EC |
1.1.3.11 |
Accepted name: |
L-sorbose oxidase |
Reaction: |
L-sorbose + O2 = 5-dehydro-D-fructose + H2O2 |
Systematic name: |
L-sorbose:oxygen 5-oxidoreductase |
Comments: |
Also acts on D-glucose, D-galactose and D-xylose, but not on D-fructose. 2,6-Dichloroindophenol can act as acceptor. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37250-81-0 |
References: |
1. |
Yamada, Y., Iizuka, K., Aida, K. and Uemura, T. Enzymatic studies on the oxidation of sugar and sugar alcohol. 3. Purification and properties of L-sorbose oxidase from Trametes sanguinea. J. Biochem. (Tokyo) 62 (1967) 223–229. [PMID: 5586487] |
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[EC 1.1.3.11 created 1972] |
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|
|
EC |
1.1.3.12 |
Accepted name: |
pyridoxine 4-oxidase |
Reaction: |
pyridoxine + O2 = pyridoxal + H2O2 |
Other name(s): |
pyridoxin 4-oxidase; pyridoxol 4-oxidase |
Systematic name: |
pyridoxine:oxygen 4-oxidoreductase |
Comments: |
A flavoprotein. Can also use 2,6-dichloroindophenol as an acceptor. |
Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37250-82-1 |
References: |
1. |
Sundaram, T.K. and Snell, E.E. The bacterial oxidation of vitamin B6. V. The enzymatic formation of pyridoxal and isopyridoxal from pyridoxine. J. Biol. Chem. 244 (1969) 2577–2584. [PMID: 5769992] |
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[EC 1.1.3.12 created 1972, modified 1976] |
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|
EC |
1.1.3.16 |
Accepted name: |
ecdysone oxidase |
Reaction: |
ecdysone + O2 = 3-dehydroecdysone + H2O2 |
Other name(s): |
β-ecdysone oxidase |
Systematic name: |
ecdysone:oxygen 3-oxidoreductase |
Comments: |
2,6-Dichloroindophenol can act as an acceptor. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 56803-12-4 |
References: |
1. |
Koolman, J. and Karlson, P. Ecdysone oxidase, an enzyme from the blowfly Calliphora erythrocephala (Meigen). Hoppe-Seyler's Z. Physiol. Chem. 35 (1975) 1131. [PMID: 297] |
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[EC 1.1.3.16 created 1976] |
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EC |
1.1.5.9 |
Accepted name: |
glucose 1-dehydrogenase (FAD, quinone) |
Reaction: |
D-glucose + a quinone = D-glucono-1,5-lactone + a quinol |
Other name(s): |
glucose dehydrogenase (Aspergillus); FAD-dependent glucose dehydrogenase; D-glucose:(acceptor) 1-oxidoreductase; glucose dehydrogenase (acceptor); gdh (gene name) |
Systematic name: |
D-glucose:quinone 1-oxidoreductase |
Comments: |
A glycoprotein containing one mole of FAD per mole of enzyme. 2,6-Dichloroindophenol can act as acceptor. cf. EC 1.1.5.2, glucose 1-dehydrogenase (PQQ, quinone). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37250-84-3 |
References: |
1. |
Bak, T.-G. Studies on glucose dehydrogenase of Aspergillus oryzae. II. Purification and physical and chemical properties. Biochim. Biophys. Acta 139 (1967) 277–293. [DOI] [PMID: 6034674] |
2. |
Cavener, D.R. and MacIntyre, R.J. Biphasic expression and function of glucose dehydrogenase in Drosophila melanogaster. Proc. Natl. Acad. Sci. USA 80 (1983) 6286–6288. [DOI] [PMID: 6413974] |
3. |
Lovallo, N. and Cox-Foster, D.L. Alteration in FAD-glucose dehydrogenase activity and hemocyte behavior contribute to initial disruption of Manduca sexta immune response to Cotesia congregata parasitoids. J. Insect Physiol. 45 (1999) 1037–1048. [DOI] [PMID: 12770264] |
4. |
Inose, K., Fujikawa, M., Yamazaki, T., Kojima, K. and Sode, K. Cloning and expression of the gene encoding catalytic subunit of thermostable glucose dehydrogenase from Burkholderia cepacia in Escherichia coli. Biochim. Biophys. Acta 1645 (2003) 133–138. [DOI] [PMID: 12573242] |
5. |
Sygmund, C., Klausberger, M., Felice, A.K. and Ludwig, R. Reduction of quinones and phenoxy radicals by extracellular glucose dehydrogenase from Glomerella cingulata suggests a role in plant pathogenicity. Microbiology 157 (2011) 3203–3212. [DOI] [PMID: 21903757] |
6. |
Sygmund, C., Staudigl, P., Klausberger, M., Pinotsis, N., Djinovic-Carugo, K., Gorton, L., Haltrich, D. and Ludwig, R. Heterologous overexpression of Glomerella cingulata FAD-dependent glucose dehydrogenase in Escherichia coli and Pichia pastoris. Microb. Cell Fact. 10:106 (2011). [DOI] [PMID: 22151971] |
|
[EC 1.1.5.9 created 1972 as EC 1.1.99.10, modified 1976, transferred 2013 to EC 1.1.5.9] |
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|
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|
EC |
1.1.5.10 |
Accepted name: |
D-2-hydroxyacid dehydrogenase (quinone) |
Reaction: |
(R)-2-hydroxyacid + a quinone = 2-oxoacid + a quinol |
Other name(s): |
(R)-2-hydroxy acid dehydrogenase; (R)-2-hydroxy-acid:(acceptor) 2-oxidoreductase; D-lactate dehydrogenase (ambiguous) |
Systematic name: |
(R)-2-hydroxyacid:quinone oxidoreductase |
Comments: |
The enzyme from mammalian kidney contains one mole of FAD per mole of enzyme.(R)-lactate, (R)-malate and meso-tartrate are good substrates. Ubiquinone-1 and the dye 2,6-dichloroindophenol can act as acceptors; NAD+ and NADP+ are not acceptors. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Tubbs, P.K. and Greville, G.D. Dehydrogenation of D-lactate by a soluble enzyme from kidney mitochondria. Biochim. Biophys. Acta 34 (1959) 290–291. [DOI] [PMID: 13839714] |
2. |
Tubbs, P.K. and Greville, G.D. The oxidation of D-α-hydroxy acids in animal tissues. Biochem. J. 81 (1961) 104–114. [PMID: 13922962] |
3. |
Cammack, R. Assay, purification and properties of mammalian D-2-hydroxy acid dehydrogenase. Biochem. J. 115 (1969) 55–64. [PMID: 5359443] |
4. |
Cammack, R. D-2-hydroxy acid dehydrogenase from animal tissue. Methods Enzymol. 41 (1975) 323–329. [DOI] [PMID: 236454] |
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[EC 1.1.5.10 created 2014] |
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EC
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1.1.99.10
|
Transferred entry: | glucose dehydrogenase (acceptor). Now EC 1.1.5.9, glucose 1-dehydrogenase (FAD, quinone)
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[EC 1.1.99.10 created 1972, modified 1976, deleted 2013] |
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EC
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1.1.99.11
|
Transferred entry: | fructose 5-dehydrogenase, now classified as EC 1.1.5.14, fructose 5-dehydrogenase.
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[EC 1.1.99.11 created 1972, deleted 2021.] |
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|
EC |
1.1.99.12 |
Accepted name: |
sorbose dehydrogenase |
Reaction: |
L-sorbose + acceptor = 5-dehydro-D-fructose + reduced acceptor |
Other name(s): |
L-sorbose:(acceptor) 5-oxidoreductase |
Systematic name: |
L-sorbose:acceptor 5-oxidoreductase |
Comments: |
2,6-Dichloroindophenol can act as acceptor. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37250-86-5 |
References: |
1. |
Sato, K., Yamada, Y., Aida, K. and Uemara, T. Enzymatic studies on the oxidation of sugar and sugar alcohol. 8. Particle-bound L-sorbose dehydrogenase from Gluconobacter suboxydans. J. Biochem. (Tokyo) 66 (1969) 521–527. [PMID: 5354025] |
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[EC 1.1.99.12 created 1972] |
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EC |
1.1.99.14 |
Accepted name: |
glycolate dehydrogenase |
Reaction: |
glycolate + acceptor = glyoxylate + reduced acceptor |
Other name(s): |
glycolate oxidoreductase; glycolic acid dehydrogenase; glycolate:(acceptor) 2-oxidoreductase |
Systematic name: |
glycolate:acceptor 2-oxidoreductase |
Comments: |
Also acts on (R)-lactate. 2,6-Dichloroindophenol and phenazine methosulfate can act as acceptors. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37368-32-4 |
References: |
1. |
Lord, J.M. Glycolate oxidoreductase in Escherichia coli. Biochim. Biophys. Acta 267 (1972) 227–237. [DOI] [PMID: 4557653] |
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[EC 1.1.99.14 created 1978] |
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|
EC |
1.1.99.18 |
Accepted name: |
cellobiose dehydrogenase (acceptor) |
Reaction: |
cellobiose + acceptor = cellobiono-1,5-lactone + reduced acceptor |
Other name(s): |
cellobiose dehydrogenase; cellobiose oxidoreductase; Phanerochaete chrysosporium cellobiose oxidoreductase; CBOR; cellobiose oxidase; cellobiose:oxygen 1-oxidoreductase; CDH; cellobiose:(acceptor) 1-oxidoreductase |
Systematic name: |
cellobiose:acceptor 1-oxidoreductase |
Comments: |
Also acts, more slowly, on cello-oligosaccharides, lactose and D-glucosyl-1,4-β-D-mannose. The enzyme from the white rot fungus Phanerochaete chrysosporium is unusual in having two redoxin domains, one containing a flavin and the other a protoheme group. It transfers reducing equivalents from cellobiose to two types of redox acceptor: two-electron oxidants, including redox dyes, benzoquinones, and molecular oxygen, and one-electron oxidants, including semiquinone species, iron(II) complexes, and the model acceptor cytochrome c [9]. 2,6-Dichloroindophenol can act as acceptor in vitro. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 54576-85-1 |
References: |
1. |
Coudray, M.-R., Canebascini, G. and Meier, H. Characterization of a cellobiose dehydrogenase in the cellulolytic fungus porotrichum (Chrysosporium) thermophile. Biochem. J. 203 (1982) 277–284. [PMID: 7103940] |
2. |
Dekker, R.F.H. Induction and characterization of a cellobiose dehydrogenase produced by a species of Monilia. J. Gen. Microbiol. 120 (1980) 309–316. |
3. |
Dekker, R.F.H. Cellobiose dehydrogenase produced by Monilia sp. Methods Enzymol. 160 (1988) 454–463. |
4. |
Habu, N., Samejima, M., Dean, J.F. and Eriksson, K.E. Release of the FAD domain from cellobiose oxidase by proteases from cellulolytic cultures of Phanerochaete chrysosporium. FEBS Lett. 327 (1993) 161–164. [DOI] [PMID: 8392950] |
5. |
Baminger, U., Subramaniam, S.S., Renganathan, V. and Haltrich, D. Purification and characterization of cellobiose dehydrogenase from the plant pathogen Sclerotium (Athelia) rolfsii. Appl. Environ. Microbiol. 67 (2001) 1766–1774. [DOI] [PMID: 11282631] |
6. |
Hallberg, B.M., Henriksson, G., Pettersson, G. and Divne, C. Crystal structure of the flavoprotein domain of the extracellular flavocytochrome cellobiose dehydrogenase. J. Mol. Biol. 315 (2002) 421–434. [DOI] [PMID: 11786022] |
7. |
Ayers, A.R., Ayers, S.B. and Eriksson, K.-E. Cellobiose oxidase, purification and partial characterization of a hemoprotein from Sporotrichum pulverulentum. Eur. J. Biochem. 90 (1978) 171–181. [DOI] [PMID: 710416] |
8. |
Ayers, A.R. and Eriksson, K.-E. Cellobiose oxidase from Sporotrichum pulverulentum. Methods Enzymol. 89 (1982) 129–135. [PMID: 7144569] |
9. |
Mason, M.G., Nicholls, P., Divne, C., Hallberg, B.M., Henriksson, G. and Wilson, M.T. The heme domain of cellobiose oxidoreductase: a one-electron reducing system. Biochim. Biophys. Acta 1604 (2003) 47–54. [DOI] [PMID: 12686420] |
|
[EC 1.1.99.18 created 1983, modified 2002 (EC 1.1.5.1 created 1983, incorporated 2002, EC 1.1.3.25 created 1986, incorporated 2005)] |
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EC |
1.1.99.20 |
Accepted name: |
alkan-1-ol dehydrogenase (acceptor) |
Reaction: |
primary alcohol + acceptor = aldehyde + reduced acceptor |
Other name(s): |
polyethylene glycol dehydrogenase; alkan-1-ol:(acceptor) oxidoreductase |
Systematic name: |
alkan-1-ol:acceptor oxidoreductase |
Comments: |
A quinoprotein. Acts on C3-C16 linear-chain saturated primary alcohols, C4-C7 aldehydes and on non-ionic surfactants containing polyethylene glycol residues, such as Tween 40 and 60, but not on methanol and only very slowly on ethanol. 2,6-Dichloroindophenol can act as acceptor. cf. EC 1.1.99.8 alcohol dehydrogenase (acceptor). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 75496-55-8 |
References: |
1. |
Kawai, F., Kimura, T., Tani, Y., Yamada, H., Ueno, T. and Fukami, H. Identification of reaction-products of polyethylene-glycol dehydrogenase. Agric. Biol. Chem. 47 (1983) 1669–1671. |
2. |
Kawai, F., Yamanaka, H., Ameyama, M., Shinagawa, E., Matsushita, K. and Adachi, O. Identification of the prosthetic group and further characterization of a novel enzyme, polyethylene-glycol dehydrogenase. Agric. Biol. Chem. 49 (1985) 1071–1076. |
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[EC 1.1.99.20 created 1989] |
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EC
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1.1.99.23
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Transferred entry: | polyvinyl-alcohol dehydrogenase (acceptor). Now EC 1.1.2.6, polyvinyl alcohol dehydrogenase (cytochrome)
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[EC 1.1.99.23 created 1989, deleted 2010] |
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EC |
1.1.99.26 |
Accepted name: |
3-hydroxycyclohexanone dehydrogenase |
Reaction: |
3-hydroxycyclohexanone + acceptor = cyclohexane-1,3-dione + reduced acceptor |
Systematic name: |
3-hydroxycyclohexanone:acceptor 1-oxidoreductase |
Comments: |
2,6-Dichloroindophenol and methylene blue can act as acceptors. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 123516-44-9 |
References: |
1. |
Dangel, W., Tschech, A. and Fuchs, G. Enzyme-reactions involved in anaerobic cyclohexanol metabolism by a denitrifying Pseudomonas species. Arch. Microbiol. 152 (1989) 273–279. [PMID: 2505723] |
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[EC 1.1.99.26 created 1992] |
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EC
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1.3.99.11
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Transferred entry: | dihydroorotate dehydrogenase. As the acceptor is now known, the enzyme has been transferred to EC 1.3.5.2, dihydroorotate dehydrogenase
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[EC 1.3.99.11 created 1983, deleted 2009] |
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|
EC |
1.3.99.14 |
Accepted name: |
cyclohexanone dehydrogenase |
Reaction: |
cyclohexanone + acceptor = cyclohex-2-enone + reduced acceptor |
Other name(s): |
cyclohexanone:(acceptor) 2-oxidoreductase |
Systematic name: |
cyclohexanone:acceptor 2-oxidoreductase |
Comments: |
2,6-Dichloroindophenol can act as acceptor. The corresponding ketones of cyclopentane and cycloheptane cannot act as donors. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 123516-43-8 |
References: |
1. |
Dangel, W., Tschech, A. and Fuchs, G. Enzyme-reactions involved in anaerobic cyclohexanol metabolism by a denitrifying Pseudomonas species. Arch. Microbiol. 152 (1989) 273–279. [PMID: 2505723] |
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[EC 1.3.99.14 created 1992] |
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EC |
1.5.8.2 |
Accepted name: |
trimethylamine dehydrogenase |
Reaction: |
trimethylamine + H2O + electron-transfer flavoprotein = dimethylamine + formaldehyde + reduced electron-transfer flavoprotein |
Systematic name: |
trimethylamine:electron-transfer flavoprotein oxidoreductase (demethylating) |
Comments: |
A number of alkyl-substituted derivatives of trimethylamine can also act as electron donors; phenazine methosulfate and 2,6-dichloroindophenol can act as electron acceptors. Contains FAD and a [4Fe-4S] cluster. |
Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 39307-09-0 |
References: |
1. |
Colby, J. and Zatman, L.J. The purification and properties of a bacterial trimethylamine dehydrogenase. Biochem. J. 121 (1971) 9P–10P. [PMID: 5116569] |
2. |
Steenkamp, D.J. and Singer, T.P. Participation of the iron-sulphur cluster and of the covalently bound coenzyme of trimethylamine dehydrogenase in catalysis. Biochem. J. 169 (1978) 361–369. [PMID: 204297] |
3. |
Huang, L.X., Rohlfs, R.J. and Hille, R. The reaction of trimethylamine dehydrogenase with electron transferring flavoprotein. J. Biol. Chem. 270 (1995) 23958–23965. [DOI] [PMID: 7592591] |
4. |
Jones, M., Talfournier, F., Bobrov, A., Grossmann, J.G., Vekshin, N., Sutcliffe, M.J. and Scrutton, N.S. Electron transfer and conformational change in complexes of trimethylamine dehydrogenase and electron transferring flavoprotein. J. Biol. Chem. 277 (2002) 8457–8465. [DOI] [PMID: 11756429] |
5. |
Scrutton, N.S. and Sutcliffe, M.J. Trimethylamine dehydrogenase and electron transferring flavoprotein. Subcell. Biochem. 35 (2000) 145–181. [PMID: 11192721] |
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[EC 1.5.8.2 created 1976 as EC 1.5.99.7, transferred 2002 to EC 1.5.8.2] |
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EC |
1.5.99.5 |
Accepted name: |
methylglutamate dehydrogenase |
Reaction: |
N-methyl-L-glutamate + acceptor + H2O = L-glutamate + formaldehyde + reduced acceptor |
Other name(s): |
N-methylglutamate dehydrogenase; N-methyl-L-glutamate:(acceptor) oxidoreductase (demethylating) |
Systematic name: |
N-methyl-L-glutamate:acceptor oxidoreductase (demethylating) |
Comments: |
A number of N-methyl-substituted amino acids can act as donor; 2,6-dichloroindophenol is the best acceptor. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37217-26-8 |
References: |
1. |
Hersh, L.B., Stark, M.J., Worthen, S. and Fiero, M.K. N-Methylglutamate dehydrogenase: kinetic studies on the solubilized enzyme. Arch. Biochem. Biophys. 150 (1972) 219–226. [DOI] [PMID: 5028076] |
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[EC 1.5.99.5 created 1976] |
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EC |
1.5.99.6 |
Accepted name: |
spermidine dehydrogenase |
Reaction: |
spermidine + acceptor + H2O = propane-1,3-diamine + 4-aminobutanal + reduced acceptor |
Glossary: |
spermidine = N-(3-aminopropyl)butane-1,4-diamine |
Other name(s): |
spermidine:(acceptor) oxidoreductase |
Systematic name: |
spermidine:acceptor oxidoreductase |
Comments: |
A flavohemoprotein (FAD). Ferricyanide, 2,6-dichloroindophenol and cytochrome c can act as acceptor. 4-Aminobutanal condenses non-enzymically to 1-pyrroline. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9076-64-6 |
References: |
1. |
Tabor, C.W. and Kellogg, P.D. Identification of flavin adenine dinucleotide and heme in a homogeneous spermidine dehydrogenase from Serratia marcescens. J. Biol. Chem. 245 (1970) 5424–5433. [PMID: 4918845] |
2. |
Tabor, H. and Tabor, C.W. Biosynthesis and metabolism of 1,4-diaminobutane, spermidine, spermine, and related amines. IIE2a Speridine dehydrogenase. Adv. Enzymol. Relat. Areas Mol. Biol. 36 (1972) 225–226. |
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[EC 1.5.99.6 created 1976] |
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EC |
1.5.99.12 |
Accepted name: |
cytokinin dehydrogenase |
Reaction: |
N6-prenyladenine + acceptor + H2O = adenine + 3-methylbut-2-enal + reduced acceptor |
Glossary: |
zeatin = (E)-2-methyl-4-(9H-purin-6-ylamino)but-2-en-1-ol = (E)-N6-(4-hydroxy-3-methylbut-2-enyl)adenine
N6-prenyladenine = N6-(3-methylbut-2-en-1-yl)purin-6-amine |
Other name(s): |
N6-dimethylallyladenine:(acceptor) oxidoreductase; 6-N-dimethylallyladenine:acceptor oxidoreductase; OsCKX2; CKX; cytokinin oxidase/dehydrogenase; N6-dimethylallyladenine:acceptor oxidoreductase |
Systematic name: |
N6-prenyladenine:acceptor oxidoreductase |
Comments: |
A flavoprotein (FAD). Catalyses the oxidation of cytokinins, a family of N6-substituted adenine derivatives that are plant hormones, where the substituent is a prenyl group. Although this activity was previously thought to be catalysed by a hydrogen-peroxide-forming oxidase, this enzyme does not require oxygen for activity and does not form hydrogen peroxide. 2,6-Dichloroindophenol, methylene blue, nitroblue tetrazolium, phenazine methosulfate and copper(II) in the presence of imidazole can act as acceptors. This enzyme plays a part in regulating rice-grain production, with lower levels of the enzyme resulting in enhanced grain production [2]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 55326-39-1 |
References: |
1. |
Galuszka, P., Frebort, I., Sebela, M., Jacobsen, S. and Pec, P. Cytokinin oxidase or dehydrogenase? Mechanism of cytokinin degradation in plants. Eur. J. Biochem. 268 (2001) 450–461. [DOI] [PMID: 11168382] |
2. |
Ashikari, M., Sakakibara, H., Lin, S., Yamamoto, T., Takashi, T., Nishimura, A., Angeles, E.R., Qian, Q., Kitano, H. and Matsuoka, M. Cytokinin oxidase regulates rice grain production. Science 309 (2005) 741–745. [DOI] [PMID: 15976269] |
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[EC 1.5.99.12 created 2001] |
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EC |
1.18.1.4 |
Accepted name: |
rubredoxin—NAD(P)+ reductase |
Reaction: |
2 reduced rubredoxin + NAD(P)+ + H+ = 2 oxidized rubredoxin + NAD(P)H |
Glossary: |
benzyl viologen = 1,1′-dibenzyl-4,4′-bipyridinium
2,6-dichloroindophenol = 4-(2,6-dichloro-4-hydroxyphenylimino)cyclohexa-2,5-dien-1-one
menadione = 2-methyl-1,4-naphthoquinone
rubredoxin = iron-containing protein found in sulfur-metabolizing bacteria and archaea, participating in electron transfer |
Other name(s): |
rubredoxin-nicotinamide adenine dinucleotide (phosphate) reductase; rubredoxin-nicotinamide adenine; dinucleotide phosphate reductase; NAD(P)+-rubredoxin oxidoreductase; NAD(P)H-rubredoxin oxidoreductase |
Systematic name: |
rubredoxin:NAD(P)+ oxidoreductase |
Comments: |
The enzyme from Pyrococcus furiosus requires FAD. It reduces a number of electron carriers, including benzyl viologen, menadione and 2,6-dichloroindophenol, but rubredoxin is the most efficient. Ferredoxin is not utilized. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 80237-97-4 |
References: |
1. |
Petitdemange, H., Blusson, H. and Gay, R. Detection of NAD(P)H-rubredoxin oxidoreductases in Clostridia. Anal. Biochem. 116 (1981) 564–570. [DOI] [PMID: 6274224] |
2. |
Ma, K. and Adams, M.W.W. A hyperactive NAD(P)H:rubredoxin oxidoreductase from the hyperthermophilic archaeon Pyrococcus furiosus. J. Bacteriol. 181 (1999) 5530–5533. [PMID: 10464233] |
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[EC 1.18.1.4 created 1984, modified 2001, modified 2011] |
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