3-phosphate dehydrogenase from Escherichia coli binds to the cytoplasmic membrane through an amphipathic α-helix. Biochem. J. 365 (2002) 471-479. [PMID: 11955283]
7. Ansell, R., Granath, K., Hohmann, S., Thevelein, J.M. and Adler, L. The two isoenzymes for yeast NAD+-dependent glycerol 3-phosphate dehydrogenase encoded by GPD1 and GPD2 have distinct roles in osmoadaptation and redox regulation. EMBO J. 16 (1997) 2179-2187. [PMID: 9171333]
8. Larsson, C., Påhlman, I.L., Ansell, R., Rigoulet, M., Adler, L. and Gustafsson, L. The importance of the glycerol 3-phosphate shuttle during aerobic growth of Saccharomyces cerevisiae. Yeast 14 (1998) 347-357. [PMID: 9559543]
Accepted name: malate dehydrogenase (quinone)
Reaction: (S)-malate + a quinone = oxaloacetate + reduced quinone
Other name(s): FAD-dependent malate-vitamin K reductase; malate-vitamin K reductase; (S)-malate:(acceptor) oxidoreductase; L-malate-quinone oxidoreductase; malate:quinone oxidoreductase; malate quinone oxidoreductase; MQO; malate:quinone reductase; malate dehydrogenase (acceptor); FAD-dependent malate dehydrogenase
Systematic name: (S)-malate:quinone oxidoreductase
Comments: A flavoprotein (FAD). Vitamin K and several other quinones can act as acceptors. Different from EC 1.1.1.37 [malate dehydrogenase (NAD+)], EC 1.1.1.82 [malate dehydrogenase (NADP+)] and EC 1.1.1.299 [malate dehydrogenase [NAD(P)+)].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Imai, D. and Brodie, A.F. A phospholipid-requiring enzyme, malate-vitamin K reductase. J. Biol. Chem. 248 (1973) 7487-7494.
2. Imai, T. FAD-dependent malate dehydrogenase, a phospholipid-requiring enzyme from Mycobacterium sp. strain Takeo. Purification and some properties. Biochim. Biophys. Acta 523 (1978) 37-46. [PMID: 629992]
3. Reddy, T.L.P., Suryanarayana, P.M. and Venkitasubramanian, T.A. Variations in the pathways of malate oxidation and phosphorylation in different species of Mycobacteria. Biochim. Biophys. Acta 376 (1975) 210-218. [PMID: 234747]
4. Molenaar, D., van der Rest, M.E. and Petrovic, S. Biochemical and genetic characterization of the membrane-associated malate dehydrogenase (acceptor) from Corynebacterium glutamicum. Eur. J. Biochem. 254 (1998) 395-403. [PMID: 9660197]
5. Kather, B., Stingl, K., van der Rest, M.E., Altendorf, K. and Molenaar, D. Another unusual type of citric acid cycle enzyme in Helicobacter pylori: the malate:quinone oxidoreductase. J. Bacteriol. 182 (2000) 3204-3209. [PMID: 10809701]
Accepted name: alcohol dehydrogenase (quinone)
Reaction: ethanol + ubiquinone = acetaldehyde + ubiquinol
Other name(s): type III ADH; membrane associated quinohemoprotein alcohol dehydrogenase
Systematic name: alcohol:quinone oxidoreductase
Comments: Only described in acetic acid bacteria where it is involved in acetic acid production. Associated with membrane. Electron acceptor is membrane ubiquinone. A model structure suggests that, like all other quinoprotein alcohol dehydrogenases, the catalytic subunit has an 8-bladed 'propeller' structure, a calcium ion bound to the PQQ in the active site and an unusual disulfide ring structure in close proximity to the PQQ; the catalytic subunit also has a heme c in the C-terminal domain. The enzyme has two additional subunits, one of which contains three molecules of heme c. It does not require amines for activation. It has a restricted substrate specificity, oxidising a few primary alcohols (C2 to C6), but not methanol, secondary alcohols and some aldehydes. It is assayed with phenazine methosulfate or with ferricyanide.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Gomez-Manzo, S., Contreras-Zentella, M., Gonzalez-Valdez, A., Sosa-Torres, M., Arreguin-Espinoza, R. and Escamilla-Marvan, E. The PQQ-alcohol dehydrogenase of Gluconacetobacter diazotrophicus. Int. J. Food Microbiol. 125 (2008) 71-78. [PMID: 18321602]
2. Shinagawa, E., Toyama, H., Matsushita, K., Tuitemwong, P., Theeragool, G. and Adachi, O. A novel type of formaldehyde-oxidizing enzyme from the membrane of Acetobacter sp. SKU 14. Biosci. Biotechnol. Biochem. 70 (2006) 850-857. [PMID: 16636451]
3. Chinnawirotpisan, P., Theeragool, G., Limtong, S., Toyama, H., Adachi, O.O. and Matsushita, K. Quinoprotein alcohol dehydrogenase is involved in catabolic acetate production, while NAD-dependent alcohol dehydrogenase in ethanol assimilation in Acetobacter pasteurianus SKU1108. J. Biosci. Bioeng. 96 (2003) 564-571. [PMID: 16233574]
4. Frebortova, J., Matsushita, K., Arata, H. and Adachi, O. Intramolecular electron transport in quinoprotein alcohol dehydrogenase of Acetobacter methanolicus: a redox-titration stud. Biochim. Biophys. Acta 1363 (1998) 24-34. [PMID: 9526036]
5. Matsushita, K., Kobayashi, Y., Mizuguchi, M., Toyama, H., Adachi, O., Sakamoto, K. and Miyoshi, H. A tightly bound quinone functions in the ubiquinone reaction sites of quinoprotein alcohol dehydrogenase of an acetic acid bacterium, Gluconobacter suboxydans. Biosci. Biotechnol. Biochem. 72 (2008) 2723-2731. [PMID: 18838797]
6. Matsushita, K., Yakushi, T., Toyama, H., Shinagawa, E. and Adachi, O. Function of multiple heme c moieties in intramolecular electron transport and ubiquinone reduction in the quinohemoprotein alcohol dehydrogenase-cytochrome c complex of Gluconobacter suboxydans. J. Biol. Chem. 271 (1996) 4850-4857. [PMID: 8617755]
7. Matsushita, K., Takaki, Y., Shinagawa, E., Ameyama, M. and Adachi, O. Ethanol oxidase respiratory chain of acetic acid bacteria. Reactivity with ubiquinone of pyrroloquinoline quinone-dependent alcohol dehydrogenases purified from Acetobacter aceti and Gluconobacter suboxydans. Biosci. Biotechnol. Biochem. 56 (1992) 304-310.
8. Matsushita, K., Toyama, H. and Adachi, O. Respiratory chains and bioenergetics of acetic acid bacteria. Adv. Microb. Physiol. 36 (1994) 247-301. [PMID: 7942316]
9. Cozier, G.E., Giles, I.G. and Anthony, C. The structure of the quinoprotein alcohol dehydrogenase of Acetobacter aceti modelled on that of methanol dehydrogenase from Methylobacterium extorquens. Biochem. J. 308 (1995) 375-379. [PMID: 7772016]
[EC 1.1.5.6 Transferred entry: formate dehydrogenase-N. Now EC 1.17.5.3, formate dehydrogenase-N (EC 1.1.5.6 created 2010, deleted 2017)]
Accepted name: cyclic alcohol dehydrogenase (quinone)
Reaction: a cyclic alcohol + a quinone = a cyclic ketone + a quinol
Other name(s): cyclic alcohol dehydrogenase; MCAD
Systematic name: cyclic alcohol:quinone oxidoreductase
Comments: This enzyme oxidizes a wide variety of cyclic alcohols. Some minor enzyme activity is found with aliphatic secondary alcohols and sugar alcohols, but not primary alcohols. The enzyme is unable to catalyse the reverse reaction of cyclic ketones or aldehydes to cyclic alcohols. This enzyme differs from EC 1.1.5.5, alcohol dehydrogenase (quinone), which shows activity with ethanol [1].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Moonmangmee, D., Fujii, Y., Toyama, H., Theeragool, G., Lotong, N., Matsushita, K. and Adachi, O. Purification and characterization of membrane-bound quinoprotein cyclic alcohol dehydrogenase from Gluconobacter frateurii CHM 9. Biosci. Biotechnol. Biochem. 65 (2001) 2763-2772. [PMID: 11826975]
Accepted name: quinate/shikimate dehydrogenase (quinone)
Reaction: quinate + quinone = 3-dehydroquinate + quinol
For diagram of reaction click here
Glossary: quinate = (1R,3R,4R,5R)-1,3,4,5-tetrahydroxycyclohexanecarboxylic acid and is a cyclitol carboxylate
The numbering system used for the 3-dehydroquinate is that of the recommendations on cyclitols, sections I-8 and I-9: and is shown in the reaction diagram. The use of the term '5-dehydroquinate' for this compound is based on an earlier system of numbering.
Other name(s): NAD(P)+-independent quinate dehydrogenase; quinate:pyrroloquinoline-quinone 5-oxidoreductase; quinate dehydrogenase (quinone)
Systematic name: quinate:quinol 3-oxidoreductase
Comments: The enzyme is membrane-bound. Does not use NAD(P)+ as acceptor. Contains pyrroloquinoline-quinone. cf. EC 1.1.1.24, quinate/shikimate dehydrogenase (NAD+), EC 1.1.1.282, quinate/shikimate dehydrogenase [NAD(P)+], and EC 1.1.1.25, shikimate dehydrogenase (NADP+).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 115299-99-5
References:
1. van Kleef, M.A.G. and Duine, J.A. Bacterial NAD(P)-independent quinate dehydrogenase is a quinoprotein. Arch. Microbiol. 150 (1988) 32-36. [PMID: 3044290]
2. Adachi, O., Tanasupawat, S., Yoshihara, N., Toyama, H. and Matsushita, K. 3-Dehydroquinate production by oxidative fermentation and further conversion of 3-dehydroquinate to the intermediates in the shikimate pathway. Biosci. Biotechnol. Biochem. 67 (2003) 2124-2131. [PMID: 14586099]
3. Vangnai, A.S., Toyama, H., De-Eknamkul, W., Yoshihara, N., Adachi, O. and Matsushita, K. Quinate oxidation in Gluconobacter oxydans IFO3244: purification and characterization of quinoprotein quinate dehydrogenase. FEMS Microbiol. Lett. 241 (2004) 157-162. [PMID: 15598527]
Accepted name: glucose 1-dehydrogenase (FAD, quinone)
Reaction: D-glucose + a quinone = D-glucono-1,5-lactone + a quinol
Other name(s): glucose dehydrogenase (Aspergillus); FAD-dependent glucose dehydrogenase; D-glucose:(acceptor) 1-oxidoreductase; glucose dehydrogenase (acceptor); gdh (gene name)
Systematic name: D-glucose:quinone 1-oxidoreductase
Comments: A glycoprotein containing one mole of FAD per mole of enzyme. 2,6-Dichloroindophenol can act as acceptor. cf. EC 1.1.5.2, quinoprotein glucose dehydrogenase.
Links to other databases: BRENDA, EXPASY, KEGG Metacyc, PDB, CAS registry number:
References:
1. Bak, T.-G. Studies on glucose dehydrogenase of Aspergillus oryzae. II. Purification and physical and chemical properties. Biochim. Biophys. Acta 139 (1967) 277-293. [PMID: 6034674]
2. Cavener, D.R. and MacIntyre, R.J. Biphasic expression and function of glucose dehydrogenase in Drosophila melanogaster. Proc. Natl. Acad. Sci. USA 80 (1983) 6286-6288. [PMID: 6413974]
3. Lovallo, N. and Cox-Foster, D.L. Alteration in FAD-glucose dehydrogenase activity and hemocyte behavior contribute to initial disruption of Manduca sexta immune response to Cotesia congregata parasitoids. J Insect Physiol 45 (1999) 1037-1048. [PMID: 12770264]
4. Inose, K., Fujikawa, M., Yamazaki, T., Kojima, K. and Sode, K. Cloning and expression of the gene encoding catalytic subunit of thermostable glucose dehydrogenase from Burkholderia cepacia in Escherichia coli. Biochim. Biophys. Acta 1645 (2003) 133-138. [PMID: 12573242]
5. Sygmund, C., Klausberger, M., Felice, A.K. and Ludwig, R. Reduction of quinones and phenoxy radicals by extracellular glucose dehydrogenase from Glomerella cingulata suggests a role in plant pathogenicity. Microbiology 157 (2011) 3203-3212. [PMID: 21903757]
6. Sygmund, C., Staudigl, P., Klausberger, M., Pinotsis, N., Djinovic-Carugo, K., Gorton, L., Haltrich, D. and Ludwig, R. Heterologous overexpression of Glomerella cingulata FAD-dependent glucose dehydrogenase in Escherichia coli and Pichia pastoris. Microb. Cell Fact. 10 (2011) 106. [PMID: 22151971]
Accepted name: D-2-hydroxyacid dehydrogenase (quinone)
Reaction: (R)-2-hydroxyacid + a quinone = 2-oxoacid + a quinol
Other name(s): (R)-2-hydroxy acid dehydrogenase; (R)-2-hydroxy-acid:(acceptor) 2-oxidoreductase; D-lactate dehydrogenase (ambiguous)
Systematic name: (R)-2-hydroxyacid:quinone oxidoreductase
Comments: The enzyme from mammalian kidney contains one mole of FAD per mole of enzyme.(R)-lactate, (R)-malate and meso-tartrate are good substrates. Ubiquinone-1 and the dye 2,6-dichloroindophenol can act as acceptors; NAD+ and NADP+ are not acceptors.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Tubbs, P.K. and Greville, G.D. Dehydrogenation of D-lactate by a soluble enzyme from kidney mitochondria. Biochim. Biophys. Acta 34 (1959) 290-291. [PMID: 13839714]
2. Tubbs, P.K. and Greville, G.D. The oxidation of D-α-hydroxy acids in animal tissues. Biochem. J. 81 (1961) 104-114. [PMID: 13922962]
3. Cammack, R. Assay, purification and properties of mammalian D-2-hydroxy acid dehydrogenase. Biochem. J. 115 (1969) 55-64. [PMID: 5359443]
4. Cammack, R. D-2-hydroxy acid dehydrogenase from animal tissue. Methods Enzymol. 41 (1975) 323-329. [PMID: 236454]
Accepted name: 1-butanol dehydrogenase (quinone)
Reaction: butan-1-ol + a quinone = butanal + a quinol
Other name(s): BOH
Systematic name: butan-1-ol:quinone oxidoreductase
Comments: This periplasmic quinoprotein alcohol dehydrogenase, characterized from the bacterium Thauera butanivorans, is involved in butane degradation. It contains a pyrroloquinoline quinone (PQQ) prosthetic group. cf. EC 1.1.2.9, 1-butanol dehydrogenase (cytochrome c).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Vangnai, A.S., Arp, D.J. and Sayavedra-Soto, L.A. Two distinct alcohol dehydrogenases participate in butane metabolism by Pseudomonas butanovora. J. Bacteriol. 184 (2002) 1916-1924. [PMID: 11889098]
2. Vangnai, A.S., Sayavedra-Soto, L.A. and Arp, D.J. Roles for the two 1-butanol dehydrogenases of Pseudomonas butanovora in butane and 1-butanol metabolism. J. Bacteriol. 184 (2002) 4343-4350. [PMID: 12142403]
Accepted name: D-lactate dehydrogenase (quinone)
Reaction: (R)-lactate + a quinone = pyruvate + a quinol
Other name(s): dld (gene name)
Systematic name: (R)-lactate:quinone 2-oxidoreductase
Comments: The enzyme is an FAD-dependent peripheral membrane dehydrogenase that participates in respiration. Electrons derived from D-lactate oxidation are transferred to the membrane soluble quinone pool.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Kohn, L.D. and Kaback, H.R. Mechanisms of active transport in isolated bacterial membrane vesicles. XV. Purification and properties of the membrane-bound D-lactate dehydrogenase from Escherichia coli. J. Biol. Chem. 248 (1973) 7012-7017. [PMID: 4582730]
2. Futai, M. Membrane D-lactate dehydrogenase from Escherichia coli. Purification and properties. Biochemistry 12 (1973) 2468-2474. [PMID: 4575624]
3. Matsushita, K. and Kaback, H.R. D-Lactate oxidation and generation of the proton electrochemical gradient in membrane vesicles from Escherichia coli GR19N and in proteoliposomes reconstituted with purified D-lactate dehydrogenase and cytochrome o oxidase. Biochemistry 25 (1986) 2321-2327. [PMID: 3013300]
4. Peersen, O.B., Pratt, E.A., Truong, H.T., Ho, C. and Rule, G.S. Site-specific incorporation of 5-fluorotryptophan as a probe of the structure and function of the membrane-bound D-lactate dehydrogenase of Escherichia coli: a 19F nuclear magnetic resonance study. Biochemistry 29 (1990) 3256-3262. [PMID: 2185834]
5. Dym, O., Pratt, E.A., Ho, C. and Eisenberg, D. The crystal structure of D-lactate dehydrogenase, a peripheral membrane respiratory enzyme. Proc. Natl. Acad. Sci. USA 97 (2000) 9413-9418. [PMID: 10944213]
Accepted name: (S)-2-hydroxyglutarate dehydrogenase
Reaction: (S)-2-hydroxyglutarate + a quinone = 2-oxoglutarate + a quinol
Other name(s): L-2-hydroxyglutarate dehydrogenase; lhgO (gene name); ygaF (gene name)
Systematic name: (S)-2-hydroxyglutarate:quinone oxidoreductase
Comments: The enzyme, characterized from the bacterium Escherichia coli, contains an FAD cofactor that is not covalently attached. It is bound to the cytoplasmic membrane and is coupled to the membrane quinone pool.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Kalliri, E., Mulrooney, S.B. and Hausinger, R.P. Identification of Escherichia coli YgaF as an L-2-hydroxyglutarate oxidase. J. Bacteriol. 190 (2008) 3793-3798. [PMID: 18390652]
2. Knorr, S., Sinn, M., Galetskiy, D., Williams, R.M., Wang, C., Muller, N., Mayans, O., Schleheck, D. and Hartig, J.S. Widespread bacterial lysine degradation proceeding via glutarate and L-2-hydroxyglutarate. Nat. Commun. 9 (2018) 5071. [PMID: 30498244]
Accepted name: fructose 5-dehydrogenase
Reaction: D-fructose + a ubiquinone = 5-dehydro-D-fructose + a ubiquinol
Other name(s): fructose 5-dehydrogenase (acceptor); D-fructose dehydrogenase; D-fructose:(acceptor) 5-oxidoreductase
Systematic name: D-fructose:ubiquinone 5-oxidoreductase
Comments: The enzyme, characterized from the bacterium Gluconobacter japonicus, is a heterotrimer composed of an FAD-containing large subunit, a small subunit, and a heme c-containing subunit, which is responsible for anchoring the complex to the cytoplasmic membrane and for transferring the electrons to ubiquinone.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Yamada, Y., Aida, K. and Uemura, T. Enzymatic studies on the oxidation of sugar and sugar alcohol. I. Purification and properties of particle-bound fructose dehydrogenase. J. Biochem. (Tokyo) 61 (1967) 636-646. [PMID: 6059959]
2. Ameyama, M. and Adachi, O. D-Fructose dehydrogenase from Gluconobacter industrius, membrane-bound. Methods Enzymol. 89 (1982) 154-159.
3. Nakashima, K., Takei, H., Adachi, O., Shinagawa, E. and Ameyama, M. Determination of seminal fructose using D-fructose dehydrogenase. Clin. Chim. Acta 151 (1985) 307-310. [PMID: 4053391]
4. Kawai, S., Goda-Tsutsumi, M., Yakushi, T., Kano, K. and Matsushita, K. Heterologous overexpression and characterization of a flavoprotein-cytochrome c complex fructose dehydrogenase of Gluconobacter japonicus NBRC3260. Appl. Environ. Microbiol. 79 (2013) 1654-1660. [PMID: 23275508]
Accepted name: 4-hydroxybenzoyl-CoA reductase
Reaction: benzoyl-CoA + oxidized ferredoxin + H2O = 4-hydroxybenzoyl-CoA + reduced ferredoxin
Other name(s): 4-hydroxybenzoyl-CoA reductase (dehydroxylating); 4-hydroxybenzoyl-CoA:(acceptor) oxidoreductase; benzoyl-CoA:acceptor oxidoreductase
Systematic name: benzoyl-CoA:oxidized ferredoxin oxidoreductase
Comments: A molybdenum-flavin-iron-sulfur protein that is involved in the anaerobic pathway of phenol metabolism in bacteria. A ferredoxin with two [4Fe-4S] clusters functions as the natural electron donor [3].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Glockler, R., Tschech, A. and Fuchs, G. Reductive dehydroxylation of 4-hydroxybenzoyl-CoA to benzoyl-CoA in a denitrifying, phenol-degrading Pseudomonas species. FEBS Lett. 251 (1989) 237-240. [PMID: 2753161]
2. Heider, J., Boll, M., Breese, K., Breinig, S., Ebenau-Jehle, C., Feil, U., Gad'on, N., Laempe, D., Leuthner, B., Mohamed, M.E.S., Schneider, S., Burchhardt, G. and Fuchs, G. Differential induction of enzymes involved in anaerobic metabolism of aromatic compounds in the denitrifying bacterium Thauera aromatica. Arch. Microbiol. 170 (1998) 120-131. [PMID: 9683649]
3. Breese, K. and Fuchs, G. 4-Hydroxybenzoyl-CoA reductase (dehydroxylating) from the denitrifying bacterium Thauera aromatica - prosthetic groups, electron donor, and genes of a member of the molybdenum-flavin-iron-sulfur proteins. Eur. J. Biochem. 251 (1998) 916-923. [PMID: 9490068]
4. Brackmann, R. and Fuchs, G. Enzymes of anaerobic metabolism of phenolic compounds. 4-Hydroxybenzoyl-CoA reductase (dehydroxylating) from a denitrifying Pseudomonas species. Eur. J. Biochem. 213 (1993) 563-571. [PMID: 8477729]
5. Heider, J. and Fuchs, G. Anaerobic metabolism of aromatic compounds. Eur. J. Biochem. 243 (1997) 577-596. [PMID: 9057820]
Accepted name: alcohol dehydrogenase (azurin)
Reaction: a primary alcohol + azurin = an aldehyde + reduced azurin
Other name(s): type II quinoprotein alcohol dehydrogenase; quinohaemoprotein ethanol dehydrogenase; QHEDH; ADHIIB
Systematic name: alcohol:azurin oxidoreductase
Comments: A soluble, periplasmic PQQ-containing quinohaemoprotein. Also contains a single haem c. Occurs in Comamonas and Pseudomonas. Does not require an amine activator. Oxidizes a wide range of primary and secondary alcohols, and also aldehydes and large substrates such as sterols; methanol is not a substrate. Usually assayed with phenazine methosulfate or ferricyanide. Like all other quinoprotein alcohol dehydrogenases it has an 8-bladed 'propeller' structure, a calcium ion bound to the PQQ in the active site and an unusual disulfide ring structure in close proximity to the PQQ.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Groen, B.W., van Kleef, M.A. and Duine, J.A. Quinohaemoprotein alcohol dehydrogenase apoenzyme from Pseudomonas testosteroni. Biochem. J. 234 (1986) 611-615. [PMID: 3521592]
2. de Jong, G.A., Caldeira, J., Sun, J., Jongejan, J.A., de Vries, S., Loehr, T.M., Moura, I., Moura, J.J. and Duine, J.A. Characterization of the interaction between PQQ and heme c in the quinohemoprotein ethanol dehydrogenase from Comamonas testosteroni. Biochemistry 34 (1995) 9451-9458. [PMID: 7626615]
3. Toyama, H., Fujii, A., Matsushita, K., Shinagawa, E., Ameyama, M. and Adachi, O. Three distinct quinoprotein alcohol dehydrogenases are expressed when Pseudomonas putida is grown on different alcohols. J. Bacteriol. 177 (1995) 2442-2450. [PMID: 7730276]
4. Matsushita, K., Yamashita, T., Aoki, N., Toyama, H. and Adachi, O. Electron transfer from quinohemoprotein alcohol dehydrogenase to blue copper protein azurin in the alcohol oxidase respiratory chain of Pseudomonas putida HK5. Biochemistry 38 (1999) 6111-6118. [PMID: 10320337]
5. Chen, Z.W., Matsushita, K., Yamashita, T., Fujii, T.A., Toyama, H., Adachi, O., Bellamy, H.D. and Mathews, F.S. Structure at 1.9 Å resolution of a quinohemoprotein alcohol dehydrogenase from Pseudomonas putida HK5. Structure 10 (2002) 837-849. [PMID: 12057198]
6. Oubrie, A., Rozeboom, H.J., Kalk, K.H., Huizinga, E.G. and Dijkstra, B.W. Crystal structure of quinohemoprotein alcohol dehydrogenase from Comamonas testosteroni: structural basis for substrate oxidation and electron transfer. J. Biol. Chem. 277 (2002) 3727-3732. [PMID: 11714714]
Accepted name: glucose-6-phosphate dehydrogenase (coenzyme-F420)
Reaction: D-glucose 6-phosphate + oxidized coenzyme F420 = 6-phospho-D-glucono-1,5-lactone + reduced coenzyme F420
Glossary: coenzyme F420
Other name(s): coenzyme F420-dependent glucose-6-phosphate dehydrogenase; F420-dependent glucose-6-phosphate dehydrogenase; FGD1; Rv0407; F420-dependent glucose-6-phosphate dehydrogenase 1
Systematic name: D-glucose-6-phosphate:F420 1-oxidoreductase
Comments: The enzyme is very specific for D-glucose 6-phosphate. No activity with NAD+, NADP+, flavin adenine dinucleotide and flavin mononucleotide [1].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Purwantini, E. and Daniels, L. Purification of a novel coenzyme F420-dependent glucose-6-phosphate dehydrogenase from Mycobacterium smegmatis. J. Bacteriol. 178 (1996) 2861-2866. [PMID: 8631674]
2. Bashiri, G., Squire, C.J., Baker, E.N. and Moreland, N.J. Expression, purification and crystallization of native and selenomethionine labeled Mycobacterium tuberculosis FGD1 (Rv0407) using a Mycobacterium smegmatis expression system. Protein Expr. Purif. 54 (2007) 38-44. [PMID: 17376702]
3. Purwantini, E., Gillis, T.P. and Daniels, L. Presence of F420-dependent glucose-6-phosphate dehydrogenase in Mycobacterium and Nocardia species, but absence from Streptomyces and Corynebacterium species and methanogenic Archaea. FEMS Microbiol. Lett. 146 (1997) 129-134. [PMID: 8997717]
Accepted name: decaprenylphospho-β-D-ribofuranose 2-dehydrogenase
Reaction: trans,octacis-decaprenylphospho-β-D-ribofuranose + FAD = trans,octacis-decaprenylphospho-β-D-erythro-pentofuranosid-2-ulose + FADH2
For diagram of reaction click here.
Other name(s): decaprenylphosphoryl-β-D-ribofuranose 2'-epimerase; Rv3790; DprE1; decaprenylphospho-β-D-ribofuranose 2-oxidase
Systematic name: trans,octacis-decaprenylphospho-β-D-ribofuranose:FAD 2-oxidoreductase
Comments: The enzyme, isolated from the bacterium Mycobacterium smegmatis, is involved, along with EC 1.1.1.333, decaprenylphospho-D-erythro-pentofuranosid-2-ulose 2-reductase, in the epimerization of trans,octacis-decaprenylphospho-β-D-ribofuranose to trans,octacis-decaprenylphospho-β-D-arabinofuranose, the arabinosyl donor for the biosynthesis of mycobacterial cell wall arabinan polymers.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Ribeiro, A.L., Degiacomi, G., Ewann, F., Buroni, S., Incandela, M.L., Chiarelli, L.R., Mori, G., Kim, J., Contreras-Dominguez, M., Park, Y.S., Han, S.J., Brodin, P., Valentini, G., Rizzi, M., Riccardi, G. and Pasca, M.R. Analogous mechanisms of resistance to benzothiazinones and dinitrobenzamides in Mycobacterium smegmatis. PLoS One 6 (2011) e26675. [PMID: 22069462]
2. Trefzer, C., Škovierová, H., Buroni, S., Bobovská, A., Nenci, S., Molteni, E., Pojer, F., Pasca, M.R., Makarov, V., Cole, S.T., Riccardi, G., Mikušová, K. and Johnsson, K. Benzothiazinones are suicide inhibitors of mycobacterial decaprenylphosphoryl-β-D-ribofuranose 2'-oxidase DprE1. J. Am. Chem. Soc. 134 (2012) 912-915. [PMID: 22188377]
Accepted name: F420H2:quinone oxidoreductase
Reaction: a quinol + oxidized coenzyme F420 = a quinone + reduced coenzyme F420
Other name(s): FqoF protein
Systematic name: quinol:coenzyme-F420 oxidoreductase
Comments: An enzyme complex that contains FAD and iron-sulfur clusters. The enzyme has been described in the archaea Methanosarcina mazei and Archaeoglobus fulgidus.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Bruggemann, H., Falinski, F. and Deppenmeier, U. Structure of the F420H2:quinone oxidoreductase of Archaeoglobus fulgidus identification and overproduction of the F420H2-oxidizing subunit. Eur. J. Biochem. 267 (2000) 5810-5814. [PMID: 10971593]
2. Kunow, J., Linder, D., Stetter, K.O. and Thauer, R.K. F420H2: quinone oxidoreductase from Archaeoglobus fulgidus. Characterization of a membrane-bound multisubunit complex containing FAD and iron-sulfur clusters. Eur. J. Biochem. 223 (1994) 503-511. [PMID: 8055920]
3. Abken, H.-J. and Deppenmeier, U. Purification and properties of an F420H2 dehydrogenase from Methanosarcina mazei Gö1. FEMS Microbiol. Lett. 154 (1997) 231-237.
Accepted name: secondary-alcohol dehydrogenase (coenzyme-F420)
Reaction: R-CHOH-R′ + oxidized coenzyme F420 = R-CO-R′ + reduced coenzyme F420
Glossary: oxidized coenzyme F420 = N-(N-{O-[5-(8-hydroxy-2,4-dioxo-2,3,4,10-tetrahydropyrimido[4,5-b]quinolin-10-yl)-5-deoxy-L-ribityl-1-phospho]-(S)-lactyl}-γ-L-glutamyl)-L-glutamate
Other name(s): F420-dependent alcohol dehydrogenase; secondary alcohol:F420 oxidoreductase; F420-dependent secondary alcohol dehydrogenase
Systematic name: secondary-alcohol:coenzyme F420 oxidoreductase
Comments: The enzyme isolated from the methanogenic archaea Methanogenium liminatans catalyses the reversible oxidation of various secondary and cyclic alcohols to the corresponding ketones.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Bleicher, K. and Winter, J. Purification and properties of F420- and NADP(+)-dependent alcohol dehydrogenases of Methanogenium liminatans and Methanobacterium palustre, specific for secondary alcohols. Eur. J. Biochem. 200 (1991) 43-51. [PMID: 1879431]
2. Aufhammer, S.W., Warkentin, E., Berk, H., Shima, S., Thauer, R.K. and Ermler, U. Coenzyme binding in F420-dependent secondary alcohol dehydrogenase, a member of the bacterial luciferase family. Structure 12 (2004) 361-370. [PMID: 15016352]
Accepted name: ribonucleoside-triphosphate reductase (formate)
Reaction: ribonucleoside 5'-triphosphate + formate = 2'-deoxyribonucleoside 5'-triphosphate + CO2 + H2O
Other name(s): nrdD (gene name); class III ribonucleoside-triphosphate reductase; anaerobic ribonucleotide reductase; anaerobic ribonucleoside-triphosphate reductase
Systematic name: ribonucleoside-5'-triphosphate:formate 2'-oxidoreductase
Comments: The enzyme, which is expressed in the bacterium Escherichia coli during anaerobic growth, contains an iron sulfur center. The active form of the enzyme contains an oxygen-sensitive glycyl radical that is generated by the activating enzyme NrdG via chemistry involving S-adenosylmethionine (SAM) and a [4Fe-4S] cluster. The glycyl radical is involved in generation of a transient thiyl radical on a cysteine residue, which attacks the substrate, forming a ribonucleotide 3'-radical, followed by water loss to form a ketyl radical. The ketyl radical gains an electron from a cysteine residue and a proton from formic acid, forming 3'-keto-deoxyribonucleotide and generating a thiosulfuranyl radical bridge between methionine and cysteine residues. Oxidation of formate by the thiosulfuranyl radical results in the release of CO2 and regeneration of the thiyl radical. cf. EC 1.17.4.1, ribonucleoside-diphosphate reductase and EC 1.17.4.2, ribonucleoside-triphosphate reductase (thioredoxin).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Eliasson, R., Pontis, E., Fontecave, M., Gerez, C., Harder, J., Jornvall, H., Krook, M. and Reichard, P. Characterization of components of the anaerobic ribonucleotide reductase system from Escherichia coli. J. Biol. Chem. 267 (1992) 25541-25547. [PMID: 1460049]
2. Mulliez, E., Fontecave, M., Gaillard, J. and Reichard, P. An iron-sulfur center and a free radical in the active anaerobic ribonucleotide reductase of Escherichia coli. J. Biol. Chem. 268 (1993) 2296-2299. [PMID: 8381402]
3. Mulliez, E., Ollagnier, S., Fontecave, M., Eliasson, R. and Reichard, P. Formate is the hydrogen donor for the anaerobic ribonucleotide reductase from Escherichia coli. Proc. Natl. Acad. Sci. USA 92 (1995) 8759-8762. [PMID: 7568012]
4. Ollagnier, S., Mulliez, E., Schmidt, P.P., Eliasson, R., Gaillard, J., Deronzier, C., Bergman, T., Graslund, A., Reichard, P. and Fontecave, M. Activation of the anaerobic ribonucleotide reductase from Escherichia coli. The essential role of the iron-sulfur center for S-adenosylmethionine reduction. J. Biol. Chem. 272 (1997) 24216-24223. [PMID: 9305874]
5. Wei, Y., Mathies, G., Yokoyama, K., Chen, J., Griffin, R.G. and Stubbe, J. A chemically competent thiosulfuranyl radical on the Escherichia coli class III ribonucleotide reductase. J. Am. Chem. Soc. 136 (2014) 9001-9013. [PMID: 24827372]
Accepted name: serine-type anaerobic sulfatase-maturating enzyme
Reaction: S-adenosyl-L-methionine + a [sulfatase]-L-serine = a [sulfatase]-3-oxo-L-alanine + 5'-deoxyadenosine + L-methionine
Glossary: 3-oxo-L-alanine = (S)-formylglycine = (S)-Cα-formylglycine = FGly
Other name(s): atsB (gene name)
Systematic name: [sulfatase]-L-serine:S-adenosyl-L-methionine oxidoreductase (3-oxo-L-alanine-forming)
Comments: A bacterial radical S-adenosyl-L-methionine (AdoMet) enzyme that contains three [4Fe-4S] clusters. The enzyme, found in some bacteria, activates a type I sulfatase enzyme (EC 3.1.6.1) by converting a conserved L-serine residue in the active site to a unique 3-oxo-L-alanine residue that is essential for the sulfatase activity. While the enzyme from Klebsiella pneumoniae is specific for L-serine, the enzyme from Clostridium perfringens can also act on L-cysteine, see EC 1.8.98.7, cysteine-type anaerobic sulfatase-maturating enzyme.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Szameit, C., Miech, C., Balleininger, M., Schmidt, B., von Figura, K. and Dierks, T. The iron sulfur protein AtsB is required for posttranslational formation of formylglycine in the Klebsiella sulfatase. J. Biol. Chem. 274 (1999) 15375-15381. [PMID: 10336424]
2. Fang, Q., Peng, J. and Dierks, T. Post-translational formylglycine modification of bacterial sulfatases by the radical S-adenosylmethionine protein AtsB. J. Biol. Chem. 279 (2004) 14570-14578. [PMID: 14749327]
3. Grove, T.L., Lee, K.H., St Clair, J., Krebs, C. and Booker, S.J. In vitro characterization of AtsB, a radical SAM formylglycine-generating enzyme that contains three [4Fe-4S] clusters. Biochemistry 47 (2008) 7523-7538. [PMID: 18558715]
Accepted name: choline dehydrogenase
Reaction: choline + acceptor = betaine aldehyde + reduced acceptor
Glossary: betaine aldehyde = N,N,N-trimethyl-2-oxoethylammonium
choline = (2-hydroxyethyl)trimethylammonium
Other name(s): choline oxidase; choline-cytochrome c reductase; choline:(acceptor) oxidoreductase; choline:(acceptor) 1-oxidoreductase
Systematic name: choline:acceptor 1-oxidoreductase
Comments: A quinoprotein. In many bacteria, plants and animals, the osmoprotectant betaine is synthesized using different enzymes to catalyse the conversion of (1) choline into betaine aldehyde and (2) betaine aldehyde into betaine. In plants, the first reaction is catalysed by EC 1.14.15.7, choline monooxygenase, whereas in animals and many bacteria, it is catalysed by either membrane-bound choline dehydrogenase (EC 1.1.99.1) or soluble choline oxidase (EC 1.1.3.17) [4]. The enzyme involved in the second step, EC 1.2.1.8, betaine-aldehyde dehydrogenase, appears to be the same in plants, animals and bacteria.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9028-67-5
References:
1. Ameyama, M., Shinagawa, E., Matsuchita, K., Takimoto, K., Nakashima, K. and Adachi, O. Mammalian choline dehydrogenase is a quinoprotein. Agric. Biol. Chem. 49 (1985) 3623-3626.
2. Ebisuzaki, K. and Williams, J.N. Preparation and partial purification of soluble choline dehydrogenase from liver mitochondria. Biochem. J. 60 (1955) 644-646. [PMID: 13249959]
3. Gadda, G. and McAllister-Wilkins, E.E. Cloning, expression, and purification of choline dehydrogenase from the moderate halophile Halomonas elongata. Appl. Environ. Microbiol. 69 (2003) 2126-2132. [PMID: 12676692]
4. Waditee, R., Tanaka, Y., Aoki, K., Hibino, T., Jikuya, H., Takano, J., Takabe, T. and Takabe, T. Isolation and functional characterization of N-methyltransferases that catalyze betaine synthesis from glycine in a halotolerant photosynthetic organism Aphanothece halophytica. J. Biol. Chem. 278 (2003) 4932-4942. [PMID: 12466265]
Accepted name: L-2-hydroxyglutarate dehydrogenase
Reaction: (S)-2-hydroxyglutarate + acceptor = 2-oxoglutarate + reduced acceptor
Other name(s): α-ketoglutarate reductase; α-hydroxyglutarate dehydrogenase; L-α-hydroxyglutarate dehydrogenase; hydroxyglutaric dehydrogenase; α-hydroxyglutarate oxidoreductase; L-α-hydroxyglutarate:NAD+ 2-oxidoreductase; α-hydroxyglutarate dehydrogenase (NAD+ specific); (S)-2-hydroxyglutarate:(acceptor) 2-oxidoreductase
Systematic name: (S)-2-hydroxyglutarate:acceptor 2-oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9028-80-2
References:
1. Weil-Malherbe, H. The oxidation of l(-)α-hydroxyglutaric acid in animal tissues. Biochem. J. 31 (1937) 2080-2094. [PMID: 16746551]
Accepted name: gluconate 2-dehydrogenase (acceptor)
Reaction: D-gluconate + acceptor = 2-dehydro-D-gluconate + reduced acceptor
Other name(s): gluconate oxidase; gluconate dehydrogenase; gluconic dehydrogenase; D-gluconate dehydrogenase; gluconic acid dehydrogenase; 2-ketogluconate reductase; D-gluconate dehydrogenase, 2-keto-D-gluconate-yielding; D-gluconate:(acceptor) 2-oxidoreductase
Systematic name: D-gluconate:acceptor 2-oxidoreductase
Comments: A flavoprotein (FAD).
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, CAS registry number: 9028-81-3
References:
1. Matsushita, K., Shinagawa, E. and Ameyama, M. D-Gluconate dehydrogenases from bacteria, 2-keto-D-gluconate-yielding membrane-bound. Methods Enzymol. 89 (1982) 187-193.
2. Ramakrishnan, T. and Campbell, J.J.R. Gluconic dehydrogenase of Pseudomonas aeruginosa. Biochim. Biophys. Acta 17 (1955) 122-127.
Accepted name: dehydrogluconate dehydrogenase
Reaction: 2-dehydro-D-gluconate + acceptor = 2,5-didehydro-D-gluconate + reduced acceptor
Other name(s): ketogluconate dehydrogenase; α-ketogluconate dehydrogenase; 2-keto-D-gluconate dehydrogenase; 2-oxogluconate dehydrogenase
Systematic name: 2-dehydro-D-gluconate:acceptor 2-oxidoreductase
Comments: A flavoprotein.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9028-82-4
References:
1. Datta, A.G. and Katznelson, H. The oxidation of 2-ketogluconate by a partially purified enzyme from Acetobacter melanogenum. Arch. Biochem. Biophys. 65 (1956) 576-578.
2. Shinagawa, E. and Ameyama, M. 2-Keto-D-gluconate dehydrogenase from Gluconobacter melanogenus, membrane-bound. Methods Enzymol. 89 (1982) 194-198.
[EC 1.1.99.5 Transferred entry: glycerol-3-phosphate dehydrogenase. As the acceptor is now known, the enzyme has been transferred to EC 1.1.5.3, glycerol-3-phosphate dehydrogenase. (EC 1.1.99.5 created 1961 as EC 1.1.2.1, transferred 1965 to EC 1.1.99.5, deleted 2009)]
Accepted name: D-lactate dehydrogenase (acceptor)
Reaction: (R)-lactate + acceptor = pyruvate + reduced acceptor
Other name(s): D-2-hydroxy acid dehydrogenase; D-2-hydroxy-acid dehydrogenase; (R)-2-hydroxy-acid:acceptor 2-oxidoreductase
Systematic name: (R)-lactate:acceptor 2-oxidoreductase
Comments: The zinc flavoprotein (FAD) from the archaeon Archaeoglobus fulgidus cannot utilize NAD+, cytochrome c, methylene blue or dimethylnaphthoquinone as acceptors. In vitro it is active with artificial electron acceptors such as 2,6-dichlorophenolindophenol, but the physiological acceptor is not yet known.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9028-83-5
References:
1. Reed, D.W. and Hartzell, P.L. The Archaeoglobus fulgidus D-lactate dehydrogenase is a Zn2+ flavoprotein. J. Bacteriol. 181 (1999) 7580-7587. [PMID: 10601217]
Accepted name: lactate—malate transhydrogenase
Reaction: (S)-lactate + oxaloacetate = pyruvate + malate
Other name(s): malate-lactate transhydrogenase
Systematic name: (S)-lactate:oxaloacetate oxidoreductase
Comments: Catalyses hydrogen transfer from C3 or C4 (S)-2-hydroxy acids to 2-oxo acids. It contains tightly bound nicotinamide nucleotide in its active centre. This prosthetic group cannot be removed without denaturation of the protein.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, CAS registry number: 9077-15-0
References:
1. Allen, S.H.G. The isolation and characterization of malate-lactate transhydrogenase from Micrococcus lactilyticus. J. Biol. Chem. 241 (1966) 5266-5275. [PMID: 4289051]
2. Allen, S.H.G. and Patil, J.R. Studies on the structure and mechanism of action of the malate-lactate transhydrogenase. J. Biol. Chem. 247 (1972) 909-916. [PMID: 4333516]
[EC 1.1.99.8 Transferred entry: alcohol dehydrogenase (acceptor). Now EC 1.1.2.7, methanol dehydrogenase (cytochrome c) and EC 1.1.2.8, alcohol dehydrogenase (cytochrome c). (EC 1.1.99.8 created 1972, modified 1982, deleted 2010)]
Accepted name: pyridoxine 5-dehydrogenase
Reaction: pyridoxine + acceptor = isopyridoxal + reduced acceptor
Other name(s): pyridoxal-5-dehydrogenase; pyridoxol 5-dehydrogenase; pyridoxin 5-dehydrogenase; pyridoxine dehydrogenase; pyridoxine 5'-dehydrogenase; pyridoxine:(acceptor) 5-oxidoreductase
Systematic name: pyridoxine:acceptor 5-oxidoreductase
Comments: A flavoprotein (FAD).
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, CAS registry number: 9023-39-6
References:
1. Sundaram, T.K. and Snell, E.E. The bacterial oxidation of vitamin B6. V. The enzymatic formation of pyridoxal and isopyridoxal from pyridoxine. J. Biol. Chem. 244 (1969) 2577-2584. [PMID: 5769992]
[EC 1.1.99.10 Transferred entry: glucose dehydrogenase (acceptor), now classified as EC 1.1.5.9, glucose 1-dehydrogenase (FAD, quinone) (EC 1.1.99.10 created 1972, modified 1976, deleted 2013)]
[EC 1.1.99.11 Transferred entry: fructose 5-dehydrogenase, now classified as EC 1.1.5.14, fructose 5-dehydrogenase. (EC 1.1.99.11 created 1972, deleted 2021.)]
Accepted name: sorbose dehydrogenase
Reaction: L-sorbose + acceptor = 5-dehydro-D-fructose + reduced acceptor
Other name(s): L-sorbose:(acceptor) 5-oxidoreductase
Systematic name: L-sorbose:acceptor 5-oxidoreductase
Comments: 2,6-Dichloroindophenol can act as acceptor.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37250-86-5
References:
1. Sato, K., Yamada, Y., Aida, K. and Uemara, T. Enzymatic studies on the oxidation of sugar and sugar alcohol. 8. Particle-bound L-sorbose dehydrogenase from Gluconobacter suboxydans. J. Biochem. (Tokyo) 66 (1969) 521-527. [PMID: 5354025]
Accepted name: glucoside 3-dehydrogenase (acceptor)
Reaction: sucrose + acceptor = 3-dehydro-α-D-glucosyl-β-D-fructofuranoside + reduced acceptor
Other name(s): D-glucoside 3-dehydrogenase (ambiguous); D-aldohexopyranoside dehydrogenase (ambiguous); D-aldohexoside:(acceptor) 3-oxidoreductase; thuA (gene name); thuB (gene name); glucoside 3-dehydrogenase
Systematic name: D-aldohexoside:acceptor 3-oxidoreductase
Comments: The enzymes from members of the Rhizobiaceae family (such as Agrobacterium tumefaciens) act on disaccharides that contain a glucose moiety at the non-reducing end, such as sucrose, trehalose, leucrose, palatinose, trehalulose, and maltitol, forming the respective 3'-keto derivatives. cf. EC 1.1.2.11, glucoside 3-dehydrogenase (cytochrome c).
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 9031-74-7
References:
1. Jensen, J.B., Ampomah, O.Y., Darrah, R., Peters, N.K. and Bhuvaneswari, T.V. Role of trehalose transport and utilization in Sinorhizobium meliloti-alfalfa interactions. Mol. Plant Microbe Interact. 18 (2005) 694-702. [PMID: 16042015]
2. Ampomah, O.Y., Avetisyan, A., Hansen, E., Svenson, J., Huser, T., Jensen, J.B. and Bhuvaneswari, T.V. The thuEFGKAB operon of Rhizobia and Agrobacterium tumefaciens codes for transport of trehalose, maltitol, and isomers of sucrose and their assimilation through the formation of their 3-keto derivatives. J. Bacteriol. 195 (2013) 3797-3807. [PMID: 23772075]
3. Ampomah, O.Y. and Jensen, J.B. The trehalose utilization gene thuA ortholog in Mesorhizobium loti does not influence competitiveness for nodulation on Lotus spp. World J. Microbiol. Biotechnol. 30 (2014) 1129-1134. [PMID: 24142427]
Accepted name: glycolate dehydrogenase
Reaction: glycolate + acceptor = glyoxylate + reduced acceptor
Other name(s): glycolate oxidoreductase; glycolic acid dehydrogenase; glycolate:(acceptor) 2-oxidoreductase
Systematic name: glycolate:acceptor 2-oxidoreductase
Comments: Also acts on (R)-lactate. 2,6-Dichloroindophenol and phenazine methosulfate can act as acceptors.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37368-32-4
References:
1. Lord, J.M. Glycolate oxidoreductase in Escherichia coli. Biochim. Biophys. Acta 267 (1972) 227-237. [PMID: 4557653]
[EC 1.1.99.15 Transferred entry: now EC 1.7.99.5 5,10-methylenetetrahydrofolate reductase (FADH2) (EC 1.1.99.15 created 1978, deleted 1980)]
[EC 1.1.99.16 Transferred entry: malate dehydrogenase (acceptor). As the acceptor is now known, the enzyme has been transferred to EC 1.1.5.4, malate dehydrogenase (quinone). (EC 1.1.99.16 created 1978, deleted 2009)]
[EC 1.1.99.17 Transferred entry: now EC 1.1.5.2 quinoprotein glucose dehydrogenase. (EC 1.1.99.17 created 1982, deleted 2003)]
Accepted name: cellobiose dehydrogenase (acceptor)
Reaction: cellobiose + acceptor = cellobiono-1,5-lactone + reduced acceptor
Other name(s): cellobiose dehydrogenase; cellobiose oxidoreductase; Phanerochaete chrysosporium cellobiose oxidoreductase; CBOR; cellobiose oxidase; cellobiose:oxygen 1-oxidoreductase; CDH; cellobiose:(acceptor) 1-oxidoreductase
Systematic name: cellobiose:acceptor 1-oxidoreductase
Comments: Also acts, more slowly, on cello-oligosaccharides, lactose and D-glucosyl-1,4-β-D-mannose. The enzyme from the white rot fungus Phanerochaete chrysosporium is unusual in having two redoxin domains, one containing a flavin and the other a protoheme group. It transfers reducing equivalents from cellobiose to two types of redox acceptor: two-electron oxidants, including redox dyes, benzoquinones, and molecular oxygen, and one-electron oxidants, including semiquinone species, iron(II) complexes, and the model acceptor cytochrome c [9]. 2,6-Dichloroindophenol can act as acceptor in vitro.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 54576-85-1
References:
1. Coudray, M.-R., Canebascini, G. and Meier, H. Characterization of a cellobiose dehydrogenase in the cellulolytic fungus porotrichum (Chrysosporium) thermophile. Biochem. J. 203 (1982) 277-284. [PMID: 7103940]
2. Dekker, R.F.H. Induction and characterization of a cellobiose dehydrogenase produced by a species of Monilia. J. Gen. Microbiol. 120 (1980) 309-316.
3. Dekker, R.F.H. Cellobiose dehydrogenase produced by Monilia sp. Methods Enzymol. 160 (1988) 454-463.
4. Habu, N., Samejima, M., Dean, J.F. and Eriksson, K.E. Release of the FAD domain from cellobiose oxidase by proteases from cellulolytic cultures of Phanerochaete chrysosporium. FEBS Lett. 327 (1993) 161-164. [PMID: 8392950]
5. Baminger, U., Subramaniam, S.S., Renganathan, V. and Haltrich, D. Purification and characterization of cellobiose dehydrogenase from the plant pathogen Sclerotium (Athelia) rolfsii. Appl. Environ. Microbiol. 67 (2001) 1766-1774. [PMID: 11282631]
6. Hallberg, B.M., Henriksson, G., Pettersson, G. and Divne, C. Crystal structure of the flavoprotein domain of the extracellular flavocytochrome cellobiose dehydrogenase. J. Mol. Biol. 315 (2002) 421-434. [PMID: 11786022]
7. Ayers, A.R., Ayers, S.B. and Eriksson, K.-E. Cellobiose oxidase, purification and partial characterization of a hemoprotein from Sporotrichum pulverulentum. Eur. J. Biochem. 90 (1978) 171-181. [PMID: 710416]
8. Ayers, A.R. and Eriksson, K.-E. Cellobiose oxidase from Sporotrichum pulverulentum. Methods Enzymol. 89 (1982) 129-135. [PMID: 7144569]
9. Mason, M.G., Nicholls, P., Divne, C., Hallberg, B.M., Henriksson, G. and Wilson, M.T. The heme domain of cellobiose oxidoreductase: a one-electron reducing system. Biochim. Biophys. Acta 1604 (2003) 47-54. [PMID: 12686420]
[EC 1.1.99.19 Deleted entry: uracil dehydrogenase. Now EC 1.17.99.4, uracil/thymine dehydrogenase (EC 1.1.99.19 created 1961 as EC 1.2.99.1, transferred 1984 to EC 1.1.99.19, deleted 2006)]
Accepted name: alkan-1-ol dehydrogenase (acceptor)
Reaction: primary alcohol + acceptor = aldehyde + reduced acceptor
Other name(s): polyethylene glycol dehydrogenase; alkan-1-ol:(acceptor) oxidoreductase
Systematic name: alkan-1-ol:acceptor oxidoreductase
Comments: A quinoprotein. Acts on C3-C16 linear-chain saturated primary alcohols, C4-C7 aldehydes and on non-ionic surfactants containing polyethylene glycol residues, such as Tween 40 and 60, but not on methanol and only very slowly on ethanol. 2,6-Dichloroindophenol can act as acceptor. cf. EC 1.1.99.8 alcohol dehydrogenase (acceptor).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 75496-55-8
References:
1. Kawai, F., Kimura, T., Tani, Y., Yamada, H., Ueno, T. and Fukami, H. Identification of reaction-products of polyethylene-glycol dehydrogenase. Agric. Biol. Chem. 47 (1983) 1669-1671.
2. Kawai, F., Yamanaka, H., Ameyama, M., Shinagawa, E., Matsushita, K. and Adachi, O. Identification of the prosthetic group and further characterization of a novel enzyme, polyethylene-glycol dehydrogenase. Agric. Biol. Chem. 49 (1985) 1071-1076.
Accepted name: D-sorbitol dehydrogenase (acceptor)
Reaction: D-sorbitol + acceptor = L-sorbose + reduced acceptor
Other name(s): D-sorbitol:(acceptor) 1-oxidoreductase
Systematic name: D-sorbitol:acceptor 1-oxidoreductase
Comments: A flavoprotein (FAD).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 86178-94-1
References:
1. Shinagawa, E. and Ameyama, M. Purification and characterization of D-sorbitol dehydrogenase from membrane of Gluconobacter suboxydans var-alpha. Agric. Biol. Chem. 46 (1982) 135-141.
Accepted name: glycerol dehydrogenase (acceptor)
Reaction: glycerol + acceptor = glycerone + reduced acceptor
Other name(s): glycerol:(acceptor) 1-oxidoreductase
Systematic name: glycerol:acceptor 1-oxidoreductase
Comments: A quinoprotein. Also acts, more slowly, on a number of other polyols including D-sorbitol, D-arabinitol, meso-erythritol, ribitol and propane-1,2-diol.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 249285-11-8
References:
1. Ameyama, M., Shinagawa, E., Matsushita, K. and Adachi, O. Solubilization, purification and properties of membrane-bound glycerol dehydrogenase from Gluconobacter industrius. Agric. Biol. Chem. 49 (1985) 1001-1010.
[EC 1.1.99.23 Transferred entry: polyvinyl-alcohol dehydrogenase (acceptor). Now EC 1.1.2.6, polyvinyl alcohol dehydrogenase (cytochrome) (EC 1.1.99.23 created 1989, deleted 2010)]
Accepted name: hydroxyacid-oxoacid transhydrogenase
Reaction: (S)-3-hydroxybutanoate + 2-oxoglutarate = acetoacetate + (R)-2-hydroxyglutarate
Other name(s): transhydrogenase, hydroxy acid-oxo acid
Systematic name: (S)-3-hydroxybutanoate:2-oxoglutarate oxidoreductase
Comments: 4-Hydroxybutanoate and (R)-2-hydroxyglutarate can also act as donors; 4-oxobutanoate can also act as acceptor.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 117698-31-4
References:
1. Kaufman, E.E., Nelson, T., Fales, H.M. and Levin, D.M. Isolation and characterization of a hydroxyacid-oxoacid transhydrogenase from rat kidney mitochondria. J. Biol. Chem. 263 (1988) 16872-16879. [PMID: 3182820]
[EC 1.1.99.25 Transferred entry: quinate dehydrogenase (pyrroloquinoline-quinone). Now EC 1.1.5.8, quinate dehydrogenase (quinone) (EC 1.1.99.25 created 1992, modified 2004, deleted 2010)]
Accepted name: 3-hydroxycyclohexanone dehydrogenase
Reaction: 3-hydroxycyclohexanone + acceptor = cyclohexane-1,3-dione + reduced acceptor
Systematic name: 3-hydroxycyclohexanone:acceptor 1-oxidoreductase
Comments: 2,6-Dichloroindophenol and methylene blue can act as acceptors.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 123516-44-9
References:
1. Dangel, W., Tschech, A. and Fuchs, G. Enzyme-reactions involved in anaerobic cyclohexanol metabolism by a denitrifying Pseudomonas species. Arch. Microbiol. 152 (1989) 273-279.
Accepted name: (R)-pantolactone dehydrogenase (flavin)
Reaction: (R)-pantolactone + acceptor = 2-dehydropantolactone + reduced acceptor
Other name(s): 2-dehydropantolactone reductase (flavin); 2-dehydropantoyl-lactone reductase (flavin); (R)-pantoyllactone dehydrogenase (flavin)
Systematic name: (R)-pantolactone:acceptor oxidoreductase (flavin-containing)
Comments: high specificity for (R)-pantolactone. Phenazine methosulfate (PMS) can act as acceptor. The enzyme has been studied in the bacterium Nocardia asteroides and shown to be membrane-bound and induced by 1,2-propanediol. The FMN cofactor is non-covalently bound.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 140879-14-7
References:
1. Kataoka, M., Shimizu, S. and Yamada, H. Purification and characterization of a novel FMN-dependent enzyme. Membrane-bound L-(+)-pantoyl lactone dehydrogenase from Nocardia asteroides. Eur. J. Biochem. 204 (1992) 799-806. [PMID: 1541293]
Accepted name: glucose-fructose oxidoreductase
Reaction: D-glucose + D-fructose = D-gluconolactone + D-glucitol
Systematic name: D-glucose:D-fructose oxidoreductase
Comments: D-mannose, D-xylose, D-galactose, 2-deoxy-D-glucose and L-arabinose will function as aldose substrates, but with low affinities. The ketose substrate must be in the open-chain form. The apparent affinity for fructose is low, because little of the fructose substrate is in the open-chain form. Xylulose and glycerone (dihydroxyacetone) will replace fructose, but they are poor substrates. The enzyme from Zymomonas mobilis contains tightly bound NADP+.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 94949-35-6
References:
1. Zachariou, M. and Scopes, R.K. Glucose-fructose oxidoreductase: a new enzyme isolated from Zymomonas mobilis that is responsible for sorbitol production. J. Bacteriol. 167 (1986) 863-869.
2. Hardman, M.J. and Scopes, R.K. The kinetics of glucose-fructose oxidoreductase from Zymomonas mobilis. Eur. J. Biochem. 173 (1988) 203-209.
3. Kanagasundaram, V. and Scopes, R.K. Cloning, sequence analysis and expression of the structural gene encoding glucose-fructose oxidoreductase. J. Bacteriol. 174 (1992) 1439-1447. [PMID: 1537789]
Accepted name: pyranose dehydrogenase (acceptor)
Reaction: (1) a pyranose + acceptor = a pyranos-2-ulose (or a pyranos-3-ulose or a pyranos-2,3-diulose) + reduced acceptor
(2)a pyranoside + acceptor = a pyranosid-3-ulose (or a pyranosid-3,4-diulose) + reduced acceptor
Glossary: ferricenium ion = bis(η5-cyclopentadienyl)iron(1+)
Other name(s): pyranose dehydrogenase; pyranose-quinone oxidoreductase; quinone-dependent pyranose dehydrogenase; PDH
Systematic name: pyranose:acceptor oxidoreductase
Comments: Requires FAD. A number of aldoses and ketoses in pyranose form, as well as glycosides, gluco-oligosaccharides, sucrose and lactose can act as a donor. 1,4-Benzoquinone or ferricenium ion (ferrocene oxidized by removal of one electron) can serve as acceptor. Unlike EC 1.1.3.10, pyranose oxidase, this fungal enzyme does not interact with O2 and exhibits extremely broad substrate tolerance with variable regioselectivity (C-3, C-2 or C-3 + C-2 or C-3 + C-4) for (di)oxidation of different sugars. D-Glucose is exclusively or preferentially oxidized at C-3 (depending on the enzyme source), but can also be oxidized at C-2 + C-3. The enzyme also acts on 14-α- and 14-β-gluco-oligosaccharides, non-reducing gluco-oligosaccharides and L-arabinose, which are not substrates of EC 1.1.3.10. Sugars are oxidized in their pyranose but not in their furanose form.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 190606-21-4
References:
1. Volc, J., Kubátová, E., Wood, D. and Daniel, G. Pyranose 2-dehydrogenase, a novel sugar oxidoreductase from the basidiomycete fungus Agaricus bisporus. Arch. Microbiol. 167 (1997) 119-125. [PMID: 9042751]
2. Volc, J., Sedmera, P., Halada, P., Pøikyrlová, V. and Daniel, G. C-2 and C-3 oxidation of D-Glc, and C-2 oxidation of D-Gal by pyranose dehydrogenase from Agaricus bisporus. Carbohydr. Res. 310 (1998) 151-156.
3. Volc, J., Sedmera, P., Halada, P., Pøikyrlová, V. and Haltrich, D. Double oxidation of D-xylose to D-glycero-pentos-2,3-diulose (2,3-diketo-D-xylose) by pyranose dehydrogenase from the mushroom Agaricus bisporus. Carbohydr. Res 329 (2000) 219-225. [PMID: 11086703]
4. Volc, J., Kubátová, E., Daniel, G., Sedmera, P. and Haltrich, D. Screening of basidiomycete fungi for the quinone-dependent sugar C-2/C-3 oxidoreductase, pyranose dehydrogenase, and properties of the enzyme from Macrolepiota rhacodes. Arch. Microbiol. 176 (2001) 178-186. [PMID: 11511865]
5. Volc, J., Sedmera, P., Halada, P., Daniel, G., Pøikyrlová, V. and Haltrich, D. C-3 oxidation of non-reducing sugars by a fungal pyranose dehydrogenase: spectral characterization. J. Mol. Catal., B Enzym. 17 (2002) 91-100.
Accepted name: 2-oxo-acid reductase
Reaction: a (2R)-hydroxy-carboxylate + acceptor = a 2-oxocarboxylate + reduced acceptor
Other name(s): (2R)-hydroxycarboxylate-viologen-oxidoreductase; HVOR; 2-oxoacid reductase
Systematic name: (2R)-hydroxy-carboxylate:acceptor oxidoreductase
Comments: Contains [4Fe-4S] and a mononucleotide molybdenum (pyranopterin) cofactor. Has broad substrate specificity, with 2-oxo-monocarboxylates and 2-oxo-dicarboxylates acting as substrates. Branching in a substrate at the C-3 position results in loss of activity. The enzyme from Proteus sp. is inactivated by oxygen.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 115299-99-5
References:
1. Trautwein, T., Krauss, F., Lottspeich, F. and Simon, H. The (2R)-hydroxycarboxylate-viologen-oxidoreductase from Proteus vulgaris is a molybdenum-containing iron-sulphur protein. Eur. J. Biochem. 222 (1994) 1025-1032. [PMID: 8026480]
2. Neumann, S. and Simon, H. On a non-pyridine nucleotide-dependent 2-oxoacid reductase of broad specificity from two Proteus species. FEBS Lett.167 (1985) 29-32.
Accepted name: (S)-mandelate dehydrogenase
Reaction: (S)-mandelate + acceptor = phenylglyoxylate + reduced acceptor
For diagram click here.
Glossary: (S)-mandelate = (S)-2-hydroxy-2-phenylacetate
phenylglyoxylate = benzoylformate = 2-oxo-2-phenylacetate
Other name(s): MDH (ambiguous)
Systematic name: (S)-mandelate:acceptor 2-oxidoreductase
Comments: This enzyme is a member of the FMN-dependent α-hydroxy-acid oxidase/dehydrogenase family [1]. While all enzymes of this family oxidize the (S)-enantiomer of an α-hydroxy acid to an α-oxo acid, the ultimate oxidant (oxygen, intramolecular heme or some other acceptor) depends on the particular enzyme. This enzyme transfers the electron pair from FMNH2 to a component of the electron transport chain, most probably ubiquinone [1,2]. It is part of a metabolic pathway in Pseudomonads that allows these organisms to utilize mandelic acid, derivatized from the common soil metabolite amygdalin, as the sole source of carbon and energy [2]. The enzyme has a large active-site pocket and preferentially binds substrates with longer sidechains, e.g. 2-hydroxyoctanoate rather than 2-hydroxybutyrate [1]. It also prefers substrates that, like (S)-mandelate, have β unsaturation, e.g. (indol-3-yl)glycolate compared with (indol-3-yl)lactate [1]. Esters of mandelate, such as methyl (S)-mandelate, are also substrates [3].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9067-95-2
References:
1. Lehoux, I.E. and Mitra, B. (S)-Mandelate dehydrogenase from Pseudomonas putida: mechanistic studies with alternate substrates and pH and kinetic isotope effects. Biochemistry 38 (1999) 5836-5848. [PMID: 10231535]
2. Dewanti, A.R., Xu, Y. and Mitra, B. Role of glycine 81 in (S)-mandelate dehydrogenase from Pseudomonas putida in substrate specificity and oxidase activity. Biochemistry 43 (2004) 10692-10700. [PMID: 15311930]
3. Dewanti, A.R., Xu, Y. and Mitra, B. Esters of mandelic acid as substrates for (S)-mandelate dehydrogenase from Pseudomonas putida: implications for the reaction mechanism. Biochemistry 43 (2004) 1883-1890. [PMID: 14967029]
Accepted name: L-sorbose 1-dehydrogenase
Reaction: L-sorbose + acceptor = 1-dehydro-L-sorbose + reduced acceptor
Glossary: 1-dehydro-L-sorbose = L-sorbosone = 2-dehydro-L-gulose
Other name(s): SDH (ambiguous)
Systematic name: L-sorbose:acceptor 1-oxidoreductase
Comments: The product, L-sorbosone, is an intermediate in bacterial 2-keto-L-gulonic-acid formation. The activity of this membrane-bound enzyme is stimulated by Fe(III) or Co2+ but is inhibited by Cu2+. The enzyme is highly specific for L-sorbose as other sugars, such as glucose, mannitol and sorbitol, are not substrates. Phenazine methosulfate and DCIP can act as artificial acceptors.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Sugisawa, T., Hoshino, T., Nomura, S. and Fujiwara, A. Isolation and characterization of membrane-bound L-sorbose dehydrogenase from Gluconobacter melanogenus UV10. Agric. Biol. Chem. 55 (1991) 363-370.
[EC 1.1.99.33 Transferred entry: formate dehydrogenase (acceptor). Now EC 1.17.99.7, formate dehydrogenase (acceptor) (EC 1.1.99.33 created 2010, deleted 2017)]
[EC 1.1.99.34 Transferred entry: glucose-6-phosphate dehydrogenase (coenzyme-F420). As the acceptor is now known, the enzyme has been transferred to EC 1.1.98.2, glucose-6-phosphate dehydrogenase (coenzyme-F420) (EC 1.1.99.34 created 2010, deleted 2011)]
Accepted name: soluble quinoprotein glucose dehydrogenase
Reaction: D-glucose + acceptor = D-glucono-1,5-lactone + reduced acceptor
Other name(s): soluble glucose dehydrogenase; sGDH; glucose dehydrogenase (PQQ-dependent)
Systematic name: D-glucose:acceptor oxidoreductase
Comments: Soluble periplasmic enzyme containing PQQ as prosthetic group, bound to a calcium ion. Electron acceptor is not known. It is assayed with Wurster's Blue or phenazine methosulfate. It has negligible sequence or structure similarity to other quinoproteins. It catalyses an exceptionally high rate of oxidation of a wide range of aldose sugars, including D-glucose, galactose, arabinose and xylose, and also the disaccharides lactose, cellobiose and maltose. It has been described only in Acinetobacter calcoaceticus.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Geiger, O. and Gorisch, H. Crystalline quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus. Biochemistry 25 (1986) 6043-6048.
2. Dokter, P., Frank, J. and Duine, J.A. Purification and characterization of quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus L.M.D. 79.41. Biochem. J. 239 (1986) 163-167. [PMID: 3800975]
3. Cleton-Jansen, A.M., Goosen, N., Wenzel, T.J. and van de Putte, P. Cloning of the gene encoding quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus: evidence for the presence of a second enzyme. J. Bacteriol. 170 (1988) 2121-2125. [PMID: 2834325]
4. Matsushita, K., Shinagawa, E., Adachi, O. and Ameyama, M. Quinoprotein D-glucose dehydrogenase of the Acinetobacter calcoaceticus respiratory chain: membrane-bound and soluble forms are different molecular species. Biochemistry 28 (1989) 6276-6280. [PMID: 2551369]
5. Oubrie, A. and Dijkstra, B.W. Structural requirements of pyrroloquinoline quinone dependent enzymatic reactions. Protein Sci. 9 (2000) 1265-1273. [PMID: 10933491]
6. Matsushita, K., Toyama, H., Ameyama, M., Adachi, O., Dewanti, A. and Duine, J.A. Soluble and membrane-bound quinoprotein D-glucose dehydrogenases of the Acinetobacter calcoaceticus: The binding process of PQQ to the apoenzymes. Biosci. Biotechnol. Biochem 59 (1995) 1548-1555.
Accepted name: alcohol dehydrogenase (nicotinoprotein)
Reaction: ethanol + acceptor - acetaldehyde + reduced acceptor
Other name(s): nicotinoprotein alcohol dehydrogenase; np-ADH; NDMA-dependent alcohol dehydrogenase; ethanol:N,N-dimethyl-4-nitrosoaniline oxidoreductase
Systematic name: ethanol:acceptor oxidoreductase
Comments: Contains Zn2+. Nicotinoprotein alcohol dehydrogenases are unique medium-chain dehydrogenases/reductases (MDR) alcohol dehydrogenases that have a tightly bound NAD+/NADH cofactor that does not dissociate during the catalytic process. Instead, the cofactor is regenerated by a second substrate or electron carrier. While the in vivo electron acceptor is not known, N,N-dimethyl-4-nitrosoaniline (NDMA), which is reduced to 4-(hydroxylamino)-N,N-dimethylaniline, can serve this function in vitro. The enzyme from the Gram-positive bacterium Amycolatopsis methanolica can accept many primary alcohols as substrates, including benzylalcohol [1].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Van Ophem, P.W., Van Beeumen, J. and Duine, J.A. Nicotinoprotein [NAD(P)-containing] alcohol/aldehyde oxidoreductases. Purification and characterization of a novel type from Amycolatopsis methanolica. Eur. J. Biochem. 212 (1993) 819-826. [PMID: 8385013]
2. Piersma, S.R., Visser, A.J., de Vries, S. and Duine, J.A. Optical spectroscopy of nicotinoprotein alcohol dehydrogenase from Amycolatopsis methanolica: a comparison with horse liver alcohol dehydrogenase and UDP-galactose epimerase. Biochemistry 37 (1998) 3068-3077. [PMID: 9485460]
3. Schenkels, P. and Duine, J.A. Nicotinoprotein (NADH-containing) alcohol dehydrogenase from Rhodococcus erythropolis DSM 1069: an efficient catalyst for coenzyme-independent oxidation of a broad spectrum of alcohols and the interconversion of alcohols and aldehydes. Microbiology 146 (2000) 775-785. [PMID: 10784035]
4. Piersma, S.R., Norin, A., de Vries, S., Jornvall, H. and Duine, J.A. Inhibition of nicotinoprotein (NAD+-containing) alcohol dehydrogenase by trans-4-(N,N-dimethylamino)-cinnamaldehyde binding to the active site. J. Protein Chem. 22 (2003) 457-461. [PMID: 14690248]
5. Norin, A., Piersma, S.R., Duine, J.A. and Jornvall, H. Nicotinoprotein (NAD+ -containing) alcohol dehydrogenase: structural relationships and functional interpretations. Cell. Mol. Life Sci. 60 (2003) 999-1006. [PMID: 12827287]
Accepted name: methanol dehydrogenase (nicotinoprotein)
Reaction: methanol + acceptor = formaldehyde + reduced acceptor
Other name(s): NDMA-dependent methanol dehydrogenase; nicotinoprotein methanol dehydrogenase; methanol:N,N-dimethyl-4-nitrosoaniline oxidoreductase
Systematic name: methanol:acceptor oxidoreductase
Comments: Contains Zn2+ and Mg2+. Nicotinoprotein methanol dehydrogenases have a tightly bound NADP+/NADPH cofactor that does not dissociate during the catalytic process. Instead, the cofactor is regenerated by a second substrate or electron carrier. While the in vivo electron acceptor is not known, N,N-dimethyl-4-nitrosoaniline (NDMA), which is reduced to 4-(hydroxylamino)-N,N-dimethylaniline, can serve this function in vitro. The enzyme has been detected in several Gram-positive methylotrophic bacteria, including Amycolatopsis methanolica, Rhodococcus rhodochrous and Rhodococcus erythropolis [1-3]. These enzymes are decameric, and possess a 5-fold symmetry [4]. Some of the enzymes can also dismutate formaldehyde to methanol and formate [5].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Vonck, J., Arfman, N., De Vries, G.E., Van Beeumen, J., Van Bruggen, E.F. and Dijkhuizen, L. Electron microscopic analysis and biochemical characterization of a novel methanol dehydrogenase from the thermotolerant Bacillus sp. C1. J. Biol. Chem. 266 (1991) 3949-3954. [PMID: 1995642]
2. Van Ophem, P.W., Van Beeumen, J. and Duine, J.A. Nicotinoprotein [NAD(P)-containing] alcohol/aldehyde oxidoreductases. Purification and characterization of a novel type from Amycolatopsis methanolica. Eur. J. Biochem. 212 (1993) 819-826. [PMID: 8385013]
3. Bystrykh, L.V., Vonck, J., van Bruggen, E.F., van Beeumen, J., Samyn, B., Govorukhina, N.I., Arfman, N., Duine, J.A. and Dijkhuizen, L. Electron microscopic analysis and structural characterization of novel NADP(H)-containing methanol: N,N'-dimethyl-4-nitrosoaniline oxidoreductases from the gram-positive methylotrophic bacteria Amycolatopsis methanolica and Mycobacterium gastri MB19. J. Bacteriol. 175 (1993) 1814-1822. [PMID: 8449887]
4. Hektor, H.J., Kloosterman, H. and Dijkhuizen, L. Identification of a magnesium-dependent NAD(P)(H)-binding domain in the nicotinoprotein methanol dehydrogenase from Bacillus methanolicus. J. Biol. Chem. 277 (2002) 46966-46973. [PMID: 12351635]
5. Park, H., Lee, H., Ro, Y.T. and Kim, Y.M. Identification and functional characterization of a gene for the methanol : N,N'-dimethyl-4-nitrosoaniline oxidoreductase from Mycobacterium sp. strain JC1 (DSM 3803). Microbiology 156 (2010) 463-471. [PMID: 19875438]
Accepted name: 2-deoxy-scyllo-inosamine dehydrogenase (AdoMet-dependent)
Reaction: 2-deoxy-scyllo-inosamine + S-adenosyl-L-methionine = 3-amino-2,3-dideoxy-scyllo-inosose + 5'-deoxyadenosine + L-methionine
For diagram of reaction click here.
Other name(s): btrN (gene name); 2-deoxy-scyllo-inosamine dehydrogenase (SAM-dependent)
Systematic name: 2-deoxy-scyllo-inosamine:S-adenosyl-L-methionine 1-oxidoreductase
Comments: Involved in the biosynthetic pathway of the aminoglycoside antibiotics of the butirosin family. The enzyme from Bacillus circulans was shown to be a radical S-adenosyl-L-methionine (SAM) enzyme. cf. EC 1.1.1.329, 2-deoxy-scyllo-inosamine dehydrogenase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Yokoyama, K., Numakura, M., Kudo, F., Ohmori, D. and Eguchi, T. Characterization and mechanistic study of a radical SAM dehydrogenase in the biosynthesis of butirosin. J. Am. Chem. Soc. 129 (2007) 15147-15155. [PMID: 18001019]
2. Yokoyama, K., Ohmori, D., Kudo, F. and Eguchi, T. Mechanistic study on the reaction of a radical SAM dehydrogenase BtrN by electron paramagnetic resonance spectroscopy. Biochemistry 47 (2008) 8950-8960. [PMID: 18672902]
Accepted name: D-2-hydroxyglutarate dehydrogenase
Reaction: (R)-2-hydroxyglutarate + acceptor = 2-oxoglutarate + reduced acceptor
Other name(s): AtD-2HGDH
Systematic name: (R)-2-hydroxyglutarate:acceptor 2-oxidoreductase
Comments: Contains FAD. The enzyme has no activity with NAD+ or NADP+, and was assayed in vitro using artificial electron acceptors. It has lower activity with (R)-lactate, (R)-2-hydroxybutyrate and meso-tartrate, and no activity with the (S) isomers. The mammalian enzyme is stimulated by Zn2+, Co2+ and Mn2+.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Engqvist, M., Drincovich, M.F., Flugge, U.I. and Maurino, V.G. Two D-2-hydroxy-acid dehydrogenases in Arabidopsis thaliana with catalytic capacities to participate in the last reactions of the methylglyoxal and β-oxidation pathways. J. Biol. Chem. 284 (2009) 25026-25037. [PMID: 19586914]
2. Achouri, Y., Noel, G., Vertommen, D., Rider, M.H., Veiga-Da-Cunha, M. and Van Schaftingen, E. Identification of a dehydrogenase acting on D-2-hydroxyglutarate. Biochem. J. 381 (2004) 35-42. [PMID: 15070399]
Accepted name: (R)-2-hydroxyglutarate—pyruvate transhydrogenase
Reaction: (R)-2-hydroxyglutarate + pyruvate = 2-oxoglutarate + (R)-lactate
Other name(s): DLD3 (gene name)
Systematic name: (R)-2-hydroxyglutarate:pyruvate oxidoreductase [(R)-lactate-forming]
Comments: The enzyme, characterized in the yeast Saccharomyces cerevisiae, also functions as EC 1.1.2.4, D-lactate dehydrogenase (cytochrome), and is active with oxaloacetate as electron acceptor forming (R)-malate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Becker-Kettern, J., Paczia, N., Conrotte, J.F., Kay, D.P., Guignard, C., Jung, P.P. and Linster, C.L. Saccharomyces cerevisiae forms D-2-hydroxyglutarate and couples its degradation to D-lactate formation via a cytosolic transhydrogenase. J. Biol. Chem. 291 (2016) 6036-6058. [PMID: 26774271]
Accepted name: 3-hydroxy-1,2-didehydro-2,3-dihydrotabersonine reductase
Reaction: (1) (3R)-3-hydroxy-16-methoxy-2,3-dihydrotabersonine + acceptor = (3R)-3-hydroxy-16-methoxy-1,2-didehydro-2,3-dihydrotabersonine + reduced acceptor
(2) (3R)-3-hydroxy-2,3-dihydrotabersonine + acceptor = (3R)-3-hydroxy-1,2-didehydro-2,3-dihydrotabersonine + reduced acceptor
For diagram of reaction, click here
Other name(s): T3R; tabersonine 3-reductase
Systematic name: (3R)-3-hydroxy-16-methoxy-2,3-dihydrotabersonine:acceptor oxidoreductase
Comments: This enzyme is involved in the biosynthesis of vindoline and vindorosine in the plant Catharanthus roseus (Madagascar periwinkle). In vivo, it functions in the direction of reduction. It has no activity with 3-epoxylated compounds, which can form spontaneously from its unstable substrates.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Qu, Y., Easson, M.L., Froese, J., Simionescu, R., Hudlicky, T. and De Luca, V. Completion of the seven-step pathway from tabersonine to the anticancer drug precursor vindoline and its assembly in yeast. Proc. Natl Acad. Sci. USA 112 (2015) 6224-6229. [PMID: 25918424]
Accepted name: 4-pyridoxic acid dehydrogenase
Reaction: 4-pyridoxate + acceptor = 5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate + reduced acceptor
For diagram of reaction click here.
Glossary: 4-pyridoxate = 3-hydroxy-5-(hydroxymethyl)-2-methylpyridine-4-carboxylate
dichloroindophenol = DCPIP = 2,6-dichloro-4-[(4-hydroxyphenyl)imino]cyclohexa-2,5-dien-1-one
Other name(s): mlr6792 (locus name)
Systematic name: 4-pyridoxate:acceptor 5-oxidoreductase
Comments: The enzyme, characterized from the bacteria Pseudomonas sp. MA-1 and Mesorhizobium loti, participates in the degradation of pyridoxine (vitamin B6). It is membrane bound and contains FAD. The enzyme has been assayed in vitro in the presence of the artificial electron acceptor dichloroindophenol (DCPIP).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Yagi, T., Kishore, G.M. and Snell, E.E. The bacterial oxidation of vitamin B6. 4-Pyridoxic acid dehydrogenase: a membrane-bound enzyme from Pseudomonas MA-1. J. Biol. Chem 258 (1983) 9419-9425. [PMID: 6348042]
2. Ge, F., Yokochi, N., Yoshikane, Y., Ohnishi, K. and Yagi, T. Gene identification and characterization of the pyridoxine degradative enzyme 4-pyridoxic acid dehydrogenase from the nitrogen-fixing symbiotic bacterium Mesorhizobium loti MAFF303099. J. Biochem. 143 (2008) 603-609. [PMID: 18216065]