The Enzyme Database

Your query returned 11 entries.    printer_iconPrintable version



EC 1.3.99.2      
Transferred entry: butyryl-CoA dehydrogenase. Now EC 1.3.8.1, butyryl-CoA dehydrogenase.
[EC 1.3.99.2 created 1961 as EC 1.3.2.1, transferred 1964 to EC 1.3.99.2, deleted 2011]
 
 
EC 1.3.99.20      
Transferred entry: EC 1.3.99.20, 4-hydroxybenzoyl-CoA reductase. Now EC 1.3.7.9, 4-hydroxybenzoyl-CoA reductase.
[EC 1.3.99.20 created 2000, deleted 2011]
 
 
EC 1.3.99.21      
Transferred entry: (R)-benzylsuccinyl-CoA dehydrogenase. Now EC 1.3.8.3, (R)-benzylsuccinyl-CoA dehydrogenase
[EC 1.3.99.21 created 2003 as EC 1.3.99.21, deleted 2012]
 
 
EC 1.3.99.22      
Transferred entry: coproporphyrinogen dehydrogenase. Now EC 1.3.98.3, coproporphyrinogen dehydrogenase
[EC 1.3.99.22 created 2004, deleted 2016]
 
 
EC 1.3.99.23     
Accepted name: all-trans-retinol 13,14-reductase
Reaction: all-trans-13,14-dihydroretinol + acceptor = all-trans-retinol + reduced acceptor
For diagram of biosynthesis of retinal and derivatives, click here
Other name(s): retinol saturase; RetSat; (13,14)-all-trans-retinol saturase; all-trans-retinol:all-trans-13,14-dihydroretinol saturase
Systematic name: all-trans-13,14-dihydroretinol:acceptor 13,14-oxidoreductase
Comments: The reaction is only known to occur in the opposite direction to that given above, with the enzyme being specific for all-trans-retinol as substrate. Neither all-trans-retinoic acid nor 9-cis, 11-cis or 13-cis-retinol isomers are substrates. May play a role in the metabolism of vitamin A.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 879291-21-1
References:
1.  Moise, A.R., Kuksa, V., Imanishi, Y. and Palczewski, K. Identification of all-trans-retinol:all-trans-13,14-dihydroretinol saturase. J. Biol. Chem. 279 (2004) 50230–50242. [DOI] [PMID: 15358783]
[EC 1.3.99.23 created 2005]
 
 
EC 1.3.99.24     
Accepted name: 2-amino-4-deoxychorismate dehydrogenase
Reaction: (2S)-2-amino-4-deoxychorismate + FMN = 3-(1-carboxyvinyloxy)anthranilate + FMNH2
For diagram of enediyne antitumour antibiotic biosynthesis, click here
Glossary: (2S)-2-amino-4-deoxychorismate = (2S,3S)-3-(1-carboxyvinyloxy)-2,3-dihydroanthranilate
3-enolpyruvoylanthranilate = 3-(1-carboxyvinyloxy)anthranilate
Other name(s): ADIC dehydrogenase; 2-amino-2-deoxyisochorismate dehydrogenase; SgcG
Systematic name: (2S)-2-amino-4-deoxychorismate:FMN oxidoreductase
Comments: The sequential action of EC 2.6.1.86, 2-amino-4-deoxychorismate synthase and this enzyme leads to the formation of the benzoxazolinate moiety of the enediyne antitumour antibiotic C-1027 [1,2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Van Lanen, S.G., Lin, S. and Shen, B. Biosynthesis of the enediyne antitumor antibiotic C-1027 involves a new branching point in chorismate metabolism. Proc. Natl. Acad. Sci. USA 105 (2008) 494–499. [DOI] [PMID: 18182490]
2.  Yu, L., Mah, S., Otani, T. and Dedon, P. The benzoxazolinate of C-1027 confers intercalative DNA binding. J. Am. Chem. Soc. 117 (1995) 8877–8878.
[EC 1.3.99.24 created 2008]
 
 
EC 1.3.99.25     
Accepted name: carvone reductase
Reaction: (1) (+)-dihydrocarvone + acceptor = (–)-carvone + reduced acceptor
(2) (–)-isodihydrocarvone + acceptor = (+)-carvone + reduced acceptor
For diagram of (–)-carvone catabolism, click here
Glossary: (+)-dihydrocarvone = (1S,4R)-menth-8-en-2-one
(+)-isodihydrocarvone = (1S,4R)-menth-8-en-2-one
(–)-carvone = (4R)-mentha-1(6),8-dien-6-one = (5R)-2-methyl-5-(prop-1-en-2-yl)cyclohex-2-en-1-one
Systematic name: (+)-dihydrocarvone:acceptor 1,6-oxidoreductase
Comments: This enzyme participates in the carveol and dihydrocarveol degradation pathway of the Gram-positive bacterium Rhodococcus erythropolis DCL14. The enzyme has not been purified, and requires an unknown cofactor, which is different from NAD+, NADP+ or a flavin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  van der Werf, M.J. and Boot, A.M. Metabolism of carveol and dihydrocarveol in Rhodococcus erythropolis DCL14. Microbiology 146 (2000) 1129–1141. [DOI] [PMID: 10832640]
[EC 1.3.99.25 created 2008]
 
 
EC 1.3.99.26     
Accepted name: all-trans-ζ-carotene desaturase
Reaction: all-trans-ζ-carotene + 2 acceptor = all-trans-lycopene + 2 reduced acceptor (overall reaction)
(1a) all-trans-ζ-carotene + acceptor = all-trans-neurosporene + reduced acceptor
(1b) all-trans-neurosporene + acceptor = all-trans-lycopene + reduced acceptor
For diagram of carotenoid biosynthesis, click here
Other name(s): Crtlb; phytoene desaturase (ambiguous); 2-step phytoene desaturase (ambiguous); two-step phytoene desaturase (ambiguous); CrtI (ambiguous)
Systematic name: all-trans-ζ-carotene:acceptor oxidoreductase
Comments: This enzyme is involved in carotenoid biosynthesis.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Iniesta, A.A., Cervantes, M. and Murillo, F.J. Cooperation of two carotene desaturases in the production of lycopene in Myxococcus xanthus. FEBS J. 274 (2007) 4306–4314. [DOI] [PMID: 17662111]
[EC 1.3.99.26 created 2011]
 
 
EC 1.3.99.27     
Accepted name: 1-hydroxycarotenoid 3,4-desaturase
Reaction: 1-hydroxy-1,2-dihydrolycopene + acceptor = 1-hydroxy-3,4-didehydro-1,2-dihydrolycopene + reduced acceptor
Other name(s): CrtD; hydroxyneurosporene desaturase; carotenoid 3,4-dehydrogenase; 1-hydroxy-carotenoid 3,4-dehydrogenase
Systematic name: 1-hydroxy-1,2-dihydrolycopene:acceptor oxidoreductase
Comments: The enzymes from Rubrivivax gelatinosus and Rhodobacter sphaeroides prefer the acyclic carotenoids (e.g. 1-hydroxy-1,2-dihydroneurosporene, 1-hydroxy-1,2-dihydrolycopene) as substrates. The conversion rate for the 3,4-desaturation of the monocyclic 1′-hydroxy-1′,2′-dihydro-γ-carotene is lower [2,3]. The enzyme from the marine bacterium strain P99-3 shows high activity with the monocyclic carotenoid 1′-hydroxy-1′,2′-dihydro-γ-carotene [1]. The enzyme from Rhodobacter sphaeroides utilizes molecular oxygen as the electron acceptor in vitro [3]. However, oxygen is unlikely to be the natural electron acceptor under anaerobic conditions.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Teramoto, M., Rahlert, N., Misawa, N. and Sandmann, G. 1-Hydroxy monocyclic carotenoid 3,4-dehydrogenase from a marine bacterium that produces myxol. FEBS Lett. 570 (2004) 184–188. [DOI] [PMID: 15251462]
2.  Steiger, S., Astier, C. and Sandmann, G. Substrate specificity of the expressed carotenoid 3,4-desaturase from Rubrivivax gelatinosus reveals the detailed reaction sequence to spheroidene and spirilloxanthin. Biochem. J. 349 (2000) 635–640. [PMID: 10880364]
3.  Albrecht, M., Ruther, A. and Sandmann, G. Purification and biochemical characterization of a hydroxyneurosporene desaturase involved in the biosynthetic pathway of the carotenoid spheroidene in Rhodobacter sphaeroides. J. Bacteriol. 179 (1997) 7462–7467. [DOI] [PMID: 9393712]
[EC 1.3.99.27 created 2011]
 
 
EC 1.3.99.28     
Accepted name: phytoene desaturase (neurosporene-forming)
Reaction: 15-cis-phytoene + 3 acceptor = all-trans-neurosporene + 3 reduced acceptor (overall reaction)
(1a) 15-cis-phytoene + acceptor = all-trans-phytofluene + reduced acceptor
(1b) all-trans-phytofluene + acceptor = all-trans-ζ-carotene + reduced acceptor
(1c) all-trans-ζ-carotene + acceptor = all-trans-neurosporene + reduced acceptor
For diagram of carotenoid biosynthesis, click here
Other name(s): 3-step phytoene desaturase; three-step phytoene desaturase; phytoene desaturase (ambiguous); CrtI (ambiguous)
Systematic name: 15-cis-phytoene:acceptor oxidoreductase (neurosporene-forming)
Comments: This enzyme is involved in carotenoid biosynthesis and catalyses up to three desaturation steps (cf. EC 1.3.99.29 [phytoene desaturase (ζ-carotene-forming)], EC 1.3.99.30 [phytoene desaturase (3,4-didehydrolycopene-forming)], EC 1.3.99.31 [phytoene desaturase (lycopene-forming)]). The enzyme is activated by FAD. NAD+, NADP+ or ATP show no activating effect [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Raisig, A., Bartley, G., Scolnik, P. and Sandmann, G. Purification in an active state and properties of the 3-step phytoene desaturase from Rhodobacter capsulatus overexpressed in Escherichia coli. J. Biochem. 119 (1996) 559–564. [PMID: 8830054]
2.  Wang, C.W. and Liao, J.C. Alteration of product specificity of Rhodobacter sphaeroides phytoene desaturase by directed evolution. J. Biol. Chem. 276 (2001) 41161–41164. [DOI] [PMID: 11526111]
[EC 1.3.99.28 created 2011]
 
 
EC 1.3.99.29     
Accepted name: phytoene desaturase (ζ-carotene-forming)
Reaction: 15-cis-phytoene + 2 acceptor = all-trans-ζ-carotene + 2 reduced acceptor (overall reaction)
(1a) 15-cis-phytoene + acceptor = all-trans-phytofluene + reduced acceptor
(1b) all-trans-phytofluene + acceptor = all-trans-ζ-carotene + reduced acceptor
For diagram of carotenoid biosynthesis, click here
Other name(s): CrtIa; 2-step phytoene desaturase (ambiguous); two-step phytoene desaturase (ambiguous)
Systematic name: 15-cis-phytoene:acceptor oxidoreductase (ζ-carotene-forming)
Comments: The enzyme is involved in carotenoid biosynthesis and catalyses up to two desaturation steps (cf. EC 1.3.99.28 [phytoene desaturase (neurosporene-forming)], EC 1.3.99.30 [phytoene desaturase (3,4-didehydrolycopene-forming)] and EC 1.3.99.31 [phytoene desaturase (lycopene-forming)]).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Iniesta, A.A., Cervantes, M. and Murillo, F.J. Cooperation of two carotene desaturases in the production of lycopene in Myxococcus xanthus. FEBS J. 274 (2007) 4306–4314. [DOI] [PMID: 17662111]
[EC 1.3.99.29 created 2011]
 
 


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