The Enzyme Database

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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 1.14.15.9     
Accepted name: spheroidene monooxygenase
Reaction: (1) spheroidene + 4 reduced ferredoxin [iron-sulfur] cluster + 2 O2 + 4 H+ = spheroiden-2-one + 4 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O (overall reaction)
(1a) spheroidene + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+ = 2-hydroxyspheroidene + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
(1b) 2-hydroxyspheroidene + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+ = 2,2-dihydroxyspheroidene + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
(1c) 2,2-dihydroxyspheroidene = spheroiden-2-one + H2O (spontaneous)
(2) spirilloxanthin + 4 reduced ferredoxin [iron-sulfur] cluster + 2 O2 + 4 H+ = 2-oxospirilloxanthin + 4 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O (overall reaction)
(2a) spirilloxanthin + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+ = 2-hydroxyspirilloxanthin + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
(2b) 2-hydroxyspirilloxanthin + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+ = 2,2-dihydroxyspirilloxanthin + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
(2c) 2,2-dihydroxyspirilloxanthin = 2-oxospirilloxanthin + H2O (spontaneous)
(3) 2-oxospirilloxanthin + 4 reduced ferredoxin [iron-sulfur] cluster + 2 O2 + 4 H+ = 2,2′-dioxospirilloxanthin + 4 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O (overall reaction)
(3a) 2-oxospirilloxanthin + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+ = 2′-hydroxy-2-oxospirilloxanthin + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
(3b) 2′-hydroxy-2-oxospirilloxanthin + reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+ = 2′,2′-dihydroxy-2-oxospirilloxanthin + oxidized ferredoxin [iron-sulfur] cluster + H2O
(3c) 2′,2′-dihydroxy-2-oxospirilloxanthin = 2,2′-dioxospirilloxanthin + H2O (spontaneous)
For diagram of 2,2′-dioxospirilloxanthin biosynthesis, click here and for diagram of 4.2.1.131, click here
Glossary: spheroidene = 3,4-didehydro-1-methoxy-1,2,7′,8′-tetrahydro-ψ,ψ-carotene
Other name(s): CrtA; acyclic carotenoid 2-ketolase; spirilloxanthin monooxygenase; 2-oxo-spirilloxanthin monooxygenase
Systematic name: spheroidene,reduced-ferredoxin:oxygen oxidoreductase (spheroiden-2-one-forming)
Comments: The enzyme is involved in spheroidenone biosynthesis and in 2,2′-dioxospirilloxanthin biosynthesis. The enzyme from Rhodobacter sphaeroides contains heme at its active site [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Lee, P.C., Holtzapple, E. and Schmidt-Dannert, C. Novel activity of Rhodobacter sphaeroides spheroidene monooxygenase CrtA expressed in Escherichia coli. Appl. Environ. Microbiol. 76 (2010) 7328–7331. [DOI] [PMID: 20851979]
2.  Gerjets, T., Steiger, S. and Sandmann, G. Catalytic properties of the expressed acyclic carotenoid 2-ketolases from Rhodobacter capsulatus and Rubrivivax gelatinosus. Biochim. Biophys. Acta 1791 (2009) 125–131. [DOI] [PMID: 19136077]
[EC 1.14.15.9 created 2012, modified 2016]
 
 
EC 2.1.1.210     
Accepted name: demethylspheroidene O-methyltransferase
Reaction: S-adenosyl-L-methionine + demethylspheroidene = S-adenosyl-L-homocysteine + spheroidene
For diagram of 4.2.1.131, click here and for diagram of mechanism, click here
Other name(s): 1-hydroxycarotenoid O-methylase; 1-hydroxycarotenoid methylase; 1-HO-carotenoid methylase; CrtF
Systematic name: S-adenosyl-L-methionine:demethylspheroidene O-methyltransferase
Comments: In Rhodopseudomonas capsulata and Rubrivivax gelatinosus the enzyme is involved in biosynthesis of spheroidene [1,2,3]. In Rubrivivax gelatinosus the enzyme also catalyses the methylation of demethylspirilloxanthin to spirilloxanthin and the methylation of 3,4-didehydrorhodopin to anhydrorhodovibrin [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Badenhop, F., Steiger, S., Sandmann, M. and Sandmann, G. Expression and biochemical characterization of the 1-HO-carotenoid methylase CrtF from Rhodobacter capsulatus. FEMS Microbiol. Lett. 222 (2003) 237–242. [DOI] [PMID: 12770713]
2.  Pinta, V., Ouchane, S., Picaud, M., Takaichi, S., Astier, C. and Reiss-Husson, F. Characterization of unusual hydroxy- and ketocarotenoids in Rubrivivax gelatinosus: involvement of enzyme CrtF or CrtA. Arch. Microbiol. 179 (2003) 354–362. [DOI] [PMID: 12664193]
3.  Scolnik, P.A., Walker, M.A. and Marrs, B.L. Biosynthesis of carotenoids derived from neurosporene in Rhodopseudomonas capsulata. J. Biol. Chem. 255 (1980) 2427–2432. [PMID: 7358679]
[EC 2.1.1.210 created 2011]
 
 


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