An asterisk before 'EC' indicates that this is an amendment to an existing enzyme rather than a new enzyme entry.
Common name: GDP-L-fucose synthase
Reaction: GDP-L-fucose + NADP+ = GDP-4-dehydro-6-deoxy-D-mannose + NADPH + H+
For diagram click here.
Other name(s): GDP-4-keto-6-deoxy-D-mannose-3,5-epimerase-4-reductase
Systematic name: GDP-L-fucose:NADP+ 4-oxidoreductase (3,5-epimerizing)
Comments: Both human and Escherichia coli enzymes can use NADH in place of NADPH to a slight extent.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number:
References:
1. Chang, S., Duerr, B. and Serif, G. An epimerase-reductase in L-fucose synthesis. J. Biol. Chem. 263 (1988) 1693-1697. [PMID: 3338988]
2. Mattila, P., Räbinä, J, Hortling, S., Jelin, J. and Renkonen, R. Functional expression of Escherichia coli enzymes synthesizing GDP-L-fucose from inherent GDP-D-mannose in Saccharomyces cerevisiae. Glycobiology, 10, (2000) 1041-1047. [PMID: 11030750]
3. Menon, S., Stahl, M., Kumar, R., Xu, G.-Y. and Sullivan, F. Stereochemical course and steady state mechanism of the reaction catalyzed by the GDP-fucose synthetase from Escherichia coli. J. Biol. Chem., 274, (1999) 26743-26750. [PMID: 10480878]
4. Somers, W.S., Stahl, M.L. and Sullivan, F.X. GDP-fucose synthetase from Escherichia coli: Structure of a unique member of the short-chain dehydrogenase/reductase family that catalyzes two distinct reactions at the same active site. Structure, 6, (1998) 1601-1612. [PMID: 9862812]
Common name: (R)-3-hydroxyacid-ester dehydrogenase
Reaction: ethyl (R)-3-hydroxyhexanoate + NADP+ = ethyl 3-oxohexanoate + NADPH + H+
Other name(s): 3-oxo ester (R)-reductase
Systematic name: ethyl-(R)-3-hydroxyhexanoate:NADP+ 3-oxidoreductase
Comments: Also acts on ethyl (R)-3-oxobutanoate and some other (R)-3-hydroxy acid esters. The (R)- symbol is allotted on the assumption that no substituents change the order of priority from O-3>C-2>C-4. A subunit of yeast fatty acid synthase EC 2.3.1.86 fatty-acyl-CoA synthase). cf. EC 1.1.1.280 (S)-3-hydroxyacid ester dehydrogenase.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 114705-02-1
References:
1. Heidlas, J., Engel, K.-H. and Tressl, R. Purification and characterization of two oxidoreductases involved in the enantioselective reduction of 3-oxo, 4-oxo and 5-oxo esters in baker's yeast. Eur. J. Biochem. 172 (1988) 633-639. [PMID: 3280313]
Common name: (S)-3-hydroxyacid-ester dehydrogenase
Reaction: ethyl (S)-3-hydroxyhexanoate + NADP+ = ethyl 3-oxohexanoate + NADPH + H+
Other name(s): 3-oxo ester (S)-reductase
Systematic name: ethyl-(S)-3-hydroxyhexanoate:NADP+ 3-oxidoreductase
Comments: Also acts on 4-oxo- and 5-oxo-fatty acids and their esters. cf. EC 1.1.1.279 (R)-3-hydroxyacid ester dehydrogenase.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 114705-03-2
References:
1. Heidlas, J., Engel, K.-H. and Tressl, R. Purification and characterization of two oxidoreductases involved in the enantioselective reduction of 3-oxo, 4-oxo and 5-oxo esters in baker's yeast. Eur. J. Biochem. 172 (1988) 633-639. [PMID: 3280313]
Common name: quinoprotein glucose dehydrogenase
Reaction: D-glucose + ubiquinone = D-glucono-1,5-lactone + ubiquinol
Other name(s): D-glucose:(pyrroloquinoline-quinone) 1-oxidoreductase; glucose dehydrogenase (PQQ-dependent); glucose dehydrogenase (pyrroloquinoline-quinone); quinoprotein D-glucose dehydrogenase; quinoprotein glucose dehydrogenase
Systematic name: D-glucose:ubiquinone oxidoreductase
Comments: Requires Mg2+ or Ca2+ for maximal activity. This is a PQQ-containing quinoprotein that catalyses a direct oxidation of D-glucose to D-gluconate in the periplasm of some bacteria and concomitantly transfers electrons to ubiquinol oxidase through ubiquinone in the respiratory chain.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 81669-60-5
References:
1. Ameyama, M., Nonobe, M., Hayashi, M., Shinagawa, E., Matsushita, K. and Adachi, O. Mode of binding of pyrroloquinoline quinone to apo-glucose dehydrogenase. Agric. Biol. Chem. 49 (1985) 1227-1231.
2. 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]
3. 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]
4. 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]
5. Oubrie, A., Rozeboom, H.J. and Dijkstra, B.W. Active-site structure of the soluble quinoprotein glucose dehydrogenase complexed with methylhydrazine: A covalent cofactor-inhibitor complex. Proc. Natl. Acad. Sci. USA 96 (1999) 11787-11791. [PMID: 10518528]
6. 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]
[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)]
[EC 1.2.1.55 Transferred entry: now EC 1.1.1.279 (R)-3-hydroxyacid ester dehydrogenase. (EC 1.2.1.55 created 1990, deleted 2003)]
[EC 1.2.1.56 Transferred entry: now EC 1.1.1.280 (S)-3-hydroxyacid ester dehydrogenase. (EC 1.2.1.56 created 1990, deleted 2003)]
Common name: carbon-monoxide oxygenase (cytochrome b-561)
Reaction: CO + H2O + ferrocytochrome b-561 = CO2 + 2 H+ + 2 ferricytochrome b-561
Other name(s): carbon monoxide oxidase; carbon monoxide oxygenase (cytochrome b-561); carbon monoxide:methylene blue oxidoreductase
Systematic name: carbon monoxide,water:cytochrome b-561 oxidoreductase
Comments: Contains molybdopterin cytosine dinucleotide, FAD and [2Fe-2S]-clusters. Oxygen, methylene blue and iodonitrotetrazolium chloride can act as nonphysiological electron acceptors.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 64972-88-9
References:
1. Meyer, O., Jacobitz, S. and Krüger, B. Biochemistry and physiology of aerobic carbon monoxide-utilizing bacteria. FEMS Microbiol. Rev. 39 (1986) 161-179.
2. Jacobitz, S. and Meyer, O. Removal of CO dehydrogenase from Pseudomonas carboxydovorans cytoplasmic membranes, rebinding of CO dehydrogenase to depleted membranes and restoration of respiratory activities. J. Bacteriol. 171 (1989) 6294-6299. [PMID: 2808305]
3. Meyer, O. and Schlegel, H.-G. Carbon monoxide:methylene blue oxidoreductase from Pseudomonas carboxydovorans. J. Bacteriol. 141 (1980) 74-80. [PMID: 7354006]
[EC 1.2.3.10 Deleted entry: carbon-monoxide oxidase. Activity due to EC 1.2.2.4 carbon-monoxide oxygenase (cytochrome b-561). (EC 1.2.3.10 created 1990, deleted 2003)]
[EC 1.2.3.12 Transferred entry: now EC 1.14.13.82 vanillate monooxygenase. (EC 1.2.3.12 created 2000, deleted 2003)]
Common name: pyruvate dehydrogenase (acetyl-transferring)
Reaction: pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2
For diagram of reaction click here.
Glossary: dihydrolipoyl group
thiamine diphosphate
Other name(s): MtPDC (mitochondrial pyruvate dehydogenase complex); pyruvate decarboxylase; pyruvate dehydrogenase; pyruvate dehydrogenase (lipoamide); pyruvate dehydrogenase complex; pyruvate:lipoamide 2-oxidoreductase (decarboxylating and acceptor-acetylating); pyruvic acid dehydrogenase; pyruvic dehydrogenase
Systematic name: pyruvate:[dihydrolipoyllysine-residue acetyltransferase]-lipoyllysine 2-oxidoreductase (decarboxylating, acceptor-acetylating)
Comments: Contains thiamine diphosphate. It is a component (in multiple copies) of the multienzyme pyruvate dehydrogenase complex in which it is bound to a core of molecules of EC 2.3.1.12, dihydrolipoyllysine acetyltransferase, which also binds multiple copies of EC 1.8.1.4, dihydrolipoyl dehydrogenase. It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in EC 2.3.1.12.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 9014-20-4
References:
1. Ochoa, S. Enzymic mechanisms in the citric acid cycle. Adv. Enzymol. Relat. Subj. Biochem. 15 (1954) 183-270.
2. Scriba, P. and Holzer, H. Gewinnung von αHydroxyäthyl-2-thiaminpyrophosphat mit Pyruvatoxydase aus Schweineherzmuskel. Biochem. Z. 334 (1961) 473-486.
3. Perham, R.N. Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions. Annu. Rev. Biochem., 69, (2000) 961-1004. [PMID: 10966480]
Common name: oxoglutarate dehydrogenase (succinyl-transferring)
Reaction: 2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
For diagram of reaction click here and for mechanism click here.
Glossary: dihydrolipoyl group
thiamine diphosphate
Other name(s): 2-ketoglutarate dehydrogenase; 2-oxoglutarate dehydrogenase; 2-oxoglutarate: lipoate oxidoreductase; 2-oxoglutarate:lipoamide 2-oxidoreductase (decarboxylating and acceptor-succinylating); α-ketoglutarate dehydrogenase; αketoglutaric acid dehydrogenase; α-ketoglutaric dehydrogenase; α-oxoglutarate dehydrogenase; AKGDH; OGDC; ketoglutaric dehydrogenase; oxoglutarate decarboxylase; oxoglutarate dehydrogenase; oxoglutarate dehydrogenase (lipoamide)
Systematic name: 2-oxoglutarate:[dihydrolipoyllysine-residue succinyltransferase]-lipoyllysine 2-oxidoreductase (decarboxylating, acceptor-succinylating)
Comments: Contains thiamine diphosphate. It is a component of the multienzyme 2-oxoglutarate dehydrogenase complex in which multiple copies of it are bound to a core of molecules of EC 2.3.1.61, dihydrolipoyllysine succinyltransferase, which also binds multiple copies of EC 1.8.1.4, dihydrolipoyl dehydrogenase. It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in EC 2.3.1.61.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 9031-02-1
References:
1. Massey, V. The composition of the ketoglutarate dehydrogenase complex. Biochim. Biophys. Acta 38 (1960) 447-460.
2. Ochoa, S. Enzymic mechanisms in the citric acid cycle. Adv. Enzymol. Relat. Subj. Biochem. 15 (1954) 183-270.
3. Sanadi, D.R., Littlefield, J.W. and Bock, R.M. Studies on α-ketoglutaric oxidase. II. Purification and properties. J. Biol. Chem.,197 (1952) 851-862.
4. Perham, R.N. Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions. Annu. Rev. Biochem., 69, (2000) 961-1004. [PMID: 10966480]
Common name: 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring)
Reaction: 3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine = [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO2
For diagram of reaction click here.
Glossary: dihydrolipoyl group
thiamine diphosphate
Other name(s):2-oxoisocaproate dehydrogenase; 2-oxoisovalerate (lipoate) dehydrogenase; 3-methyl-2-oxobutanoate dehydrogenase (lipoamide); 3-methyl-2-oxobutanoate:lipoamide oxidoreductase (decarboxylating and acceptor-2-methylpropanoylating); α-keto-α-methylvalerate dehydrogenase; α-ketoisocaproate dehydrogenase; α-ketoisocaproic dehydrogenase; α-ketoisocaproic-α-keto-α-methylvaleric dehydrogenase; α-ketoisovalerate dehydrogenase; α-oxoisocaproate dehydrogenase; BCKDH; BCOAD; branched chain keto acid dehydrogenase; branched-chain (-2-oxoacid) dehydrogenase (BCD); branched-chain 2-keto acid dehydrogenase; branched-chain 2-oxo acid dehydrogenase; branched-chain α-keto acid dehydrogenase; branched-chain α-oxo acid dehydrogenase; branched-chain keto acid dehydrogenase; branched-chain ketoacid dehydrogenase; dehydrogenase, 2-oxoisovalerate (lipoate); dehydrogenase, branched chain α-keto acid
Systematic name: 3-methyl-2-oxobutanoate:[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase]-lipoyllysine 2-oxidoreductase (decarboxylating, acceptor-2-methylpropanoylating)
Comments: Contains thiamine diphosphate. It acts not only on 3-methyl-2-oxobutanaoate, but also on 4-methyl-2-oxopentanoate and (S)-3-methyl-2-oxopentanoate, so that it acts on the 2-oxo acids that derive from the action of transaminases on valine, leucine and isoleucine. It is a component of the multienzyme 3-methyl-2-oxobutanoate dehydrogenase complex in which multiple copies of it are bound to a core of molecules of EC 2.3.1.168, dihydrolipoyllysine (2-methylpropanoyl)transferase, which also binds multiple copies of EC 1.8.1.4, dihydrolipoyl dehydrogenase. It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in EC 2.3.1.168.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 9082-72-8
References:
1. Bowden, J.A. and Connelly, J.L. Branched chain α-keto acid metabolism. II. Evidence for the common identity of α-ketoisocaproic acid and α-keto-β-methyl-valeric acid dehydrogenases. J. Biol. Chem. 243 (1968) 3526-3531. [PMID: 5656388]
2.Connelly, J.L., Danner, D.J. and Bowden, J.A. Branched chain α-keto acid metabolism. I. Isolation, purification, and partial characterization of bovine liver α-ketoisocaproic:α-keto-β-methylvaleric acid dehydrogenase. J. Biol. Chem. 243 (1968) 1198-1203. [PMID: 5689906]
3. Danner, D.J., Lemmon, S.K., Beharse, J.C. and Elsas, L.J., II, Purification and characterization of branched chain α-ketoacid dehydrogenase from bovine liver mitochondria. J. Biol. Chem., 254, (1979) 5522-5526. [PMID: 447664]
4. Pettit, F.H., Yeaman, S.J. and Reed, L.J. Purification and characterization of branched chain α-keto acid dehydrogenase complex of bovine kidney. Proc. Natl. Acad. Sci. USA, 75, (1978) 4881-4885. [PMID: 283398]
5. Perham, R.N. Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions. Annu. Rev. Biochem., 69, (2000) 961-1004. [PMID: 10966480]
Common name: pyruvate synthase
Reaction: pyruvate + CoA + oxidized ferredoxin = acetyl-CoA + CO2 + reduced ferredoxin
Other name(s): pyruvate oxidoreductase; pyruvate synthetase; pyruvate:ferredoxin oxidoreductase; pyruvic-ferredoxin oxidoreductase
Systematic name: pyruvate:ferredoxin 2-oxidoreductase (CoA-acetylating)
Comments: Contains thiamine diphosphate and [4Fe-4S] clusters.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 9082-51-3
References:
1. Evans, M.C.W. and Buchanan, B.B. Photoreduction of ferredoxin and its use in carbon dioxide fixation by a subcellular system from a photosynthetic bacterium. Proc. Natl. Acad. Sci. USA 53 (1965) 1420-1425. [PMID: 5217644]
2. Gehring, U. and Arnon, D.I. Purification and properties of α-ketoglutarate synthase from a photosynthetic bacterium. J. Biol. Chem. 247 (1972) 6963-6969. [PMID: 4628267]
3. Uyeda, K. and Rabinowitz, J.C. Pyruvate-ferredoxin oxidoreductase. 3. Purification and properties of the enzyme. J. Biol. Chem. 246 (1971) 3111-3119. [PMID: 5574389]
4. Uyeda, K. and Rabinowitz, J.C. Pyruvate-ferredoxin oxidoreductase. IV. Studies on the reaction mechanism. J. Biol. Chem. 246 (1971) 3120-3125. [PMID: 4324891]
5. Charon, M.-H., Volbeda, A., Chabriere, E., Pieulle, L. and Fontecilla-Camps, J.C. Structure and electron transfer mechanism of pyruvate:ferredoxin oxidoreductase. Curr. Opin. Struct. Biol. 9 (1999) 663-669. [PMID: 10607667]
Common name: carbon-monoxide dehydrogenase (ferredoxin)
Reaction: CO + H2O + oxidized ferredoxin = CO2 + reduced ferredoxin
Other name(s):
Systematic name: carbon-monoxide,water:ferredoxin oxidoreductase
Comments: Contains nickel, zinc and non-heme iron. Methyl viologen can act as acceptor. The enzyme from Moorella thermoacetica exists as a complex with EC 2.3.1.169, CO-methylating acetyl CoA synthase, which catalyses the overall reaction:
methylcorrinoid protein + CoA + CO2 + reduced ferredoxin = acetyl-CoA + corrinoid protein + H2O + oxidized ferredoxin.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number:
References:
1. Meyer, O. and Schlegel, H.-G. Carbon monoxide:methylene blue oxidoreductase from Pseudomonas carboxydovorans. J. Bacteriol. 141 (1980) 74-80. [PMID: 7354006]
2.Ragsdale, S.W., Clark, J.E., Ljungdahl, L.G., Lundie, L.L. and Drake, H.L. Properties of purified carbon monoxide dehydrogenase from Clostridium thermoaceticum a nickel, iron-sulfur protein. J. Biol. Chem. 258 (1983) 2364-2369. [PMID: 6687389]
3. Doukov, T.I., Iverson, T., Seravalli, J., Ragsdale, S.W. and Drennan, C.L. A Ni-Fe-Cu center in a bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase. Science 298 (2002) 567-572. [PMID: 12386327]
Common name: aldehyde ferredoxin oxidoreductase
Reaction: an aldehyde + H2O + 2 oxidized ferredoxin = an acid + 2 H+ + 2 reduced ferredoxin
Other name(s): AOR
Systematic name: aldehyde:ferredoxin oxidoreductase
Comments: This is an oxygen-sensitive enzyme that contains tungsten-molybdopterin and iron-sulfur clusters. Catalyses the oxidation of aldehydes (including crotonaldehyde, acetaldehyde, formaldehyde and glyceraldehyde) to their corresponding acids. However, it does not oxidize glyceraldehyde 3-phosphate (see EC 1.2.7.6, glyceralde-3-phosphate ferredoxin reductase). Can use ferredoxin or methyl viologen but not NAD(P)+ as electron acceptor.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number:
References:
1. Mukund, S. and Adams, M.W.W. The novel tungsten-iron-sulfur protein of the hyperthermophilic archaebacterium, Pyrococcus furiosus, is an aldehyde ferredoxin oxidoreductase - evidence for its participation in a unique glycolytic pathway. J. Biol. Chem. 266 (1991) 14208-14216. [PMID: 1907273]
2. Johnson, J.L., Rajagopalan, K.V., Mukund, S. and Adams, M.W.W. Identification of molybdopterin as the organic-component of the tungsten cofactor in four enzymes from hyperthermophilic archaea. J. Biol. Chem. 268 (1993) 4848-4852. [PMID: 8444863]
3. Chan, M.K., Mukund, S., Kletzin, A., Adams, M.W.W. and Rees, D.C. Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase. Science 267 (1995) 1463-1469. [PMID: 7878465]
4. Roy, R., Menon, A.L. and Adams, M.W.W. Aldehyde oxidoreductases from Pyrococcus furiosus. Methods Enzymol. 331 (2001) 132-144. [PMID: 11265456]
Common name: glyceraldehyde-3-phosphate ferredoxin reductase
Reaction: D-glyceraldehyde-3-phosphate + H2O + 2 oxidized ferredoxin = 3-phospho-D-glycerate + 2 H+ + 2 reduced ferredoxin
Other name(s): GAPOR; glyceraldehyde-3-phosphate Fd oxidoreductase
Systematic name: D-glyceraldehyde-3-phosphate:ferredoxin oxidoreductase
Comments: Contains tungsten-molybdopterin and iron-sulfur clusters. This enzyme is thought to function in place of glyceralde-3-phosphate dehydrogenase and possibly phosphoglycerate kinase in the novel Embden-Meyerhof-type glycolytic pathway found in Pyrococcus furiosus [1]. It is specific for glyceraldehyde-3-phosphate.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number:
References:
1. Mukund, S. and Adams, M.W.W. Glyceraldehyde-3-phosphate ferredoxin oxidoreductase, a novel tungsten-containing enzyme with a potential glycolytic role in the hyperthermophilic archaeon Pyrococcus furiosus. J. Biol. Chem. 270 (1995) 8389-8392. [PMID: 7721730]
2. Roy, R., Menon, A.L. and Adams, M.W.W. Aldehyde oxidoreductases from Pyrococcus furiosus. Methods Enzymol. 331 (2001) 132-144. [PMID: 11265456]
Common name: 2-oxoisovalerate ferredoxin reductase
Reaction: 3-methyl-2-oxobutanoate + CoA + oxidized ferredoxin = S-(2-methylpropanoyl)-CoA + CO2 + reduced ferredoxin
Other name(s): 2-ketoisovalerate ferredoxin reductase; 3-methyl-2-oxobutanoate synthase (ferredoxin); VOR; branched-chain ketoacid ferredoxin reductase; branched-chain oxo acid ferredoxin reductase; keto-valine-ferredoxin oxidoreductase; ketoisovalerate ferredoxin reductase
Systematic name: 3-methyl-2-oxobutanoate:ferredoxin oxidoreductase (decarboxylating; CoA-2-methylpropanoylating)
Comments: This enzyme is one of four 2-oxoacid oxidoreductases that are differentiated by their abilities to oxidatively decarboxylate different 2-oxoacids and form their CoA derivatives (see also EC 1.2.7.1, pyruvate synthase; EC 1.2.7.8, indolepyruvate ferredoxin oxidoreductase and EC 1.2.7.9, 2-oxoglutarate ferredoxin oxidoreductase). It is CoA-dependent and contains thiamine diphosphate and iron-sulfur clusters. Preferentially utilizes 2-oxo-acid derivatives of branched chain amino acids, e.g. 3-methyl-2-oxopentanoate, 4-methyl-2-oxo-pentanoate, 2-oxobutyrate and 3-methylthiopropanamine.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number:
References:
1. Heider, J., Mai, X.H. and Adams, M.W.W. Characterization of 2-ketoisovalerate ferredoxin oxidoreductase, a new and reversible coenzyme A-dependent enzyme involved in peptide fermentation by hyperthermophilic archaea. J. Bacteriol. 178 (1996) 780-787. [PMID: 8550513]
2. Tersteegen, A., Linder, D., Thauer, R.K. and Hedderich, R. Structures and functions of four anabolic 2-oxoacid oxidoreductases in Methanobacterium thermoautotrophicum. Eur. J. Biochem. 244 (1997) 862-868. [PMID: 9108258]
3. Schut, G.J., Menon, A.L. and Adams, M.W.W. 2-Keto acid oxidoreductases from Pyrococcus furiosus and Thermococcus litoralis. Methods Enzymol. 331 (2001) 144-158. [PMID: 11265457]
Common name: indolepyruvate ferredoxin oxidoreductase
Reaction: (indol-3-yl)pyruvate + CoA + oxidized ferredoxin = S-2-(indol-3-yl)acetyl-CoA + CO2 + reduced ferredoxin
Other name(s):3-(indol-3-yl)pyruvate synthase (ferredoxin); IOR
Systematic name: 3-(indol-3-yl)pyruvate:ferredoxin oxidoreductase (decarboxylating, CoA-indole-acetylating)
Comments: This enzyme, which is found in archaea, is one of four 2-oxoacid oxidoreductases that are differentiated by their abilities to oxidatively decarboxylate different 2-oxoacids and form their CoA derivatives (see also EC 1.2.7.1, pyruvate synthase, EC 1.2.7.7, 2-oxoisovalerate ferredoxin reductase and EC 1.2.7.9, 2-oxoglutarate ferredoxin oxidoreductase) [4]. Contains thiamine diphosphate and [4Fe-4S] clusters. Preferentially utilizes the transaminated forms of aromatic amino acids and can use phenylpyruvate and p-hydroxyphenylpyruvate as substrates.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number:
References:
1. Mai, X.H. and Adams, M.W.W. Indolepyruvate ferredoxin oxidoreductase from the hyperthermophilic archaeon Pyrococcus furiosus - a new enzyme involved in peptide fermentation. J. Biol. Chem. 269 (1994) 16726-16732. [PMID: 8206994]
2. Siddiqui, M.A., Fujiwara, S. and Imanaka, T. Indolepyruvate ferredoxin oxidoreductase from Pyrococcus sp. K0d1 possesses a mosaic: Structure showing features of various oxidoreductases. Mol. Gen. Genet. 254 (1997) 433-439. [PMID: 9180697]
3. Tersteegen, A., Linder, D., Thauer, R.K. and Hedderich, R. Structures and functions of four anabolic 2-oxoacid oxidoreductases in Methanobacterium thermoautotrophicum. Eur. J. Biochem. 244 (1997) 862-868. [PMID: 9108258]
4. Schut, G.J., Menon, A.L. and Adams, M.W.W. 2-Keto acid oxidoreductases from Pyrococcus furiosus and Thermococcus litoralis. Methods Enzymol. 331 (2001) 144-158. [PMID: 11265457]
Common name: 2-oxoglutarate ferredoxin oxidoreductase
Reaction: 2-oxoglutarate + CoA + 2 oxidized ferredoxin = succinyl-CoA + CO2 + 2 reduced ferredoxin
Other name(s): 2-ketotglutarate ferredoxin oxidoreductase; 2-oxoglutarate:ferredoxin oxidoreductase; KGOR
Systematic name: 2-oxoglutarate:ferredoxin oxidoreductase (decarboyxlating)
Comments: This enzyme is one of four 2-oxoacid oxidoreductases that are differentiated by their abilities to oxidatively decarboxylate different 2-oxoacids and form their CoA derivatives (see also EC 1.2.7.1, pyruvate synthase, EC 1.2.7.7, 2-oxoisovalerate ferredoxin reductase and EC 1.2.7.8, indolepyruvate ferredoxin oxidoreductase) [3]. Contains thiamine diphosphate and 2 [4Fe-4S] clusters. Highly specific for 2-oxoglutarate.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number:
References:
1. Dorner ,E. and Boll, M. Properties of 2-oxoglutarate:ferredoxin oxidoreductase from Thauera aromatica and its role in enzymatic reduction of the aromatic ring. J. Bacteriol. 184 (2002) 3975-3983. [PMID: 12081970]
2. Mai, X., Adams, M.W. Characterization of a fourth type of 2-keto acid-oxidizing enzyme from a hyperthermophilic archaeon: 2-ketoglutarate ferredoxin oxidoreductase from Thermococcus litoralis. J. Bacteriol. 178 (1996) 5890-5896. [PMID: 8830683]
3. Schut, G.J., Menon, A.L. and Adams, M.W.W. 2-Keto acid oxidoreductases from Pyrococcus furiosus and Thermococcus litoralis. Methods Enzymol. 331 (2001) 144-158. [PMID: 11265457]
Common name: carbon-monoxide dehydrogenase (acceptor)
Reaction: CO + H2O + A = CO2 + AH2
Other name(s): anaerobic carbon monoxide dehydrogenase; carbon monoxide oxygenase; carbon-monoxide dehydrogenase
Systematic name: carbon-monoxide:(acceptor) oxidoreductase
Comments: Contains a [Ni3Fe-4S] cluster and [4Fe-4S] clusters. It uses many electron acceptors, including ferredoxin, methyl viologen and benzyl viologen and flavins, but not pyridine nucleotides. Forms part of a membrane-bound multienzyme complex with EC 1.12.99.6, hydrogenase (acceptor), which catalyses the overall reaction: CO + H2O = CO2 + H2.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 64972-88-9
References:
1. Bonam, D. and Ludden, P.W. Purification and characterization of carbon monoxide dehydrogenase, a nickel, zinc, iron-sulfur protein, from Rhodospirillum rubrum. J. Biol. Chem. 262 (1987) 2980-2987. [PMID: 3029096]
2. Diekert, G. and Ritter, M. Purification of the nickel protein carbon monoxide dehydrogenase of Clostridium thermoaceticum. FEBS Lett. 151 (1983) 41-44. [PMID: 6687458]
3. Drennan, C.L., Heo, J., Sintchak, M.D., Schreiter, E. and Ludden, P.W. Life on carbon monoxide: X-ray structure of Rhodospirillum rubrum Ni-Fe-S carbon monoxide dehydrogenase. Proc. Natl. Acad. Sci. USA 98 (2001) 11973-11978. [PMID: 11593006]
4. Dobbek, H., Svetlitchnyi, V., Gremer, L., Huber, R. and Meyer, O. Crystal structure of a carbon monoxide dehydrogenase reveals a [Ni-4Fe-5S] cluster. Science 293 (2001) 1281-1285. [PMID: 11509720]
Common name: tryptophan α,β-oxidase
Reaction: L-tryptophan + O2 = α,β-didehydrotryptophan + H2O2
Other name(s): L-tryptophan 2',3'-oxidase; L-tryptophan α,β-dehydrogenase
Systematic name: L-tryptophan:oxygen α,β-oxidoreductase
Comments: Requires heme. The enzyme from Chromobacterium violaceum is specific for tryptophan derivatives possessing its carboxyl group free or as an amide or ester, and an unsubstituted indole ring. Also catalyses the α,β dehydrogenation of L-tryptophan side chains in peptides. The product of the reaction can hydrolyse spontaneously to form indolepyruvate.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 156859-19-7
References:
1. Genet, R., Denoyelle, C. and Menez, A. Purification and partial characterization of an amino acid α,β-dehydrogenase, L-tryptophan 2',3'-oxidase from Chromobacterium violaceum. J. Biol. Chem. 269 (1994) 18177-18184. [PMID: 8027079]
2. Genet, R., Benetti, P.H., Hammadi, A. and Menez, A. L-Tryptophan 2',3'-oxidase from Chromobacterium violaceum. Substrate specificity and mechanistic implications. J. Biol. Chem. 270 (1995) 23540-23545. [PMID: 7559518]
[EC 1.4.3.17 Transferred entry: now EC 1.3.3.10 tryptophan α,β-oxidase. (EC 1.4.3.17 created 2000, deleted 2003)]
Common name: glycine dehydrogenase (decarboxylating)
Reaction: glycine + H-protein-lipoyllysine = H-protein-S-aminomethyldihydrolipoyllysine + CO2
For diagram of reaction click here.
Glossary: dihydrolipoyl group
Other name(s): P-protein; glycine decarboxylase; glycine-cleavage complex; glycine:lipoylprotein oxidoreductase (decarboxylating and acceptor-aminomethylating); protein P1
Systematic name: glycine:H-protein-lipoyllysine oxidoreductase (decarboxylating, acceptor-amino-methylating)
Comments: A pyridoxal-phosphate protein. A component, with EC 2.1.2.10, aminomethyltransferase and EC 1.8.1.4, dihydrolipoyl dehydrogenanse, of the glycine cleavage system, previously known as glycine synthase.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 37259-67-9
References:
1. Hiraga, K. and Kikuchi, G. The mitochondrial glycine cleavage system. Functional association of glycine decarboxylase and aminomethyl carrier protein. J. Biol. Chem. 255 (1980) 11671-11676. [PMID: 7440563]
2. Perham, R.N. Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions. Annu. Rev. Biochem. 69 (2000) 961-1004. [PMID: 10966480]
Common name: NADPH—hemoprotein reductase
Reaction: NADPH + H+ + n oxidized hemoprotein = NADP+ + n reduced hemoprotein
Other name(s): CPR; FAD-cytochrome c reductase; NADP—cytochrome c reductase; NADP—cytochrome reductase; NADPH-dependent cytochrome c reductase; NADPH:P-450 reductase; NADPH:ferrihemoprotein oxidoreductase; NADPH—cytochrome P-450 oxidoreductas; NADPH—cytochrome c oxidoreductase; NADPH—cytochrome c reductase; NADPH—cytochrome p-450 reductase; NADPH—ferricytochrome c oxidoreductase; NADPH—ferrihemoprotein reductase; TPNH2 cytochrome c reductase; TPNH-cytochrome c reductase; aldehyde reductase (NADPH-dependent); cytochrome P-450 reductase; cytochrome c reductase (reduced nicotinamide adenine dinucleotide phosphate, NADPH, NADPH-dependent); dihydroxynicotinamide adenine dinucleotide phosphate-cytochrome c reductase; ferrihemoprotein P-450 reductase; reduced nicotinamide adenine dinucleotide phosphate-cytochrome c reductase; reductase, cytochrome c (reduced nicotinamide adenine dinucleotide phosphate)
Systematic name: NADPH:hemoprotein oxidoreductase
Comments: A flavoprotein (FMN, FAD) containing both FMN and FAD. The number n in the equation is 1 if the hemoprotein undergoes a 2-electron reduction, and is 2 if it undergoes a 1-electron reduction. The enzyme catalyses the reduction of the heme-thiolate-dependent monooxygenases, such as EC 1.14.14.1, unspecific monooxygenase and reduction of EC 1.14.99.3, heme oxygenase. It is part of the microsomal hydroxylating system. It also reduces cytochrome b5 and cytochrome c.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 923-03-4
References:
1. Haas, E., Horecker, B.L. and Hogness, T.R. The enzymatic reduction of cytochrome c, cytochrome c reductase. J. Biol. Chem. 136 (1940) 747-774.
2. Horecker, B.L. Triphosphopyridine nucleotide-cytochrome c reductase in liver. J. Biol. Chem. 183, (1950) 593-605.
3. Lu, A.Y.H., Junk, K.W. and Coon, M.J. Resolution of the cytochrome P-450-containing ω-hydroxylation system of liver microsomes into three components. J. Biol. Chem. 244, (1969) 3714-3721. [PMID: 4389465]
4. Masters, B.S.S., Kamin, H., Gibson, Q.H. and Williams, C.H., Jr. Studies on the mechanism of microsomal triphosphopyridine nucleotide-cytochrome c reductase. J. Biol. Chem. 240, (1965) 921-931.
5. Williams, C.H.,Jr. and Kamin, H. Microsomal triphosphopyridine nucleotide-cytochrome c reductase in liver. J. Biol. Chem. 237, (1962) 587-595. p> 6.Masters, B.S.S., Bilimoria, M.H, Kamen, H. and Gibson, Q.H. The mechanism of 1- and 2-electron transfers catalyzed by reduced triphosphopyridine nucleotide-cytochrome c reductase. J. Biol. Chem. 240, (1965) 4081-4088. [PMID: 4378860]
7. Sevrioukova, I.F. and Peterson, J.A. NADPH-P-450 reductase: Structural and functional comparisons of the eukaryotic and prokaryotic isoforms. Biochimie 77, (1995) 562-572. [PMID: 8589067]
8. Wang, M., Roberts, D.L., Paschke, R., Shea, T.M., Masters, B.S.S. and Kim, J.-J.P. Three-dimensional structure of NADPH-cytochrome P450 reductase: Prototype for FMN- and FAD-containing enzymes. Proc. Natl. Acad. Sci. USA 94, (1997) 8411-8416. [PMID: 9237990]
9. Munro, A.W., Noble, M.A., Robledo, L., Daff, S.N. and Chapman, S.K. Determination of the redox properties of human NADPH-cytochrome P450 reductase. Biochemistry 40, (2001) 1956-1963. [PMID: 11329262]
10. Gutierrez, A., Grunau, A., Paine, M., Munro, A.W., Wolf, C.R., Roberts, G.C.K. and Scrutton, N.S. Electron transfer in human cytochrome P450 reductase. Biochem. Soc. Trans. 31, (2003) 497-501. [PMID: 12773143]
Common name: hydroxylamine oxidoreductase
Reaction: (1) hydroxylamine + NH3 = hydrazine + H2O
(2) hydrazine + acceptor = N2 + reduced acceptor
Systematic name: hydroxylamine:acceptor oxidoreductase
Comments: The enzyme from anammox bacteria is inhibited by phosphate, oxygen and high nitrite concentrations and is also capable of reducing NO to N2O. Ferricyanide, phenazine methosulfate and methylthiazolyltetrazolium bromide can act as acceptors in this 4-electron transfer reaction.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number:
References:
1. Schalk, J., de Vries, S., Kuenen, J.G. and Jetten, M.S. Involvement of a novel hydroxylamine oxidoreductase in anaerobic ammonium oxidation. Biochemistry 39 (2000) 5405-5412. [PMID: 10820012]
2. Jetten, M.S., Wagner, M., Fuerst, J., van Loosdrecht, M., Kuenen, G. and Strous, M. Microbiology and application of the anaerobic ammonium oxidation ('anammox') process. Curr. Opin. Biotechnol. 12 (2001) 283-288. [PMID: 11404106]
Common name: dihydrolipoyl dehydrogenanse
Reaction: protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+
For diagram of reaction click here (e.g. citric acid cycle and glycine cleavage).
Glossary: dihydrolipoyl group
Other name(s): LDP-Glc; LDP-Val; dehydrolipoate dehydrogenase; diaphorase; dihydrolipoamide dehydrogenase; dihydrolipoamide:NAD+ oxidoreductase; dihydrolipoic dehydrogenase; dihydrolipoyl dehydrogenase; dihydrothioctic dehydrogenase; lipoamide dehydrogenase (NADH); lipoamide oxidoreductase (NADH); lipoamide reductase; lipoamide reductase (NADH2); lipoate dehydrogenase; lipoic acid dehydrogenase; lipoyl dehydrogenase
Systematic name:protein-N6-(dihydrolipoyl)lysine:NAD+ oxidoreductase
Comments: A flavoprotein (FAD). A component of the multienzyme 2-oxo-acid dehydrogenase complexes. In the pyruvate dehydrogenase complex, it binds to the core of EC 2.3.1.12, dihydrolipoyllysine acetyltransferase, and catalyses oxidation of its dihydrolipoyl groups. It plays a similar role in the oxoglutarate and 3-methyl-2-oxobutanoate dehydrogenase complexes. Another substrate is the dihydrolipoyl group in the H-protein of the glycine-cleavage system (click here for diagram), in which it acts, together with EC 1.4.4.2, glycine dehydrogenase (decarboxylating), and EC 2.1.2.10, aminomethyltransferase, to break down glycine. It can also use free dihydrolipoate, dihydrolipoamide or dihydrolipoyllysine as substrate. This enzyme was first shown to catalyse the oxidation of NADH by methylene blue; this activity was called diaphorase.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 9001-18-7
References:
1. Massey, V. Lipoyl dehydrogenase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes 2nd ed., vol. 7, Academic Press, New York, 1963, pp. 275-306.
2. Massey, V., Gibson, Q.H. and Veeger, C. Intermediates in the catalytic action of lipoyl dehydrogenase (diaphorase). Biochem. J. 77 (1960) 341-351.
3. Savage, N. Preparation and properties of highly purified diaphorase. Biochem. J. 67 (1957) 146-155.
4. Straub, F.B. Isolation and properties of a flavoprotein from heart muscle tissue. Biochem. J. 33 (1939) 787-792.
5. Perham, R.N. Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions. Annu. Rev. Biochem. 69 (2000) 961-1004. [PMID: 10966480]
EC 1.8.98 With other, known, acceptors
Common name: CoB—CoM heterodisulfide reductase
Reaction: coenzyme B + coenzyme M + methanophenazine = N-{7-[(2-sulfoethyl)dithio]heptanoyl}-3-O-phospho-L-threonine + dihydromethanophenazine
For diagram click here.
Glossary:
coenzyme B (CoB) = N-(7-mercaptoheptanoyl)threonine 3-O-phosphate
coenzyme M (CoM) = 2-mercaptoethanesulfonate
Other name(s): heterodisulfide reductase; soluble heterodisulfide reductase
Systematic name: coenzyme B:coenzyme M:methanophenazine oxidoreductase
Comments: This enzyme is found in methanogenic archaea, particularly Methanosarcina species, and regenerates coenzyme M and coenzyme B after the action of EC 2.8.4.1, coenzyme-B sulfoethylthiotransferase. Contains (per heterodimeric unit) two distinct b-type hemes and two [4Fe-4S] clusters [3]. Highly specific for both coenzyme M and coenzyme B. Reacts with various phenazine derivatives, including 2-hydroxyphenazine and 2-bromophenazine.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number:
References:
1. Hedderich, R., Berkessel, A. and Thauer, R.K. Purification and properties of heterodisulfide reductase from Methanobacterium thermoautotrophicum (strain Marburg). Eur. J. Biochem. 193 (1990) 255-261. [PMID: 2121478]
2. Abken, H.J., Tietze, M., Brodersen, J., Bäumer, S., Beifuss, U. and Deppenmeier, U. Isolation and characterization of methanophenazine and function of phenazines in membrane-bound electron transport of Methanosarcina mazei gol. J. Bacteriol. 180 (1998) 2027-2032. [PMID: 9555882]
3. Simianu, M., Murakami, E., Brewer, J.M. and Ragsdale, S.W. Purification and properties of the heme- and iron-sulfur-containing heterodisulfide reductase from Methanosarcina thermophila. Biochemistry 37 (1998) 10027-10039. [PMID: 9665708]
4. Murakami, E., Deppenmeier, U. and Ragsdale, S.W. Characterization of the intramolecular electron transfer pathway from 2-hydroxyphenazine to the heterodisulfide reductase from Methanosarcina thermophilo. J. Biol. Chem. 276 (2001) 2432-2439. [PMID: 11034998]
Common name: hydrogenase (acceptor)
Reaction: H2 + A = AH2
Other name(s): H2 producing hydrogenase[ambiguous]; hydrogen-lyase[ambiguous]; hydrogenlyase[ambiguous]; uptake hydrogenase[ambiguous]
Systematic name: hydrogen:(acceptor) oxidoreductase
Comments: Uses molecular hydrogen for the reduction of a variety of substances. Contains iron-sulfur clusters. The enzyme from some sources contains nickel.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 9027-05-8
References:
1. Shug, A.L., Wilson, P.W., Green, D.E. and Mahler, H.R. The role of molybdenum and flavin in hydrogenase. J. Am. Chem. Soc. 76 (1954) 3355-3356.
2. Adams, M.W.W., Mortenson, L.E. and Chen, J.S. Hydrogenase. Biochim. Biophys. Acta 594 (1981) 105-176.
3. Vignais, P.M., Billoud, B. and Meyer, J. Classification and phylogeny of hydrogenases. FEMS Microbiol. Rev. 25 (2001) 455-501. [PMID: 11524134]
Common name: phenylalanine 2-monooxygenase
Reaction: L-phenylalanine + O2 = 2-phenylacetamide + CO2 + H2O
Other name(s): L-phenylalanine oxidase (deaminating and decarboxylating); phenylalanine (deaminating, decarboxylating)oxidase
Systematic name: L-phenylalanine:oxygen 2-oxidoreductase (decarboxylating)
Comments: The reaction shown above is about 80% of the reaction catalysed; the remaining 20% is:
L-phenylalanine + O2 + H2O = 3-phenylpyruvic acid + NH3 + H2O2
a reaction similar to that of EC 1.4.3.2, L-amino-acid oxidase.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 84012-76-0; 69403-11-8
References:
1. Koyama, H. Purification and characterization of a novel L-phenylalanine oxidase (deaminating and decarboxylating) from Pseudomonas sp. P-501. J. Biochem. (Tokyo) 92 (1982) 1235-1240. [PMID: 7174643]
2. Koyama, H. Oxidation and oxygenation of L-amino acids catalyzed by a L-phenylalanine oxidase (deaminating and decarboxylating) from Pseudomonas sp. P-501. J. Biochem. (Tokyo) 96 (1984) 421-427. [PMID: 6501250]
3. Koyama, H. A simple and rapid enzymatic determination of L-phenylalanine with a novel L-phenylalanine oxidase (deaminating and decarboxylating) from Pseudomonas sp. P-501. Clin. Chim. Acta 1361 (1984) 131-136. [PMID: 6692570]
4. Koyama, H. and Suzuki, H. Spectral and kinetic studies on Pseudomonas L-phenylalanine oxidase (deaminating and decarboxylating). J. Biochem. (Tokyo) 100 (1986) 859-866. [PMID: 3818566]
[EC 1.14.13.45 Transferred entry: now EC 1.14.18.2 CMP-N-acetylneuraminate monooxygenase. (EC 1.14.13.45 created 1992, deleted 2003)]
Common name: (S)-limonene 3-monooxygenase
Reaction: (-)-(S)-limonene + NADPH + H+ + O2 = (-)-trans-isopiperitenol + NADP+ + H2O
For diagram click here.
Glossary:
limonene: a monoterpenoid
Other name(s): (-)-limonene 3-hydroxylase; (-)-limonene 3-monooxygenase; (-)-limonene,NADPH:oxygen oxidoreductase (3-hydroxylating)
Systematic name: (S)-limonene,NADPH:oxygen oxidoreductase (3-hydroxylating)
Comments: High specificity, but NADH can act instead of NADPH, although more slowly. A heme-thiolate protein (P-450).
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 138066-92-9
References:
1. Karp, F., Mihaliak, C.A., Harris, J.L. and Croteau, R. Monoterpene biosynthesis: specificity of the hydroxylations of (-)-limonene by enzyme preparations from peppermint (Mentha piperita), spearmint (Mentha spicata), and perilla (Perilla frutescens) leaves. Arch. Biochem. Biophys. 276 (1990) 219-226. [PMID: 2297225]
Common name: (S)-limonene 6-monooxygenase
Reaction: (-)-(S)-limonene + NADPH + H+ + O2 = (-)-trans-carveol + NADP+ + H2O
For diagram click here.
Glossary:
limonene: a monoterpenoid
Other name(s): (-)-limonene 6-hydroxylase; (-)-limonene 6-monooxygenase; (-)-limonene,NADPH:oxygen oxidoreductase (6-hydroxylating)
Systematic name: (S)-limonene,NADPH:oxygen oxidoreductase (6-hydroxylating)
Comments: High specificity, but NADH can act instead of NADPH, but more slowly. A heme-thiolate protein (P-450).
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 138066-93-0
References:
1. Karp, F., Mihaliak, C.A., Harris, J.L. and Croteau, R. Monoterpene biosynthesis: specificity of the hydroxylations of (-)-limonene by enzyme preparations from peppermint (Mentha piperita), spearmint (Mentha spicata), and perilla (Perilla frutescens) leaves. Arch. Biochem. Biophys. 276 (1990) 219-226. [PMID: 90120595]
Common name: (S)-limonene 7-monooxygenase
Reaction: (-)-(S)-limonene + NADPH + H+ + O2 = (-)-perillyl alcohol + NADP+ + H2O
For diagram click here.
Glossary:
limonene: a monoterpenoid
Other name(s): (-)-limonene 7-monooxygenase; (-)-limonene hydroxylase; (-)-limonene monooxygenase; (-)-limonene,NADPH:oxygen oxidoreductase (7-hydroxylating)
Systematic name: (S)-limonene,NADPH:oxygen oxidoreductase (7-hydroxylating)
Comments: High specificity, but NADH can act instead of NADPH, although more slowly. A heme-thiolate protein (P-450).
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 122653-75-2
References:
1. Karp, F., Mihaliak, C.A., Harris, J.L. and Croteau, R. Monoterpene biosynthesis: specificity of the hydroxylations of (-)-limonene by enzyme preparations from peppermint (Mentha piperita), spearmint (Mentha spicata), and perilla (Perilla frutescens) leaves. Arch. Biochem. Biophys. 276 (1990) 219-226. [PMID: 2297225]
Common name: vanillate monooxygenase
Reaction: vanillate + O2 + NADH + H+ = 3,4-dihydroxybenzoate + NAD+ + H2O + formaldehyde
Glossary entries: vanillate = 4-hydroxy-3-methoxybenzoate
Other name(s): 4-hydroxy-3-methoxybenzoate demethylase; vanillate demethylase
Systematic name: vanillate:oxygen oxidoreductase (demethylating)
Comments: Forms part of the vanillin degradation pathway in Arthrobacter sp.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number:
References:
1. Brunel, F. and Davison, J. Cloning and sequencing of Pseudomonas genes encoding vanillate demethylase. J. Bacteriol. 170 (1988) 4924-4930. [PMID: 3170489]
2. Priefert, H., Rabenhorst, J. and Steinbuchel, A. Molecular characterization of genes of Pseudomonas sp. strain HR199 involved in bioconversion of vanillin to protocatechuate. J. Bacteriol. 179 (1997) 2595-2607. [PMID: 9098058]
Common name: CMP-N-acetylneuraminate monooxygenase
Reaction: CMP-N-acetylneuraminate + 2 ferrocytrochrome b5 + O2 + 2 H+ = CMP-N-glycoloylneuraminate + 2 ferricytrochrome b5 + H2O
Other name(s): CMP-N-acetylneuraminic acid hydroxylase; CMP-Neu5Ac hydroxylase; cytidine monophosphoacetylneuraminate monooxygenase
Systematic name: CMP-N-acetylneuraminate,ferrocytrochrome-b5:oxygen oxidoreductase (N-acetyl-hydroxylating)
Comments: This enzyme contains both a Rieske-type [2Fe-2S] cluster and a second iron site. The ferricytochrome b5 produced is reduced by NADH and cytochrome-b5 reductase (EC 1.6.2.2). The enzyme can be activated by Fe2+ or Fe3+.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 116036-67-0
References:
1. Shaw, L. and Schauer, R. The biosynthesis of N-glycoloylneuraminic acid occurs by hydroxylation of the CMP-glycoside of N-acetylneuraminic acid. Biol. Chem. Hoppe-Seyler 369 (1988) 477-486. [PMID: 3202954]
2. Kozutsumi, Y., Kawano, T., Yamakawa, T. and Suzuki, A. Participation of cytochrome b5 in CMP-N-acetylneuraminic acid hydroxylation in mouse liver cytosol. J. Biochem. (Tokyo) 109 (1990) 704-706.[PMID: 1964451]
3. Schneckenburger, P., Shaw, L. and Schauer, R. Purification, characterization and reconstitution of CMP-N-acetylneuraminate hydroxylase from mouse liver. Glycoconj. J. 11 (1994) 194-203. [PMID: 7841794]
4. Kawano, T., Koyama, S., Takematsu, H., Kozutsumi, Y., Kawasaki, H., Kawashima, S., Kawasaki, T. and Suzuki, A. Molecular cloning of cytidine monophospho-N-acetylneuraminic acid hydroxylase. Regulation of species- and tissue-specific expression of N-glycolylneuraminic acid. J. Biol. Chem. 270 (1995) 16458-16463. [PMID: 7608218]
5. Schlenzka, W., Shaw, L., Kelm, S., Schmidt, C.L., Bill, E., Trautwein, A.X., Lottspeich, F. and Schauer, R. CMP-N-acetylneuraminic acid hydroxylase: the first cytosolic Rieske iron-sulphur protein to be described in Eukarya. FEBS Lett. 385 (1996) 197-200. [PMID: 8647250]
Common name: stearoyl-CoA 9-desaturase
Reaction: stearoyl-CoA + 2 ferrocytrochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytrochrome b5 + H2O
Other name(s): δ9-desaturase; acyl-CoA desaturase; fatty acid desaturase; stearoyl-CoA, hydrogen-donor:oxygen oxidoreductase
Systematic name: stearoyl-CoA,ferrocytochrome-b5:oxygen oxidoreductase (9,10-dehydrogenating)
Comments: An iron protein. The rat liver enzyme is an enzyme system involving cytochrome b5 and EC 1.6.2.2, cytochrome-b5 reductase. The ferricytochrome b5 produced is reduced by NADH and cytochrome-b5 reductase (EC 1.6.2.2).
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 9014-34-0
References:
1. Fulco, A.J. and Bloch, K. Cofactor requirements for the formation of δ9-unsaturated fatty acids in Mycobacterium phlei. J. Biol. Chem. 239 (1964) 993-997.
2. Oshino, N., Imai, Y. and Sato, R. Electron-transfer mechanism associated with fatty acid desaturation catalyzed by liver microsomes. Biochim. Biophys. Acta 128 (1966) 13-27. [PMID: 4382040]
3. Oshino, N., Imai, Y. and Sato, R. A function of cytochrome b5 in fatty acid desaturation by rat liver microsomes. J. Biochem. (Tokyo) 69 (1971) 155-167. [PMID: 5543646]
4. Strittmatter, P., Sputz, L., Corcoran, D., Rogers, M.J., Setlow, B. and Redline, R. Purification and properties of rat liver microsomal stearyl coenzyme A desaturase. Proc. Natl. Acad. Sci. USA 71 (1974) 4565-4569. [PMID: 4373719]
[EC 1.14.99.18 Deleted entry: CMP-N-acetylneuraminate monooxygenase. (EC 1.14.99.18 created 1976, modified 1999, deleted 2003)]
Common name: [methionine synthase] reductase
Reaction: 2 [methionine synthase]-methylcob(I)alamin + 2 S-adenosylhomocysteine + NADP+ = 2 [methionine synthase]-cob(II)alamin + NADPH + H+ + 2 S-adenosyl-L-methionine
For diagram click here
Systematic name: [methionine synthase]-methylcob(I)alamin,S-adenosylhomocysteine:NADP+ oxidoreductase
Comments: In humans, the enzyme is a flavoprotein containing FAD and FMN. The substrate of the enzyme is the inactivated [Co(II)] form of EC 2.1.1.13, methionine synthase. Electrons are transferred from NADPH to FAD to FMN. Defects in this enzyme lead to hereditary hyperhomocysteinemia.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 207004-87-3
References:
1. Leclerc, D., Wilson, A., Dumas, R., Gafuik, C., Song, D., Watkins, D., Heng, H.H.Q., Rommens, J.M., Scherer, S.W., Rosenblatt, D.S. and Gravel, R.A. Cloning and mapping of a cDNA for methionine synthase reductase, a flavoprotein defective in patients with homocystinuria. Proc. Natl. Acad. Sci. USA 95 (1998) 3059-3064. [PMID: 9501215]
2. Olteanu, H. and Banerjee, R. Human methionine synthase reductase, a soluble P-450 reductase-like dual flavoprotein, is sufficient for NADPH-dependent methionine synthase activation. J. Biol. Chem. 276 (2001) 35558-35563. [PMID: 11466310]
3. Olteanu, H., Munson, T. and Banerjee, R. Differences in the efficiency of reductive activation of methionine synthase and exogenous electron acceptors between the common polymorphic variants of human methionine synthase reductase. Biochemistry 41 (2002) 13378-13385. [PMID: 12416982]
Common name: aureusidin synthase
Reaction: (1) 2',4,4',6'-tetrahydroxychalcone + O2 = aureusidin + H2O
(2) 2',3,4,4',6'-pentahydroxychalcone + 0.5 O2 = aureusidin + H2O
For diagram click here.
Glossary: chalcone = 1,3-diphenylprop-2-en-1-one
Other name(s):
Systematic name: 2',4,4',6'-tetrahydroxychalcone:oxygen oxidoreductase
Comments: A copper-containing glycoprotein that plays a key role in the yellow coloration of flowers such as snapdragon. The enzyme is a homologue of plant polyphenol oxidase [1] and catalyses two separate chemical transformations, i.e. 3-hydroxylation and oxidative cyclization (2',α-dehydrogenation). H2O2 activates reaction (1) but inhibits reaction (2).
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number:
References:
1. Nakayama, T., Yonekura-Sakakibara, K., Sato, T., Kikuchi, S., Fukui, Y., Fukuchi-Mizutani, M., Ueda, T., Nakao, M., Tanaka, Y., Kusumi, T. and Nishino, T. Aureusidin synthase: A polyphenol oxidase homolog responsible for flower coloration. Science 290 (2000) 1163-1166. [PMID: 11073455]
2. Nakayama, T., Sato, T., Fukui, Y., Yonekura-Sakakibara, K., Hayashi, H., Tanaka, Y., Kusumi, T. and Nishino, T. Specificity analysis and mechanism of aurone synthesis catalyzed by aureusidin synthase, a polyphenol oxidase homolog responsible for flower coloration. FEBS Lett. 499 (2001) 107-111. [PMID: 11418122]
3. Sato, T., Nakayama, T., Kikuchi, S., Fukui, Y., Yonekura-Sakakibara, K., Ueda, T., Nishino, T., Tanaka, Y. and Kusumi, T. Enzymatic formation of aurones in the extracts of yellow snapdragon flowers. Plant Sci. 160 (2001) 229-236. [PMID: 11164594]
Common name: selenate reductase
Reaction: selenite + H2O + acceptor = selenate + reduced acceptor
Systematic name: selenite:reduced acceptor oxidoreductase
Comments: The periplasmic enzyme from Thauera selenatis is a complex comprising three heterologous subunits (α, β and γ) that contains molybdenum, iron, acid-labile sulfide and heme b as cofactor constituents. Nitrate, nitrite, chlorate and sulfate are not substrates. A number of compounds, including acetate, lactate, pyruvate, and certain sugars, amino acids, fatty acids, di- and tricarboxylic acids, and benzoate can serve as electron donors.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number:
References:
1. Schröder, I., Rech, S., Krafft, T. and Macy, J.M. Purification and characterization of the selenate reductase from Thauera selenatis. J. Biol. Chem. 272 (1997) 23765-23768. [PMID: 9295321]
2. Macy, J.M., Rech, S., Auling, G., Dorsch, M., Stackebrandt, E. and Sly, L.I. Thauera selenatis gen. nov., sp. nov., a member of the beta subclass of Proteobacteria with a novel type of anaerobic respiration. Int. J. Syst. Bacteriol. 43 (1993) 135-142. [PMID: 8427805]
3. Krafft, T., Bowen, A., Theis, F. and Macy, J.M. Cloning and sequencing of the genes encoding the periplasmic-cytochrome B-containing selenate reductase of Thauera selenatis. DNA Seq. 10 (2000) 365-377. [PMID: 10826693]
4. Stolz, J.F. and Oremland, R.S. Bacterial respiration of arsenic and selenium. FEMS Microbiol. Rev. 23 (1999) 615-627. [PMID: 10525169]
Common name: thyroxine 5'-deiodinase
Reaction: 3,5,3'-triiodo-L-thyronine + iodide + A + H+ = L-thyroxine + AH2
Other name(s): diiodothyronine 5'-deiodinase [ambiguous]; iodothyronine 5'-deiodinase; iodothyronine outer ring monodeiodinase; type I iodothyronine deiodinase; type II iodothyronine deiodinase; thyroxine 5-deiodinase [misleading]; L-thyroxine iodohydrolase (reducing)
Systematic name: acceptor:3,5,3'-triiodo-L-thyronine oxidoreductase (iodinating)
Comments: The enzyme activity has only been demonstrated in the direction of 5'-deiodination, which renders the thyroid hormone more active. The enzyme consists of type I and type II enzymes, both containing selenocysteine, but with different kinetics. For the type I enzyme the first reaction is a reductive deiodination converting the -Se-H group of the enzyme into an -Se-I group; the reductant then reconverts this into -Se-H, releasing iodide.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 70712-46-8
References:
1. Chopra, I.J. and Teco, G.N.C. Characteristics of inner ring (3 or 5) monodeiodination of 3,5-diiodothyronine in rat liver: evidence suggesting marked similarities of inner and outer ring deiodinases for iodothyronines. Endocrinology 110 (1982) 89-97. [PMID: 7053997]
2. Goswani, A., Leonard, J.L. and Rosenberg, I.N. Inhibition by coumadin anticoagulants of enzymatic outer ring monodeiodination of iodothyronines. Biochem. Biophys. Res. Commun. 104 (1982) 1231-1238. [PMID: 6176242]
3. Smallridge, R.C., Burman, K.D., Ward, K.E., Wartofsky, L., Dimond, R.C., Wright, F.D. and Lathan, K.R. 3',5'-Diiodothyronine to 3'-monoiodothyronine conversion in the fed and fasted rat: enzyme characteristics and evidence for two distinct 5'-deiodinases. Endocrinology 108 (1981) 2336-2345. [PMID: 7227308]
4. Körhle, J. Iodothyronine deiodinases. Methods Enzymol. 347 (2002) 125-167. [PMID: 11898402]
Common name: thyroxine 5-deiodinase
Reaction: 3,3',5'-triiodo-L-thyronine + iodide + A + H+ = L-thyroxine + AH2
Other name(s): diiodothyronine 5'-deiodinase[ambiguous]; iodothyronine 5-deiodinase; iodothyronine inner ring monodeiodinase; type III iodothyronine deiodinase
Systematic name: acceptor:3,3',5'-triiodo-L-thyronine oxidoreductase (iodinating)
Comments: The enzyme activity has only been demonstrated in the direction of 5-deiodination. This removal of the 5-iodine, i.e. from the inner ring, largely inactivates the hormone thyroxine.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number:
References:
1. Chopra, I.J. and Teco, G.N.C. Characteristics of inner ring (3 or 5) monodeiodination of 3,5-diiodothyronine in rat liver: evidence suggesting marked similarities of inner and outer ring deiodinases for iodothyronines. Endocrinology 110 (1982) 89-97. [PMID: 7053997]
2. Körhle, J. Iodothyronine deiodinases. Methods Enzymol. 347 (2002) 125-167. [PMID: 11898402]