The Enzyme Database

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EC 1.1.99.1     
Accepted name: choline dehydrogenase
Reaction: choline + acceptor = betaine aldehyde + reduced acceptor
Glossary: betaine aldehyde = N,N,N-trimethyl-2-oxoethylammonium
choline = (2-hydroxyethyl)trimethylammonium
Other name(s): choline oxidase; choline-cytochrome c reductase; choline:(acceptor) oxidoreductase; choline:(acceptor) 1-oxidoreductase
Systematic name: choline:acceptor 1-oxidoreductase
Comments: A quinoprotein. In many bacteria, plants and animals, the osmoprotectant betaine is synthesized using different enzymes to catalyse the conversion of (1) choline into betaine aldehyde and (2) betaine aldehyde into betaine. In plants, the first reaction is catalysed by EC 1.14.15.7, choline monooxygenase, whereas in animals and many bacteria, it is catalysed by either membrane-bound choline dehydrogenase (EC 1.1.99.1) or soluble choline oxidase (EC 1.1.3.17) [4]. The enzyme involved in the second step, EC 1.2.1.8, betaine-aldehyde dehydrogenase, appears to be the same in plants, animals and bacteria.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9028-67-5
References:
1.  Ameyama, M., Shinagawa, E., Matsuchita, K., Takimoto, K., Nakashima, K. and Adachi, O. Mammalian choline dehydrogenase is a quinoprotein. Agric. Biol. Chem. 49 (1985) 3623–3626.
2.  Ebisuzaki, K. and Williams, J.N. Preparation and partial purification of soluble choline dehydrogenase from liver mitochondria. Biochem. J. 60 (1955) 644–646. [PMID: 13249959]
3.  Gadda, G. and McAllister-Wilkins, E.E. Cloning, expression, and purification of choline dehydrogenase from the moderate halophile Halomonas elongata. Appl. Environ. Microbiol. 69 (2003) 2126–2132. [DOI] [PMID: 12676692]
4.  Waditee, R., Tanaka, Y., Aoki, K., Hibino, T., Jikuya, H., Takano, J., Takabe, T. and Takabe, T. Isolation and functional characterization of N-methyltransferases that catalyze betaine synthesis from glycine in a halotolerant photosynthetic organism Aphanothece halophytica. J. Biol. Chem. 278 (2003) 4932–4942. [DOI] [PMID: 12466265]
[EC 1.1.99.1 created 1961, modified 1989, modified 2005]
 
 
EC 1.1.99.10      
Transferred entry: glucose dehydrogenase (acceptor). Now EC 1.1.5.9, glucose 1-dehydrogenase (FAD, quinone)
[EC 1.1.99.10 created 1972, modified 1976, deleted 2013]
 
 
EC 1.1.99.11     
Accepted name: fructose 5-dehydrogenase
Reaction: D-fructose + acceptor = 5-dehydro-D-fructose + reduced acceptor
Other name(s): fructose 5-dehydrogenase (acceptor); D-fructose dehydrogenase; D-fructose:(acceptor) 5-oxidoreductase
Systematic name: D-fructose:acceptor 5-oxidoreductase
Comments: 2,6-Dichloroindophenol can act as acceptor.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37250-85-4
References:
1.  Ameyama, M. and Adachi, O. D-Fructose dehydrogenase from Gluconobacter industrius, membrane-bound. Methods Enzymol. 89 (1982) 154–159.
2.  Yamada, Y., Aida, K. and Uemura, T. Enzymatic studies on the oxidation of sugar and sugar alcohol. I. Purification and properties of particle-bound fructose dehydrogenase. J. Biochem. (Tokyo) 61 (1967) 636–646. [PMID: 6059959]
[EC 1.1.99.11 created 1972]
 
 
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]
[EC 1.1.99.12 created 1972]
 
 
EC 1.1.99.13     
Accepted name: glucoside 3-dehydrogenase
Reaction: sucrose + acceptor = 3-dehydro-α-D-glucosyl-β-D-fructofuranoside + reduced acceptor
Other name(s): D-glucoside 3-dehydrogenase; D-aldohexopyranoside dehydrogenase; D-aldohexoside:cytochrome c oxidoreductase; D-glucoside 3-dehydrogenase; hexopyranoside-cytochrome c oxidoreductase; D-aldohexoside:(acceptor) 3-oxidoreductase
Systematic name: D-aldohexoside:acceptor 3-oxidoreductase
Comments: A flavoprotein (FAD). The enzyme acts on D-glucose, D-galactose, D-glucosides and D-galactosides, but D-glucosides react more rapidly than D-galactosides.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 9031-74-7
References:
1.  Hayano, K. and Fukui, S. Purification and properties of 3-ketosucrose-forming enzyme from the cells of Agrobacterium tumefaciens. J. Biol. Chem. 242 (1967) 3665–3672. [PMID: 6038493]
[EC 1.1.99.13 created 1972]
 
 
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]
[EC 1.1.99.14 created 1978]
 
 
EC 1.1.99.15      
Transferred entry: 5,10-methylenetetrahydrofolate reductase (FADH2). Now EC 1.5.1.20, methylenetetrahydrofolate reductase [NAD(P)H]
[EC 1.1.99.15 created 1978, deleted 1980]
 
 
EC 1.1.99.16      
Transferred entry: malate dehydrogenase (acceptor). As the acceptor is now known, the enzyme has been transferred to EC 1.1.5.4, malate dehydrogenase (quinone).
[EC 1.1.99.16 created 1978, deleted 2009]
 
 
EC 1.1.99.17      
Transferred entry: glucose dehydrogenase (pyrroloquinoline-quinone). Now EC 1.1.5.2, quinoprotein glucose dehydrogenase
[EC 1.1.99.17 created 1982, deleted 2003]
 
 
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)]
 
 
EC 1.1.99.19      
Transferred entry: uracil dehydrogenase. Now EC 1.17.99.4, uracil/thymine dehydrogenase
[EC 1.1.99.19 created 1961 as EC 1.2.99.1, transferred 1984 to EC 1.1.99.19, deleted 2006]
 
 


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