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.
An asterisk before 'EC' indicates that this is an amendment to an existing enzyme rather than a new enzyme entry.
Common name: quinate dehydrogenase
Reaction: quinate + NAD+ = 3-dehydroquinate + NADH + H+
For diagram click here.
Glossary: quinate = 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): quinic dehydrogenase; quinate dehydrogenase; quinate:NAD oxidoreductase; quinate 5-dehydrogenase; quinate:NAD+ 5-oxidoreductase
Systematic name: L-quinate:NAD+ 3-oxidoreductase
Comments: The enzyme is specific for quinate as substrate; phenylpyruvate, phenylalanine, cinnamate and shikimate will not act as substrates. NAD+ cannot be replaced by NADP+.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, ERGO, CAS registry number: 9028-28-8
References:
1. Gamborg, O.L. Aromatic metabolism in plants. III. Quinate dehydrogenase from mung bean cell suspension cultures. Biochim. Biophys. Acta 128 (1966) 483-491.
2. Mitsuhashi, S. and Davis, B.D. Aromatic biosynthesis. XIII. Conversion of quinic acid to 5-dehydroquinic acid by quinic dehydrogenase. Biochim. Biophys. Acta 15 (1954) 268-280.
Common name: shikimate dehydrogenase
Reaction: shikimate + NADP+ = 3-dehydroshikimate + NADPH + H+
For diagram click here.
Other name(s): dehydroshikimic reductase; shikimate oxidoreductase; shikimate:NADP+ oxidoreductase; 5-dehydroshikimate reductase; shikimate 5-dehydrogenase; 5-dehydroshikimic reductase; DHS reductase; shikimate:NADP+ 5-oxidoreductase; AroE
Systematic name: shikimate:NADP+ 3-oxidoreductase
Comments: NAD+ cannot replace NADP+ [3]. In higher organisms, this enzyme forms part of a multienzyme complex with EC 4.2.1.10, 3-dehydroquinate dehydratase [4].
Links to other databases: BRENDA, EXPASY, GTD, KEGG, ERGO, CAS registry number: 9026-87-3
References:
1. Balinsky, D. and Davies, D.D. Aromatic biosynthesis in higher plants. 1. Preparation and properties of dehydroshikimic reductase. Biochem. J. 80 (1961) 292-296. [PMID: 13686342]
2. Mitsuhashi, S. and Davis, B.D. Aromatic biosynthesis. XIII. Conversion of quinic acid to 5-dehydroquinic acid by quinic dehydrogenase. Biochim. Biophys. Acta 15 (1954) 268-280. [PMID: 13208693]
3. Yaniv, H. and Gilvarg, C. Aromatic biosynthesis. XIV. 5-Dehydroshikimic reductase. J. Biol. Chem. 213 (1955) 787-795. [PMID: 14367339]
4. Chaudhuri, S. and Coggins, J.R. The purification of shikimate dehydrogenase from Escherichia coli. Biochem. J. 226 (1985) 217-223. [PMID: 3883995]
5. Anton, I.A. and Coggins, J.R. Sequencing and overexpression of the Escherichia coli aroE gene encoding shikimate dehydrogenase. Biochem. J. 249 (1988) 319-326. [PMID: 3277621]
6. Ye, S., Von Delft, F., Brooun, A., Knuth, M.W., Swanson, R.V. and McRee, D.E. The crystal structure of shikimate dehydrogenase (AroE) reveals a unique NADPH binding mode. J. Bacteriol. 185 (2003) 4144-4151. [PMID: 12837789]
Common name: homoisocitrate dehydrogenase
Reaction: (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+ = 2-oxoadipate + CO2 + NADH + H+
Other name(s): 2-hydroxy-3-carboxyadipate dehydrogenase; 3-carboxy-2-hydroxyadipate dehydrogenase; homoisocitric dehydrogenase; (-)-1-hydroxy-1,2,4-butanetricarboxylate:NAD+ oxidoreductase (decarboxylating); 3-carboxy-2-hydroxyadipate:NAD+ oxidoreductase (decarboxylating)
Systematic name: (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate:NAD+ oxidoreductase (decarboxylating)
Comments: Forms part of the lysine biosynthesis pathway in fungi [3].
Links to other databases: BRENDA, EXPASY, KEGG, ERGO, CAS registry number: 37250-23-0
References:
1. Strassman, M. and Ceci, L.N. Enzymatic formation of a-ketoadipic acid from homoisocitric acid. J. Biol. Chem. 240 (1965) 4357-4361. [PMID: 4284830]
2. Rowley, B. and Tucci, A.F. Homoisocitric dehydrogenase from yeast. Arch. Biochem. Biophys. 141 (1970) 499-510. [PMID: 4395693]
3. Zabriskie, T.M. and Jackson, M.D. Lysine biosynthesis and metabolism in fungi. Nat. Prod. Rep. 17 (2000) 85-97. [PMID: 10714900]
[EC 1.1.1.155 Deleted entry. The enzyme is identical to EC 1.1.1.87, homoisocitrate dehydrogenase (EC 1.1.1.155 created 1976, deleted 2004)]
[EC 1.1.1.204 Transferred entry: now EC 1.17.1.4, xanthine dehydrogenase. The enzyme was incorrectly classified as acting on a CH-OH group (EC 1.1.1.204 created 1972 as EC 1.2.1.37, transferred 1984 to EC 1.1.1.204, modified 1989, deleted 2004)]
Common name: quinate/shikimate dehydrogenase
Reaction: (1) L-quinate + NAD(P)+ = 3-dehydroquinate + NAD(P)H + H+
(2) shikimate + NAD(P)+ = 3-dehydroshikimate + NAD(P)H + H+
For diagram, click here.
Glossary: quinate = 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): YdiB
Systematic name: L-quinate:NAD(P)+ 3-oxidoreductase
Comments: This is the second shikimate dehydrogenase enzyme found in Escherichia coli and differs from EC 1.1.1.25, shikimate 3-dehydrogenase, in that it can use both quinate and shikimate as substrate and either NAD+ or NADP+ as acceptor.
References:
1. Michel, G., Roszak, A.W., Sauvé, V., Maclean, J., Matte, A., Coggins, J.R., Cygler, M. and Lapthorn, A.J. Structures of shikimate dehydrogenase AroE and its paralog YdiB. A common structural framework for different activities. J. Biol. Chem. 278 (2003) 19463-19472. [PMID: 12637497]
2. Benach, J., Lee, I., Edstrom, W., Kuzin, A.P., Chiang, Y., Acton, T.B., Montelione, G.T. and Hunt, J.F. The 2.3-Å crystal structure of the shikimate 5-dehydrogenase orthologue YdiB from Escherichia coli suggests a novel catalytic environment for an NAD-dependent dehydrogenase. J. Biol. Chem. 278 (2003) 19176-19182. [PMID: 12624088]
[EC 1.1.3.22 Transferred entry: Now EC 1.17.3.2, xanthine oxidase. The enzyme was incorrectly classified as acting on a CH-OH group (EC 1.1.3.22 created 1961 as EC 1.2.3.2, transferred 1984 to EC 1.1.3.22, modified 1989, deleted 2004)]
Common name: quinate dehydrogenase (pyrroloquinoline-quinone)
Reaction: quinate + pyrroloquinoline-quinone = 3-dehydroquinate + reduced pyrroloquinoline-quinone
For diagram, click here.
Glossary: quinate = 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
Systematic name: quinate:pyrroloquinoline-quinone 3-oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, ERGO, 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]
Common name: pyranose dehydrogenase (acceptor)
Reaction: (1) pyranose + acceptor = 2-dehydropyranose (or 3-dehydropyranose or 2,3-didehydropyranose) + reduced acceptor
(2) a pyranoside + acceptor = a 3-dehydropyranoside (or 3,4-didehydropyranoside) + 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.
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: Enzymatic 17 (2002) 91-100.
Common name: 2-oxo-acid reductase
Reaction: a (2R)-hydroxy-carboxylate + acceptor = a 2-oxo-carboxylate + 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.
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.
Common name: aldehyde oxidase
Reaction: an aldehyde + H2O + O2 = a carboxylic acid + H2O2
Other name(s): quinoline oxidase
Systematic name: aldehyde:oxygen oxidoreductase
Comments: Contains molybdenum, [2Fe-2S] centres and FAD. Also oxidizes quinoline and pyridine derivatives. May be identical with EC 1.2.3.11, retinal oxidase.
Links to other databases: BRENDA, EXPASY, KEGG, ERGO, CAS registry number: 9029-07-6
References:
1. Gordon, A.H., Green, D.E. and Subrahmanyan, V. Liver aldehyde oxidase. Biochem. J. 34 (1940) 764-774.
2. Knox, W.E. The quinine-oxidizing enzyme and liver aldehyde oxidase. J. Biol. Chem. 163 (1946) 699-711.
3. Mahler, H.R., Mackler, B., Green, D.E. and Bock, R.M. Studies on metalloflavoproteins. III. Aldehyde oxidase: a molybdoflavoprotein J. Biol. Chem. 210 (1954) 465-480. [PMID: 13201608]
4. Huang D.-Y., Furukawa, A. and Ichikawa, Y. Molecular cloning of retinal oxidase/aldehyde oxidase cDNAs from rabbit and mouse livers and functional expression of recombinant mouse retinal oxidase cDNA in Escherichia coli. Arch. Biochem. Biophys. 364 (1999) 264-272. [PMID: 10190983]
5. Uchida, H., Kondo, D., Yamashita, A., Nagaosa, Y., Sakurai, T., Fujii, Y., Fujishiro, K., Aisaka, K. and Uwajima, T. Purification and characterization of an aldehyde oxidase from Pseudomonas sp. KY 4690. FEMS Microbiol. Lett. 229 (2003) 31-36. [PMID: 14659539]
Common name: indole-3-acetaldehyde oxidase
Reaction: 2 indole-3-acetaldehyde + O2 = 2 indole-3-acetate + 2 H2O
Other name(s): indoleacetaldehyde oxidase
Systematic name: indole-3-acetaldehyde:oxygen oxidoreductase
Comments: A hemoprotein. Also oxidizes indole-3-aldehyde and acetaldehyde, but more slowly. The enzyme from maize contains FAD, iron and molybdenum [4].
Links to other databases: BRENDA, EXPASY, KEGG, ERGO, CAS registry number: 66082-22-2
References:
1. Bower, P.J., Brown, H.M. and Purves, W.K. Cucumber seedling indoleacetaldehyde oxidase. Plant Physiol. 61 (1978) 107-110.
2. Miyata, S., Suzuki, Y., Kamisaka, S. and Masuda, Y. Indole-3-acetaldehyde oxidase of pea-seedlings. Physiol. Plant. 51 (1981) 402-406.
3. Rajagopal, R. Metabolism of indole-3-acetaldehyde. III. Some characteristics of the aldehyde oxidase of Avena coleoptiles. Physiol. Plant. 24 (1971) 272-281.
4. Koshiba, T., Saito, E., Ono, N., Yamamoto, N. and Sato, M. Purification and properties of flavin- and molybdenum-containing aldehyde oxidase from coleoptiles of maize. Plant Physiol. 110 (1996) 781-789. [PMID: 12226218]
Common name: aldehyde dehydrogenase (FAD-independent)
Reaction: an aldehyde + H2O + acceptor = a carboxylate + reduced acceptor
Other name(s): aldehyde oxidase; aldehyde oxidoreductase; Mop; AORDd
Systematic name: aldehyde:acceptor oxidoreductase (FAD-independent)
Comments: Belongs to the xanthine oxidase family of enzymes. The enzyme from Desulfovibrio sp. contains a molybdenum-molybdopterin-cytosine dinucleotide (MCD) complex and two types of [2Fe-2S] cluster per monomer, but does not contain FAD.
References:
1. Uchida, H., Kondo, D., Yamashita, A., Nagaosa, Y., Sakurai, T., Fujii, Y., Fujishiro, K., Aisaka, K. and Uwajima, T. Purification and characterization of an aldehyde oxidase from Pseudomonas sp. KY 4690. FEMS Microbiol. Lett. 229 (2003) 31-36. [PMID: 14659539]
2. Duarte, R.O., Archer, M., Dias, J.M., Bursakov, S., Huber, R., Moura, I., Romao, M.J. and Moura, J.J. Biochemical/spectroscopic characterization and preliminary X-ray analysis of a new aldehyde oxidoreductase isolated from Desulfovibrio desulfuricans ATCC 27774. Biochem. Biophys. Res. Commun. 268 (2000) 745-749. [PMID: 10679276]
3. Andrade, S.L., Brondino, C.D., Feio, M.J., Moura, I. and Moura, J.J. Aldehyde oxidoreductase activity in Desulfovibrio alaskensis NCIMB 13491. EPR assignment of the proximal [2Fe-2S] cluster to the Mo site. Eur. J. Biochem. 267 (2000) 2054-2061. [PMID: 10727945]
4. Romao, M.J., Archer, M., Moura, I., Moura, J.J., LeGall, J., Engh, R., Schneider, M., Hof, P. and Huber, R. Crystal structure of the xanthine oxidase-related aldehyde oxido-reductase from D. gigas. Science 270 (1995) 1170-1176. [PMID: 7502041]
Common name: 1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase
Reaction: (1R,6R)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate + NAD+ = catechol + CO2 + NADH + H+
Other name(s): 3,5-cyclohexadiene-1,2-diol-1-carboxylate dehydrogenase; 3,5-cyclohexadiene-1,2-diol-1-carboxylic acid dehydrogenase; dihydrodihydroxybenzoate dehydrogenase; DHBDH; cis-1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate dehydrogenase; 2-hydro-1,2-dihydroxybenzoate dehydrogenase; cis-1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate:NAD+ oxidoreductase; dihydrodihydroxybenzoate dehydrogenase
Systematic name: (1R,6R)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate:NAD+ oxidoreductase (decarboxylating)
Links to other databases: BRENDA, EXPASY, KEGG, ERGO, CAS registry number: 60496-16-4, 146888-20-2 and 146888-19-9
References:
1. Reiner, A.M. Metabolism of aromatic compounds in bacteria. Purification and properties of the catechol-forming enzyme, 3,5-cyclohexadiene-1,2-diol-1-carboxylic acid (NAD+) oxidoreductase (decarboxylating). J. Biol. Chem. 247 (1972) 4960-4965. [PMID: 4341530]
2. Neidle, E.L., Hartnett, C., Ornston, N.L., Bairoch, A., Rekik, M. and Harayama, S. cis-Diol dehydrogenases encoded by the TOL pWW0 plasmid xylL gene and the Acinetobacter calcoaceticus chromosomal benD gene are members of the short-chain alcohol dehydrogenase superfamily. Eur. J. Biochem. 204 (1992) 113-120. [PMID: 1740120]
[EC 1.3.1.55 Deleted entry: cis-1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate dehydrogenase. Enzyme is identical to EC 1.3.1.25, 1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (EC 1.3.1.55 created 1999, deleted 2004)]
[EC 1.5.1.13 Transferred entry: now EC 1.17.1.5, nicotinate dehydrogenase. The enzyme was incorrectly classified as acting on a CH-NH group. (EC 1.5.1.13 created 1972, deleted 2004)].
Common name: methylenetetrahydromethanopterin dehydrogenase
Reaction: 5,10-methylenetetrahydromethanopterin + coenzyme F420 = 5,10-methenyltetrahydromethanopterin + reduced coenzyme F420
For diagram of reaction click here
Glossary: coenzyme F420
tetrahydromethanopterin
Other name(s): N5,N10-methylenetetrahydromethanopterin dehydrogenase; 5,10-methylenetetrahydromethanopterin dehydrogenase
Systematic name: 5,10-methylenetetrahydromethanopterin:coenzyme-F420 oxidoreductase
Comments: Coenzyme F420 is a 7,8-didemethyl-8-hydroxy-5-deazariboflavin derivative; methanopterin is a pterin analogue. The enzyme is involved in the formation of methane from CO2 in Methanobacterium thermoautotrophicum.
Links to other databases: BRENDA, EXPASY, KEGG, UM-BBD, ERGO, CAS registry number: 100357-01-5
References:
1. Hartzell, P.L., Zvilius, G., Escalante-Semerena, J.C. and Donnelly, M.I. Coenzyme F420 dependence of the methylenetetrahydromethanopterin dehydrogenase of Methanobacterium thermoautotrophicum. Biochem. Biophys. Res. Commun. 133 (1985) 884-890. [PMID: 4084309]
2. te Brömmelstroet, B.W., Geerts, W.J., Keltjens, J.T., van der Drift, C. and Vogels, G.D. Purification and properties of 5,10-methylenetetrahydromethanopterin dehydrogenase and 5,10-methylenetetrahydromethanopterin reductase, two coenzyme F420-dependent enzymes, from Methanosarcina barkeri. Biochim. Biophys. Acta 1079 (1991) 293-302. [PMID: 1911853]
Common name: 5,10-methylenetetrahydromethanopterin reductase
Reaction: 5-methyltetrahydromethanopterin + coenzyme F420 = 5,10-methylenetetrahydromethanopterin + reduced coenzyme F420
For diagram of reaction click here.
Glossary: coenzyme F420
tetrahydromethanopterin
Other name(s): 5,10-methylenetetrahydromethanopterin cyclohydrolase; 5,10-methylenetetrahydromethanopterin reductase; N5,N10-methylenetetrahydromethanopterin reductase; methylene-H4MPT reductase; coenzyme F420-dependent N5,N10-methenyltetrahydromethanopterin reductase; N5,N10-methylenetetrahydromethanopterin:coenzyme-F420 oxidoreductase
Systematic name: 5-methyltetrahydromethanopterin:coenzyme-F420 oxidoreductase
Comments: Catalyses an intermediate step in methanogenesis from CO2 and H2 in bacteria.
Links to other databases: BRENDA, EXPASY, KEGG, UM-BBD, ERGO, CAS registry number:
References:
1. Ma, K. and Thauer, R.K. Purification and properties of N5,N10-methylenetetrahydromethanopterin reductase from Methanobacterium thermoautotrophicum (strain Marburg). Eur. J. Biochem. 191 (1990) 187-193. [PMID: 2379499]
2. te Brömmelstroet, B.W., Geerts, W.J., Keltjens, J.T., van der Drift, C. and Vogels, G.D. Purification and properties of 5,10-methylenetetrahydromethanopterin dehydrogenase and 5,10-methylenetetrahydromethanopterin reductase, two coenzyme F420-dependent enzymes, from Methanosarcina barkeri. Biochim. Biophys. Acta 1079 (1991) 293-302. [PMID: 1911853]
3. Ma, K. and Thauer, R.K. Single step purification of methylenetetrahydromethanopterin reductase from Methanobacterium thermoautotrophicum by specific binding to blue sepharose CL-6B. FEBS Lett. 268 (1990) 59-62. [PMID: 1696553]
4. te Brömmelstroet, B.W., Hensgens, C.M., Keltjens, J.T., van der Drift, C. and Vogels, G.D. Purification and properties of 5,10-methylenetetrahydromethanopterin reductase, a coenzyme F420-dependent enzyme, from Methanobacterium thermoautotrophicum strain δH*. J. Biol. Chem. 265 (1990) 1852-1857 [PMID: 2298726]
5. te Brömmelstroet, B.W., Hensgens, C.M., Geerts, W.J., Keltjens, J.T., van der Drift, C. and Vogels, G.D. Purification and properties of 5,10-methenyltetrahydromethanopterin cyclohydrolase from Methanosarcina barkeri. J. Bacteriol. 172 (1990) 564-571 PMID: 2298699]
Common name: 5,10-methenyltetrahydromethanopterin hydrogenase
Reaction: H2 + 5,10-methenyltetrahydromethanopterin = H+ + 5,10-methylenetetrahydromethanopterin
Other name(s): H2-forming N5,N10-methylenetetrahydromethanopterin dehydrogenase; nonmetal hydrogenase; N5,N10-methenyltetrahydromethanopterin hydrogenase; hydrogen:N5,N10-methenyltetrahydromethanopterin oxidoreductase
Systematic name: hydrogen:5,10-methenyltetrahydromethanopterin oxidoreductase
Comments: Does not catalyse the reduction of artificial dyes. Does not by itself catalyse a H2/H+ exchange reaction. Does not contain nickel or iron-sulfur clusters.
Links to other databases: BRENDA, EXPASY, KEGG, ERGO, CAS registry number: 100357-01-5
References:
1. Zirngibl, C., Hedderich, R. and Thauer, R.K. N5,N10-Methylenetetrahydromethanopterin dehydrogenase from Methanobacterium thermoautotrophicum has hydrogenase activity. FEBS Lett. 261 (1990) 112-116.
2. Klein, A., Fernandez, V.M. and Thauer, R.K. H2-Forming N5,N10-methylenetetrahydromethanopterin dehydrogenase: mechanism of H2-formation analyzed using hydrogen isotopes. FEBS Lett. 368 (1995) 203-206. [PMID: 7628605]
Common name: Renilla-luciferin 2-monooxygenase
Reaction: Renilla luciferin + O2 = oxidized Renilla luciferin + CO2 + hν
For diagram click here
Glossary: Renilla luciferin = 2,8-dibenzyl-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one
Other name(s): Renilla-type luciferase; aequorin; luciferase (Renilla luciferin)
Systematic name: Renilla-luciferin:oxygen 2-oxidoreductase (decarboxylating)
Comments: From the soft coral coelenterate Renilla reniformis. The luciferin is bound to a luciferin-binding protein (BP-LH2). The bioluminescent reaction between the luciferin complex, luciferase and oxygen is triggered by calcium ions. In vivo, the excited state luciferin—luciferase complex undergoes the process of nonradiative energy transfer to an accessory protein, Renilla green fluorescent protein, which results in green bioluminescence. In vitro, Renilla luciferase emits blue light in the absence of any green fluorescent protein.
Links to other databases: BRENDA, EXPASY, KEGG, ERGO, CAS registry number: 61869-41-8
References:
1. Cormier, M.J., Hori, K. and Anderson, J.M. Bioluminescence in coelenterates. Biochim. Biophys. Acta 346 (1974) 137-164. [PMID: 4154104]
2. Hori, K., Anderson, J.M., Ward, W.W. and Cormier, M.J. Renilla luciferin as the substrate for calcium induced photoprotein bioluminescence. Assignment of luciferin tautomers in aequorin and mnemiopsin. Biochemistry 14 (1975) 2371-2376. [PMID: 237531]
3. Shimomura, O. and Johnson, F.H. Chemical nature of bioluminescence systems in coelenterates. Proc. Natl. Acad. Sci. USA 72 (1975) 1546-1549. [PMID: 236561]
4. Charbonneau, H. and Cormier, M.J. Ca2+-induced bioluminescence in Renilla reniformis. Purification and characterization of a calcium-triggered luciferin-binding protein. J. Biol. Chem. 254 (1979) 769-780. [PMID: 33174]
5. Anderson, J.M., Charbonneau, H. and Cormier, M.J. Mechanism of calcium induction of Renilla bioluminescence. Involvement of a calcium-triggered luciferin binding protein. Biochemistry 13 (1974) 1195-1200. [PMID: 4149963]
6. Lorenz, W.W., McCann, R.O., Longiaru, M. and Cormier, M.J. Isolation and expression of a cDNA encoding Renilla reniformis luciferase. Proc. Natl. Acad. Sci. USA 88 (1991) 4438-4442. [PMID: 1674607]
Common name: Oplophorus-luciferin 2-monooxygenase
Reaction: Oplophorus luciferin + O2 = oxidized Oplophorus luciferin + CO2 + hν
For diagram click here.
Glossary: Oplophorus luciferin = 8-benzyl-2-(4-hydroxybenzyl)-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one
Other name(s): Oplophorus luciferase
Systematic name: Oplophorus-luciferin:oxygen 2-oxidoreductase (decarboxylating)
Comments: The luciferase from the deep sea shrimp Oplophorus gracilorostris is a complex composed of more than one protein. The enzyme's specificity is quite broad, with both coelenterazine and bisdeoxycoelenterazine being good substrates.
References:
1. Shimomura, O., Masugi, T., Johnson, F.H. and Haneda, Y. Properties and reaction mechanism of the bioluminescence system of the deep-sea shrimp Oplophorus gracilorostris. Biochemistry 17 (1978) 994-998. [PMID: 629957]
2. Inouye, S., Watanabe, K., Nakamura, H., Shimomura, O. Secretional luciferase of the luminous shrimp Oplophorus gracilirostris: cDNA cloning of a novel imidazopyrazinone luciferase. FEBS Lett. 481 (2000) 19-25. [PMID: 10984608]
Common name: cyclohexanone monooxygenase
Reaction: cyclohexanone + NADPH + H+ + O2 = hexano-6-lactone + NADP+ + H2O
For diagram of reaction click here.
Other name(s): cyclohexanone 1,2-monooxygenase; cyclohexanone oxygenase; cyclohexanone:NADPH:oxygen oxidoreductase (6-hydroxylating, 1,2-lactonizing)
Systematic name: cyclohexanone,NADPH:oxygen oxidoreductase (lactone-forming)
Comments: A flavoprotein (FAD). In the catalytic mechanism of this enzyme, the nucleophilic species that attacks the carbonyl group is a peroxyflavin intermediate that is generated by reaction of the enzyme-bound flavin cofactor with NAD(P)H and oxygen [2]. This enzyme is able to catalyse a wide range of oxidative reactions, including enantioselective Baeyer-Villiger reactions [3], sulfoxidations [4], amine oxidations [5] and epoxidations [6].
Links to other databases: BRENDA, EXPASY, KEGG, UM-BBD, ERGO, CAS registry number: 52037-90-8 and 59088-27-6
References:
1. Donoghue, N.A., Morris, D.B. and Trudgill, P.W. The purification and properties of cyclohexanone oxygenase from Nocardia globerula CL1 and Acinetobacter NCIB 9871. Eur. J. Biochem. 63 (1976) 175-192. [PMID: 1261545]
2. Sheng, D., Ballou, D.P. and Massey, V. Mechanistic studies of cyclohexanone monooxygenase: chemical properties of intermediates involved in catalysis. Biochemistry 40 (2001) 11156-11167. [PMID: 11551214]
3. Stewart, J.D. Cyclohexanone monooxygenase: a useful reagent for asymmetric Baeyer-Villiger reactions. Curr. Org. Chem. 2 (1998) 195-216.
4. Chen, G., Kayser, M.M., Milhovilovic, M.D., Mrstik, M.E., Martinez, C.A. and Stewart, J.D. Asymmetric oxidations at sulfur catalyzed by engineered strains that overexpress cyclohexanone monooxygenase. New J. Chem. 23 (1999) 827-832.
5. Ottolina, G., Bianchi, S., Belloni, B., Carrea, G. and Danieli, B. First asymmetric oxidation of tertiary amines by cyclohexanone monooxygenase. Tetrahedron Lett. 40 (1999) 8483-8486.
6. Colonna, S., Gaggero, N., Carrea, G., Ottolina, G., Pasta, P. and Zambianchi, F. First asymmetric epoxidation catalysed by cyclohexanone monooxygenase. Tetrahedron Lett. 43 (2002) 1797-1799. [PMID: ]
Common name: 4-hydroxyacetophenone monooxygenase
Reaction: (4-hydroxyphenyl)ethan-1-one + NADPH + H+ + O2 = 4-hydroxyphenyl acetate + NADP+ + H2O
For diagram of reaction click here.
Other name(s): HAPMO
Systematic name: (4-hydroxyphenyl)ethan-1-one,NADPH:oxygen oxidoreductase (ester-forming)
Comments: Contains FAD. The enzyme from Pseudomonas fluorescens ACB catalyses the conversion of a wide range of acetophenone derivatives. Highest activity occurs with compounds bearing an electron-donating substituent at the para position of the aromatic ring [1]. In the absence of substrate, the enzyme can act as an NADPH oxidase (EC 1.6.3.1).
References:
1. Kamerbeek, N.M., Moonen, M.J., van der Ven, J.G., van Berkel, W.J.H., Fraaije, M.W. and Janssen, D.B. 4-Hydroxyacetophenone monooxygenase from Pseudomonas fluorescens ACB: a novel flavoprotein catalyzing Baeyer-Villiger oxidation of aromatic compounds. Eur. J. Biochem. 268 (2001) 2547-2557. [PMID: 11322873 ]
2. Kamerbeek, N.M, Olsthoorn, A.J.J., Fraaije, M.W. and Janssen, D.B. Substrate specificity of a novel Baeyer-Villiger monooxygenase, 4-hydroxyacetophenone monooxygenase. Appl. Environ. Microbiol. 69 (2003) 419-426. [PMID: 12514023]
*EC 1.17 Acting on CH or CH2 groups
Common name: xanthine dehydrogenase
Reaction: xanthine + NAD+ + H2O = urate + NADH + H+
For diagram of reaction click here.
Glossary: 4-mercuribenzoate = (4-carboxylatophenyl)mercury
Other name(s): NAD-xanthine dehydrogenase; xanthine-NAD oxidoreductase; xanthine/NAD+ oxidoreductase; xanthine oxidoreductase
Systematic name: xanthine:NAD+ oxidoreductase
Comments: Acts on a variety of purines and aldehydes, including hypoxanthine. The enzyme from eukaryotes contains [2Fe-2S], FAD and a molybdenum centre. The animal enzyme can be interconverted to EC 1.17.3.2, xanthine oxidase (the oxidase form). That from liver exists in vivo mainly in the dehydrogenase form, but can be converted into EC 1.17.3.2 by storage at -20 °C, by treatment with proteolytic agents or organic solvents, or by thiol reagents such as Cu2+, N-ethylmaleamide or 4-mercuribenzoate. The effect of thiol reagents can be reversed by thiols such as 1,4-dithioerythritol. This enzyme can also be converted into EC 1.17.3.2 by EC 1.8.4.7, enzyme-thiol transhydrogenase (glutathione-disulfide) in the presence of glutathione disulfide. In other animal tissues, the enzyme exists almost entirely as EC 1.17.3.2, but can be converted into the dehydrogenase form by 1,4-dithioerythritol. Formerly EC 1.2.1.37 and EC 1.1.1.204.
References:
1. Battelli, M.G. and Lorenzoni, E. Purification and properties of a new glutathione-dependent thiol:disulphide oxidoreductase from rat liver. Biochem. J. 207 (1982) 133-138. [PMID: 6960894]
2. Della Corte, E. and Stirpe, F. The regulation of rat liver xanthine oxidase. Involvement of thiol groups in the conversion of the enzyme activity from dehydrogenase (type D) into oxidase (type O) and purification of the enzyme. Biochem. J. 126 (1972) 739-745. [PMID: 4342395]
3. Parzen, S.D. and Fox, A.S. Purification of xanthine dehydrogenase from Drosophila melanogaster. Biochim. Biophys. Acta 92 (1964) 465-471.
4. Rajagopalan, K.V. and Handler, P. Purification and properties of chicken liver xanthine dehydrogenase. J. Biol. Chem. 242 (1967) 4097-4107. [PMID: 4294045]
5. Smith, S.T., Rajagopalan, K.V. and Handler, P. Purification and properties of xanthine dehydroganase from Micrococcus lactilyticus. J. Biol. Chem. 242 (1967) 4108-4117. [PMID: 6061702]
6. Parschat, K., Canne, C., Hüttermann, J., Kappl, R. and Fetzner, S. Xanthine dehydrogenase from Pseudomonas putida 86: specificity, oxidation-reduction potentials of its redox-active centers, and first EPR characterization. Biochim. Biophys. Acta 1544 (2001) 151-165. [PMID: 11341925]
7. Ichida, K., Amaya, Y., Noda, K., Minoshima, S., Hosoya, T., Sakai, O., Shimizu, N. and Nishino, T. Cloning of the cDNA encoding human xanthine dehydrogenase (oxidase): structural analysis of the protein and chromosomal location of the gene. Gene 133 (1993) 279-284. [PMID: 8224915]
8. Enroth, C., Eger, B.T., Okamoto, K., Nishino, T., Nishino, T. and Pai, E.F. Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: structure-based mechanism of conversion. Proc. Natl. Acad. Sci. USA 97 (2000) 10723-10728. [PMID: 11005854]
9. Truglio, J.J., Theis, K., Leimkuhler, S., Rappa, R., Rajagopalan, K.V. and Kisker, C. Crystal structures of the active and alloxanthine-inhibited forms of xanthine dehydrogenase from Rhodobacter capsulatus. Structure 10 (2002) 115-125. [PMID: 11796116]
10. Hille, R. The mononuclear molybdenum enzymes. Chem. Rev. 96 (1996) 2757-2816. [PMID: 11848841]
Common name: nicotinate dehydrogenase
Reaction: nicotinate + H2O + NADP+ = 6-hydroxynicotinate + NADPH + H+
Other name(s): nicotinic acid hydroxylase; nicotinate hydroxylase
Systematic name: nicotinate:NADP+ 6-oxidoreductase (hydroxylating)
Comments: A flavoprotein containing non-heme iron. The enzyme is capable of acting on a variety of nicotinate analogues to varying degrees, including pyrazine-2-carboxylate, pyrazine 2,3-dicarboxylate, trigonelline and 6-methylnicotinate. The enzyme from Clostridium barkeri also possesses a catalytically essential, labile selenium that can be removed by reaction with cyanide.
Links to other databases: BRENDA, EXPASY, KEGG, ERGO, CAS registry number: 9059-03-4
References:
1. Holcenberg, J.S. and Stadtman, E.R. Nicotinic acid metabolism. 3. Purification and properties of a nicotinic acid hydroxylase. J. Biol. Chem. 244 (1969) 1194-1203. [PMID: 4388026]
2. Gladyshev, V.N., Khangulov, S.V. and Stadtman, T.C. Properties of the selenium- and molybdenum-containing nicotinic acid hydroxylase from Clostridium barkeri. Biochemistry 35 (1996) 212-223. [PMID: 8555176]
3. Gladyshev, V.N., Khangulov, S.V. and Stadtman, T.C. Nicotinic-acid hydroxylase from Clostridium barkeri - electron-paramagnetic-resonance studies show that selenium is coordinated with molybdenum in the catalytically active selenium-dependent enzyme. Proc. Natl. Acad. Sci. USA 91 (1994) 232-236. [PMID: 8278371]
4. Dilworth, G.L. Occurrence of molybdenum in the nicotinic-acid hydroxylase from Clostridium barkeri. Arch. Biochem. Biophys. 221 (1983) 565-569. [PMID: 6838209]
5. Dilworth, G.L. Properties of the selenium-containing moiety of nicotinic-acid hydroxylase from Clostridium barkeri. Arch. Biochem. Biophys. 219 (1983) 30-38.
6. Nagel, M. and Andreesen, J.R. Purification and characterization of the molybdoenzymes nicotinate dehydrogenase and 6-hydroxynicotinate dehydrogenase from Bacillus niacini. Arch. Microbiol. 154 (1990) 605-613.
Common name: xanthine oxidase
Reaction: xanthine + H2O + O2 = urate + H2O2
For reaction pathway click here.
Glossary: 4-mercuribenzoate = (4-carboxylatophenyl)mercury
Other name(s): hypoxanthine oxidase; hypoxanthine:oxygen oxidoreductase; Schardinger enzyme; xanthine oxidoreductase; hypoxanthine-xanthine oxidase; xanthine:O2 oxidoreductase; xanthine:xanthine oxidase
Systematic name: xanthine:oxygen oxidoreductase
Comments: An iron-molybdenum flavoprotein (FAD) containing [2Fe-2S] centres. Also oxidizes hypoxanthine, some other purines and pterins, and aldehydes (i.e. possesses the activity of EC 1.2.3.1, aldehyde oxidase). Under some conditions the product is mainly superoxide rather than peroxide: R-H + H2O + 2 O2 = ROH + 2 O2•- + 2 H+. The enzyme from animal tissues can be converted into EC 1.17.1.4, xanthine dehydrogenase. That from liver exists in vivo mainly as the dehydrogenase form, but can be converted into the oxidase form by storage at -20 °C, by treatment with proteolytic enzymes or with organic solvents, or by thiol reagents such as Cu2+, N-ethylmaleamide or 4-mercuribenzoate. The effect of thiol reagents can be reversed by thiols such as 1,4-dithioerythritol. EC 1.17.1.4 can also be converted into this enzyme by EC 1.8.4.7, enzyme-thiol transhydrogenase (oxidized-glutathione) in the presence of glutathione disulfide. The Micrococcus enzyme can use ferredoxin as acceptor.
Links to other databases: BRENDA, EXPASY, KEGG, ERGO, CAS registry number: 9002-17-9
References:
1. Avis, P.G., Bergel, F. and Bray, R.C. Cellular constituents. The chemistry of xanthine oxidase. Part I. The preparation of a crystalline xanthine oxidase from cow's milk. J. Chem. Soc. (Lond.) (1955) 1100-1105.
2. Battelli, M.G. and Lorenzoni, E. Purification and properties of a new glutathione-dependent thiol:disulphide oxidoreductase from rat liver. Biochem. J. 207 (1982) 133-138. [PMID: 6960894]
3. Bray, R.C. Xanthine oxidase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd ed., vol. 7, Academic Press, New York, 1963, pp. 533-556.
4. Della Corte, E. and Stirpe, F. The regulation of rat liver xanthine oxidase. Involvement of thiol groups in the conversion of the enzyme activity from dehydrogenase (type D) into oxidase (type O) and purification of the enzyme. Biochem. J. 126 (1972) 739-745. [PMID: 4342395]
5. Carpani, G., Racchi, M., Ghezzi, P., Terao, M. and Garattini, E. Purification and characterization of mouse liver xanthine oxidase. Arch. Biochem. Biophys. 279 (1990) 237-241. [PMID: 2350174]
6. Eger, B.T., Okamoto, K., Enroth, C., Sato, M., Nishino, T., Pai, E.F. and Nishino, T. Purification, crystallization and preliminary X-ray diffraction studies of xanthine dehydrogenase and xanthine oxidase isolated from bovine milk. Acta Crystallogr. D Biol. Crystallogr. 56 (2000) 1656-1658. [PMID: 11092937]
Common name: 6-hydroxynicotinate dehydrogenase
Reaction: 6-hydroxynicotinate + H2O + O2 = 2,6-dihydroxynicotinate + H2O2
Other name(s): 6-hydroxynicotinic acid hydroxylase; 6-hydroxynicotinic acid dehydrogenase; 6-hydroxynicotinate hydroxylase
Systematic name: 6-hydroxynicotinate:O2 oxidoreductase
Comments: Contains [2Fe-2S] iron-sulfur centres, FAD and molybdenum. It also has a catalytically essential, labile selenium that can be removed by reaction with cyanide. In Bacillus niacini, this enzyme is required for growth on nicotinic acid.
References:
1. Nagel, M. and Andreesen, J.R. Molybdenum-dependent degradation of nicotinic acid by Bacillus sp. DSM 2923. FEMS Microbiol. Lett. 59 (1989) 147-152.
2. Nagel, M. and Andreesen, J.R. Purification and characterization of the molybdoenzymes nicotinate dehydrogenase and 6-hydroxynicotinate dehydrogenase from Bacillus niacini. Arch. Microbiol. 154 (1990) 605-613.
EC 1.17.5 With a quinone or similar compound as acceptor
Common name: phenylacetyl-CoA dehydrogenase
Reaction: phenylacetyl-CoA + H2O + 2 quinone = phenylglyoxylyl-CoA + 2 quinol
For diagram of reaction click here.
Other name(s): phenylacetyl-CoA:acceptor oxidoreductase
Systematic name: phenylacetyl-CoA:quinone oxidoreductase
Comments: The enzyme from Thauera aromatica is a membrane-bound molybdenum—iron—sulfur protein. The enzyme is specific for phenylacetyl-CoA as substrate. Phenylacetate, acetyl-CoA, benzoyl-CoA, propionyl-CoA, crotonyl-CoA, succinyl-CoA and 3-hydroxybenzoyl-CoA cannot act as substrates. The oxygen atom introduced into the product, phenylglyoxylyl-CoA, is derived from water and not molecular oxygen. Duroquinone, menaquinone and 2,6-dichlorophenolindophenol (DCPIP) can act as acceptor, but the likely physiological acceptor is ubiquinone [1]. A second enzyme, EC 3.1.2.25, phenylglyoxylyl-CoA hydrolase, converts the phenylglyoxylyl-CoA formed into phenylglyoxylate.
References:
1. Rhee, S.K. and Fuchs, G. Phenylacetyl-CoA:acceptor oxidoreductase, a membrane-bound molybdenum-iron-sulfur enzyme involved in anaerobic metabolism of phenylalanine in the denitrifying bacterium Thauera aromatica. Eur. J. Biochem. 262 (1999) 507-515. [PMID: 10336636]
2. Schneider, S. and Fuchs, G. Phenylacetyl-CoA:acceptor oxidoreductase, a new α-oxidizing enzyme that produces phenylglyoxylate. Assay, membrane localization, and differential production in Thauera aromatica. Arch. Microbiol. 169 (1998) 509-516. [PMID: 9575237]
Common name: sucrose:sucrose fructosyltransferase
Reaction: 2 sucrose = D-glucose + β-D-fructofuranosyl-(21)-β-D-fructofuranosyl α-D-glucopyranoside
Other name(s): SST; sucrose:sucrose 1-fructosyltransferase; sucrose-sucrose 1-fructosyltransferase; sucrose 1F-fructosyltransferase; sucrose:sucrose 1F-β-D-fructosyltransferase
Systematic name: sucrose:sucrose 1'-β-D-fructosyltransferase
For definition of the prime in the systematic name, see 2-Carb-36.2
Comments:
Links to other databases: BRENDA, EXPASY, KEGG, ERGO, CAS registry number: 73379-56-3
References:
1. Henry, R.J. and Darbyshire, B. Sucrose:sucrose fructosyltransferase and fructan:fructan fructosyltransferase from Allium cepa. Phytochemistry 19 (1980) 1017-1020.
2. Lüscher, M., Hochstrasser, U., Vogel, G., Aeschbacher, R., Galati, V., Nelson, C.J., Boller, T. and Wiemken, A. Cloning and functional analysis of sucrose:sucrose 1-fructosyltransferase from tall fescue. Plant Physiol 124 (2000) 1217-1228. [PMID: 11080298]
Common name: 2,1-fructan:2,1-fructan 1-fructosyltransferase
Reaction: [β-D-fructosyl-(21)-]m + [β-D-fructosyl-(21)-]n = [β-D-fructosyl-(21)-]m-1 + [β-D-fructosyl-(21)-]n+1
Other name(s): 1,2-β-D-fructan 1F-fructosyltransferase; fructan:fructan fructosyl transferase; FFT; 1,2-β-fructan 1F-fructosyltransferase; 1,2-β-D-fructan:1,2-β-D-fructan 1F-β-D-fructosyltransferase
Systematic name: 2,1-β-D-fructan:2,1-β-D-fructan 1-β-D-fructosyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, ERGO, CAS registry number: 73379-55-2
References:
1. Henry, R.J. and Darbyshire, B. Sucrose:sucrose fructosyltransferase and fructan:fructan fructosyltransferase from Allium cepa. Phytochemistry 19 (1980) 1017-1020.
2. Vergauwen, R., Van Laere, A. and Van den Ende, W. Properties of fructan:fructan 1-fructosyltransferases from chicory and globe thistle, two asteracean plants storing greatly different types of inulin.Plant Physiol. 133 (2003) 391-401. [PMID: 12970504]
Common name: initiation-specific α-1,6-mannosyltransferase
Reaction: Transfers an α-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an α-1,6-D-mannosyl-D-mannose linkage
Other name(s): α-1,6-mannosyltransferase; GDP-mannose:oligosaccharide 1,6-α-D-mannosyltransferase; GDP-mannose:glycolipid 1,6-α-D-mannosyltransferase; glycolipid 6-α-mannosyltransferase
Systematic name: GDP-mannose:oligosaccharide 1,6-α-D-mannosyltransferase
Comments: Requires Mn2+. In Saccharomyces cerevisiae, this enzyme catalyses an essential step in the outer chain elongation of N-linked oligosaccharides. Man8GlcNAc and Man9GlcNAc are equally good substrates.
CAS registry number: 346003-17-6
References:
1. Romero, P.A. and Herscovics, A. Glycoprotein biosynthesis in Saccharomyces cerevisiae. Characterization of α-1,6-mannosyltransferase which initiates outer chain formation. J. Biol. Chem. 264 (1989) 1946-1950. [PMID: 2644248]
2. Reason, A.J., Dell, A., Romero, P.A. and Herscovics, A. Specificity of the mannosyltransferase which initiates outer chain formation in Saccharomyces cerevisiae. Glycobiology 1 (1991) 387-391. [PMID: 1820199]
3. Nakanishi-Shindo, Y., Nakayama, K., Tanaka, A., Toda, Y. and Jigami, Y. Structure of the N-linked oligosaccharides that show the complete loss of α-1,6-polymannose outer chain from och1, och1 mnn1, and och1 mnn1 alg3 mutants of Saccharomyces cerevisiae. J. Biol. Chem. 268 (1993) 26338-26345. [PMID: 8253757]
4. Yamamoto, K., Okamoto, M., Yoko-o, T. and Jigami, Y. Salt stress induces the expression of the Schizosaccharomyces pombe och1+, which encodes an initiation-specific α-1,6-mannosyltransferase for N-linked outer chain synthesis of cell wall mannoproteins. Biosci. Biotechnol. Biochem. 67 (2003) 927-929. [PMID: 12784644]
5. Cui, Z., Horecka, J. and Jigami, Y. Cdc4 is involved in the transcriptional control of OCH1, a gene encoding α-1,6-mannosyltransferase in Saccharomyces cerevisiae. Yeast 19 (2002) 69-77. [PMID: 11754484]
6. Tsukahara, K., Watanabe, T., Yoko-o, T. and Chigami, Y. Schizosaccharomyces pombe och1+ gene encoding α-1,6-mannosyltransferase and use of och1+ gene knockout fission yeast for production of glycoproteins with reduced glycosylation. Jpn. Kokai Tokkyo Koho (2001) 11 pp.
7. Nakayama, K., Nakanishi-Shindo, Y., Tanaka, A., Haga-Toda, Y. and Jigami, Y. Substrate specificity of α-1,6-mannosyltransferase that initiates N-linked mannose outer chain elongation in Saccharomyces cerevisiae. FEBS Lett. 412 (1997) 547-550. [PMID: 9276464]
8. Suzuki, A., Shibata, N., Suzuki, M., Saitoh, F., Takata, Y., Oshie, A., Oyamada, H., Kobayashi, H., Suzuki, S. and Okawa, Y. Characterization of α-1,6-mannosyltransferase responsible for the synthesis of branched side chains in Candida albicans mannan. Eur. J. Biochem. 240 (1996) 37-44. [PMID: 8797833]
9. Yip, C.L., Welch, S.K., Klebl, F., Gilbert, T., Seidel, P., Grant, F., O'Hara, P.J. and MacKay, V.L. Cloning and analysis of the Saccharomyces cerevisiae MNN9 and MNN1 genes required for complex glycosylation of secreted proteins. Proc. Natl. Acad. Sci. USA 91 (1994) 2723-2727. [PMID: 8146181]
Common name: acetylornithine transaminase
Reaction: N2-acetyl-L-ornithine + 2-oxoglutarate = N-acetyl-L-glutamate 5-semialdehyde + L-glutamate
For diagram click here.
Other name(s): acetylornithine δ-transaminase; ACOAT; acetylornithine 5-aminotransferase; acetylornithine aminotransferase; N-acetylornithine aminotransferase; N-acetylornithine-δ-transaminase; N2-acetylornithine 5-transaminase; N2-acetyl-L-ornithine:2-oxoglutarate aminotransferase; succinylornithine aminotransferase
Systematic name: N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase
Comments: A pyridoxal-phosphate protein. Also acts on L-ornithine and N2-succinyl-L-ornithine.
Links to other databases: BRENDA, EXPASY, KEGG, ERGO, CAS registry number: 9030-40-4
References:
1. Albrecht, A. and Vogel, H.J. Acetylornithine δ-transaminase. Partial purification and repression behavior. J. Biol. Chem. 239 (1964) 1872-1876. [PMID: 14213368]
2. Vogel, H.J. Path of ornithine synthesis in Escherichia coli. Proc. Natl. Acad. Sci. USA 39 (1953) 578-583.
3. Van der Wauven, C. and Stalon, V. Occurrence of succinyl derivatives in the catabolism of arginine in Pseudomonas cepacia. J. Bacteriol. 164 (1985) 882-886. [PMID: 2865249]
4. Voellmy, R. and Leisinger, T. Dual role for N-2-acetylornithine 5-aminotransferase from Pseudomonas aeruginosa in arginine biosynthesis and arginine catabolism. J. Bacteriol. 122 (1975) 799-809. [PMID: 238949]
[EC 2.6.1.69 Deleted entry: N2-acetylornithine 5-transaminase. Enzyme is identical to EC 2.6.1.11, acetylornithine transaminase (EC 2.6.1.69 created 1989, deleted 2004)]
[EC 2.7.1.70 Deleted entry: protamine kinase. This enzyme is not dependent on cAMP as was thought and is therefore identical to EC 2.7.1.37, protein kinase. (EC 2.7.1.70 created 1972, deleted 2004)]
Common name: nucleoside-triphosphate-aldose-1-phosphate nucleotidyltransferase
Reaction: nucleoside triphosphate + α-D-aldose 1-phosphate = diphosphate + NDP-hexose
Other name(s): NDP hexose pyrophosphorylase; hexose 1-phosphate nucleotidyltransferase; hexose nucleotidylating enzyme; nucleoside diphosphohexose pyrophosphorylase; hexose-1-phosphate guanylyltransferase; GTP:α-D-hexose-1-phosphate guanylyltransferase; GDP hexose pyrophosphorylase; guanosine diphosphohexose pyrophosphorylase; nucleoside-triphosphate-hexose-1-phosphate nucleotidyltransferase; NTP:hexose-1-phosphate nucleotidyltransferase
Systematic name: NTP:α-D-aldose-1-phosphate nucleotidyltransferase
Comments: In decreasing order of activity, guanosine, inosine and adenosine diphosphate hexoses are substrates in the reverse reaction, with either glucose or mannose as the sugar.
Links to other databases: BRENDA, EXPASY, KEGG, ERGO, CAS registry number: 37278-26-5
References:
1. Verachtert, H., Rodriguez, P., Bass, S.T. and Hansen, R.G. Purification and properties of guanosine diphosphate hexose pyrophosphorylase from mammalian tissues. J. Biol. Chem. 241 (1966) 2007-2013. [PMID: 5946626]
2. Hansen, R.G., Verachtert, H., Rodriguez, P. and Bass, S.T. GDP-hexose pyrophosphorylase from liver. Methods Enzymol. 8 (1966) 269-271.
[EC 2.7.7.29 Deleted entry: hexose-1-phosphate guanylyltransferase. Enzyme is not specific for GTP and therefore is identical to EC 2.7.7.28, nucleoside-triphosphate-hexose-1-phosphate nucleotidyltransferase (EC 2.7.7.29 created 1972, deleted 2004)]
Common name: hormone-sensitive lipase
Reaction: (1) diacylglycerol + H2O = monoacylglycerol + a carboxylate
(2) triacylglycerol + H2O = diacylglycerol + a carboxylate
(3) monoacylglycerol + H2O = glycerol + a carboxylate
Other name(s): HSL
Systematic name: diacylglycerol acylhydrolase
Comments: This enzyme is a serine hydrolase. Compared with other lipases, hormone-sensitive lipase has a uniquely broad substrate specificity. It hydrolyses all acylglycerols (triacylglycerol, diacylglycerol and monoacylglycerol) [2,3,4] as well as cholesteryl esters [2,4], steroid fatty acid esters [5], retinyl esters [6] and p-nitrophenyl esters [4,7]. It exhibits a preference for the 1- or 3-ester bond of its acylglycerol substrate compared with the 2-ester bond [8]. The enzyme shows little preference for the fatty acids in the triacylglycerol, although there is some increase in activity with decreasing chain length. The enzyme activity is increased in response to hormones that elevate intracellular levels of cAMP.
References:
1. Holm, C., Osterlund, T., Laurell, H. and Contreras, J.A. Molecular mechanisms regulating hormone-sensitive lipase and lipolysis. Annu. Rev. Nutr. 20 (2000) 365-393. [PMID: 10940339]
2. Fredrikson, G., Stralfors, P., Nilsson, N.O. and Belfrage, P. Hormone-sensitive lipase of rat adipose tissue. Purification and some properties. J. Biol. Chem. 256 (1981) 6311-6320. [PMID: 7240206]
3. Vaughan, M., Berger, J.E. and Steinberg, D. Hormone-sensitive lipase and monoglyceride lipase activities in adipose tissue. J. Biol. Chem. 239 (1964) 401-409. [PMID: 14169138]
4. Østerlund, T., Danielsson, B., Degerman, E., Contreras, J.A., Edgren, G., Davis, R.C., Schotz, M.C. and Holm, C. Domain-structure analysis of recombinant rat hormone-sensitive lipase. Biochem. J. 319 (1996) 411-420. [PMID: 8912675]
5. Lee, F.T., Adams, J.B., Garton, A.J. and Yeaman, S.J. Hormone-sensitive lipase is involved in the hydrolysis of lipoidal derivatives of estrogens and other steroid hormones. Biochim. Biophys. Acta 963 (1988) 258-264. [PMID: 3196730]
6. Wei, S., Lai, K., Patel, S., Piantedosi, R., Shen, H., Colantuoni, V., Kraemer, F.B. and Blaner, W.S. Retinyl ester hydrolysis and retinol efflux from BFC-1β adipocytes. J. Biol. Chem. 272 (1977) 14159-14165. [PMID: 9162045]
7. Tsujita, T., Ninomiya, H. and Okuda, H. p-Nitrophenyl butyrate hydrolyzing activity of hormone-sensitive lipase from bovine adipose tissue. J. Lipid Res. 30 (1989) 997-1004. [PMID: 2794798]
8. Yeaman, S.J. Hormone-sensitive lipase - new roles for an old enzyme. Biochem. J. 379 (2004) 11-22. [PMID: 14725507]
Common name: phenylacetyl-CoA hydrolase
Reaction: phenylglyoxylyl-CoA + H2O = phenylglyoxylate + CoA
For diagram of reaction click here.
Systematic name: phenylglyoxylyl-CoA hydrolase
Comments: This is the second step in the conversion of phenylacetyl-CoA to phenylglyoxylate, the first step being carried out by EC 1.17.5.1, phenylacetyl-CoA dehydrogenase.
References:
1. Rhee, S.K. and Fuchs, G. Phenylacetyl-CoA:acceptor oxidoreductase, a membrane-bound molybdenum-iron-sulfur enzyme involved in anaerobic metabolism of phenylalanine in the denitrifying bacterium Thauera aromatica. Eur. J. Biochem. 262 (1999) 507-515. [PMID: 10336636]
2. Schneider, S. and Fuchs, G. Phenylacetyl-CoA:acceptor oxidoreductase, a new α-oxidizing enzyme that produces phenylglyoxylate. Assay, membrane localization, and differential production in Thauera aromatica. Arch. Microbiol. 169 (1998) 509-516. [PMID: 9575237]
Common name: NAD+ nucleosidase
Reaction: NAD+ + H2O = ADP-ribose + nicotinamide
Other name(s): NADase; DPNase; DPN hydrolase; NAD hydrolase; diphosphopyridine nucleosidase; nicotinamide adenine dinucleotide nucleosidase; NAD glycohydrolase; NAD nucleosidase; nicotinamide adenine dinucleotide glycohydrolase
Systematic name: NAD+ glycohydrolase
Comments: This enzyme can also hydrolyse NADP+ to yield phospho-ADP-ribose and nicotinamide, but more slowly.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, ERGO, CAS registry number: 9032-65-9
References:
1. Hofmann, E.C.G. and Rapoport, S. DPN- und TPN-spezifische Nukleosidasen in Erythrozyten. Biochim. Biophys. Acta 18 (1955) 296 only.
2. Nakazawa, K., Ueda, K., Honjo, T., Yoshihara, K., Nishizuka, Y. and Hayaishi, O. Nicotinamide adenine dinucleotide glycohydrolases and poly adenosine diphosphate ribose synthesis in rat liver. Biochem. Biophys. Res. Commun. 32 (1968) 143-149. [PMID: 5672131]
3. Ueda, K., Fukushima, M., Okayamo, H. and Hayaishi, O. Nicotinamide adenine dinucleotide glycohydrolase from rat liver nuclei. Isolation and characterization of a new enzyme. J. Biol. Chem. 250 (1975) 7541-7546. [PMID: 240831]
4. Yamamoto-Katayama, S., Ariyoshi, M., Ishihara, K., Hirano, T., Jingami, H. and Morikawa, K. Crystallographic studies on human BST-1/CD157 with ADP-ribosyl cyclase and NAD glycohydrolase activities. J. Mol. Biol. 316 (2002) 711-723. [PMID: 11866528]
Common name: [protein ADP-ribosylarginine] hydrolase
Reaction: protein-Nω-(ADP-D-ribosyl)-L-arginine + H2O = ADP-ribose + protein-L-arginine
Other name(s): ADP-ribose-L-arginine cleavage enzyme; ADP-ribosylarginine hydrolase; Nω-(ADP-D-ribosyl)-L-arginine ADP-ribosylhydrolase
Systematic name: protein-Nω-(ADP-D-ribosyl)-L-arginine ADP-ribosylhydrolase
Comments: The enzyme will remove ADP-ribose from arginine residues in ADP-ribosylated proteins. The enzyme can also catalyse the reaction Nω-(ADP-D-ribosyl)-L-arginine + H2O = ADP-ribose + L-arginine.
Links to other databases: BRENDA, EXPASY, KEGG, ERGO, CAS registry number: 98668-52-1
References:
1. Moss, J., Jacobson, M.K. and Stanley, S.J. Reversibility of arginine-specific mono(ADP-ribosyl)ation: identification in erythrocytes of an ADP-ribose-L-arginine cleavage enzyme. Proc. Natl. Acad. Sci. USA 82 (1985) 5603-5607. [PMID: 2994036]
2. Moss, J., Stanley, S.J., Nightingale, M.S., Murtagh, J.J., Jr., Monaco, L., Mishima, K., Chen, H.C., Williamson, K.C. and Tsai, S.C. Molecular and immunological characterization of ADP-ribosylarginine hydrolases. J. Biol. Chem. 267 (1992)10481-10488. [PMID: 1375222]
3. Konczalik, P. and Moss, J. Identification of critical, conserved vicinal aspartate residues in mammalian and bacterial ADP-ribosylarginine hydrolases. J. Biol. Chem. 274 (1999) 16736-16740. [PMID: 10358013]
4. Takada, T., Iida, K. and Moss, J. Cloning and site-directed mutagenesis of human ADP-ribosylarginine hydrolase. J. Biol. Chem. 268 (1993) 17837-17843 [PMID: 8349667]
5. Ohno, T., Tsuchiya, M., Osago, H., Hara, N., Jidoi, J. and Shimoyama, M. Detection of arginine-ADP-ribosylated protein using recombinant ADP-ribosylarginine hydrolase. Anal. Biochem. 10 (1995) 115-122 [PMID: 8678289]
Common name: adenosylcobinamide hydrolase
Reaction: adenosylcobinamide + H2O = adenosylcobyric acid + (R)-1-aminopropan-2-ol
For diagram click here.
Other name(s): CbiZ; AdoCbi amidohydrolase
Systematic name: adenosylcobinamide amidohydrolase
Comments: Involved in the salvage pathway of cobinamide in archaea. Archaea convert adenosylcobinamide (AdoCbi) into adenosylcobinamide phosphate (AdoCbi-P) in two steps. First, the amidohydrolase activity of CbiZ cleaves off the aminopropanol moiety of AdoCbi yielding adenosylcobyric acid (AdoCby); second, AdoCby is converted into AdoCbi-P by the action of EC 6.3.1.10, adenosylcobinamide-phosphate synthase (CbiB).
References:
1. Woodson, J.D. and Escalante-Semerena, J.C. CbiZ, an amidohydrolase enzyme required for salvaging the coenzyme B12 precursor cobinamide in archaea. Proc. Natl. Acad. Sci. USA 101 (2004) 3591-3596. [PMID: 14990804]
[EC 4.2.1.29 Transferred entry: now EC 4.99.1.6, indoleacetaldoxime dehydratase. The enzyme was classified incorrectly as a C-O lyase when the bond broken is a N-O bond. (EC 4.2.1.29 created 1965, deleted 2004)
Common name: vetispiradiene synthase
Reaction: trans,trans-farnesyl diphosphate = vetispiradiene + diphosphate
For diagram, click here.
Other name(s): vetispiradiene-forming farnesyl pyrophosphate cyclase; pemnaspirodiene synthase; HVS; vetispiradiene cyclase
Systematic name: trans,trans-farnesyl-diphosphate diphosphate-lyase (cyclizing, vetispiradiene-forming)
Comments: The initial internal cyclization produces the monocyclic intermediate germacrene A.
CAS registry no.: 192465-18-2
References:
1. Back, K. and Chappell, J. Cloning and bacterial expression of a sesquiterpene cyclase from Hyoscyamus muticus and its molecular comparison to related terpene cyclases. J. Biol. Chem. 270 (1995) 7375-7381. [PMID: 7706281]
2. Keller, H., Czernic, P., Ponchet, M., Ducrot, P.H., Back, K., Chappell, J., Ricci, P. and Marco, Y. Sesquiterpene cyclase is not a determining factor for elicitor- and pathogen-induced capsidiol accumulation in tobacco. Planta 205 (1998) 467-476.
3. Mathis, J.R., Back, K., Starks, C., Noel, J., Poulter, C.D. and Chappell, J. Pre-steady-state study of recombinant sesquiterpene cyclases. Biochemistry 36 (1997) 8340-8348. [PMID: 9204881]
4. Yoshioka, H., Yamada, N. and Doke, N. cDNA cloning of sesquiterpene cyclase and squalene synthase, and expression of the genes in potato tuber infected with Phytophthora infestans. Plant Cell Physiol. 40 (1999) 993-998. [PMID: 10588069]
5. Martin, V.J., Yoshikuni, Y. and Keasling, J.D. The in vivo synthesis of plant sesquiterpenes by Escherichia coli. Biotechnol. Bioeng. 75 (2001) 497-503. [PMID: 11745124]
Common name: aliphatic aldoxime dehydratase
Reaction: an aliphatic aldoxime = an aliphatic nitrile + H2O
Other name(s): OxdA
Systematic name: aliphatic aldoxime hydro-lyase
Comments: The enzyme from Pseudomonas chlororaphis contains Ca2+ and protoheme IX, the iron of which must be in the form Fe2+ for activity. The enzyme exhibits a strong preference for aliphatic aldoximes, such as butyraldoxime and acetaldoxime, over aromatic aldoximes, such as pyridine-2-aldoxime, which is a poor substrate. No activity was found with the aromatic aldoximes benzaldoxime and pyridine-4-aldoxime.
References:
1. Oinuma, K-I., Hashimoto, Y., Konishi, K., Goda, M., Noguchi, T., Higashibata, H. and Kobayashi, M. Novel aldoxime dehydratase involved in carbon-nitrogen triple bond synthesis of Pseudomonas chlororaphis B23: Sequencing, gene expression, purification and characterization. J. Biol. Chem. 278 (2003) 29600-29608. [PMID: 12773527]
Common name: indoleacetaldoxime dehydratase
Reaction: indole-3-acetaldehyde oxime = indole-3-acetonitrile + H2O
Other name(s): indoleacetaldoxime hydro-lyase; 3-indoleacetaldoxime hydro-lyase; indole-3-acetaldoxime hydro-lyase
Systematic name: indole-3-acetaldehyde-oxime hydro-lyase
Links to other databases: BRENDA, EXPASY, KEGG, ERGO, CAS registry number: 9024-27-5
References:
1. Kumar, S.A. and Mahadevan, S. 3-Indoleacetaldoxime hydro-lyase: a pyridoxal-5'-phosphate activated enzyme. Arch. Biochem. Biophys. 103 (1963) 516-518. [PMID: 14099566]
2. Mahadevan, S. Conversion of 3-indoleacetoxime to 3-indoleacetonitrile by plants. Arch. Biochem. Biophys. 100 (1963) 557-558.