The Enzyme Database

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EC 1.3.99.37     
Accepted name: 1-hydroxy-2-isopentenylcarotenoid 3,4-desaturase
Reaction: (1) dihydroisopentenyldehydrorhodopin + acceptor = isopentenyldehydrorhodopin + reduced acceptor
(2) dihydrobisanhydrobacterioruberin + acceptor = bisanhydrobacterioruberin + reduced acceptor
For diagram of bacterioruberin biosynthesis, click here
Glossary: bisanhydrobacterioruberin = (2S,2S′)-2,2′-bis(3-methylbut-2-en-1-yl)-3,4-didehydro-1,1′,2,2′-tetrahydro-ψ,ψ-carotene-1,1′-diol
dihydrobisanhydrobacterioruberin = (2S,2S′)-2,2′-bis(3-methylbut-2-en-1-yl)-3,3′,4,4′-tetradehydro-1,1′,2,2′-tetrahydro-ψ,ψ-carotene-1,1′-diol
dihydroisopentenyldehydrorhodopin = (2S)-2-(3-methylbut-2-en-1-yl)-3,4-didehydro-1,2-dihydro-ψ,ψ-caroten-1-ol
isopentenyldehydrorhodopin = (2S)-2-(3-methylbut-2-en-1-yl)-1,2-dihydro-ψ,ψ-caroten-1-ol
Other name(s): crtD (gene name)
Systematic name: dihydroisopentenyldehydrorhodopin:acceptor 3,4-oxidoreductase
Comments: The enzyme, isolated from the archaeon Haloarcula japonica, is involved in the biosynthesis of the C50 carotenoid bacterioruberin. In this pathway it catalyses the desaturation of the C-3,4 double bond in dihydroisopentenyldehydrorhodopin and the desaturation of the C-3′,4′ double bond in dihydrobisanhydrobacterioruberin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Yang, Y., Yatsunami, R., Ando, A., Miyoko, N., Fukui, T., Takaichi, S. and Nakamura, S. Complete biosynthetic pathway of the C50 carotenoid bacterioruberin from lycopene in the extremely halophilic archaeon Haloarcula japonica. J. Bacteriol. 197 (2015) 1614–1623. [DOI] [PMID: 25712483]
[EC 1.3.99.37 created 2015]
 
 
EC 2.5.1.149     
Accepted name: lycopene elongase/hydratase (flavuxanthin-forming)
Reaction: (1) dimethylallyl diphosphate + all-trans-lycopene + acceptor + H2O = nonaflavuxanthin + reduced electron acceptor + diphosphate
(2) dimethylallyl diphosphate + nonaflavuxanthin + acceptor + H2O = flavuxanthin + reduced electron acceptor + diphosphate
Glossary: flavuxanthin = 2,2′-bis-(4-hydroxy-3-methylbut-2-enyl)-1,16,1′,16′-tetradehydro-1,2,1′,2′-tetrahydro-ψ,ψ-carotene = (2E,8E,10E,12E,14E,16E,18E,20E,22E,24E,26E,28E,34E)-5,32-diisopropenyl-2,8,12,16,21,25,29,35-octamethylhexatriaconta-2,8,10,12,14,16,18,20,22,24,26,28,34-tridecaene-1,36-diol
Other name(s): crtEb (gene name)
Systematic name: dimethylallyl-diphosphate:all-trans-lycopene dimethylallyltransferase (hydrating, flavuxanthin-forming)
Comments: The enzyme, characterized from the bacterium Corynebacterium glutamicum, is bifunctional. It catalyses the elongation of the C40 carotenoid all-trans-lycopene by attaching an isoprene unit at C-2, as well as the hydroxylation of the new isoprene unit. The enzyme acts at both ends of the substrate, forming the C50 carotenoid flavuxanthin via the C45 intermediate nonaflavuxanthin. cf. EC 2.5.1.150, lycopene elongase/hydratase (dihydrobisanhydrobacterioruberin-forming).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Krubasik, P., Kobayashi, M. and Sandmann, G. Expression and functional analysis of a gene cluster involved in the synthesis of decaprenoxanthin reveals the mechanisms for C50 carotenoid formation. Eur. J. Biochem. 268 (2001) 3702–3708. [PMID: 11432736]
2.  Heider, S.A., Peters-Wendisch, P. and Wendisch, V.F. Carotenoid biosynthesis and overproduction in Corynebacterium glutamicum. BMC Microbiol. 12:198 (2012). [PMID: 22963379]
[EC 2.5.1.149 created 2018]
 
 
EC 2.5.1.150     
Accepted name: lycopene elongase/hydratase (dihydrobisanhydrobacterioruberin-forming)
Reaction: (1) dimethylallyl diphosphate + all-trans-lycopene + H2O = dihydroisopentenyldehydrorhodopin + diphosphate
(2) dimethylallyl diphosphate + isopentenyldehydrorhodopin + H2O = dihydrobisanhydrobacterioruberin + diphosphate
Glossary: dihydrobisanhydrobacterioruberin = (2S,2S′)-2,2′-bis(3-methylbut-2-en-1-yl)-3,3′,4,4′-tetradehydro-1,1′,2,2′-tetrahydro-ψ,ψ-carotene-1,1′-diol = (3S,4E,6E,8E,10E,12E,14E,16E,18E,20E,22E,24E,26E,30R)-2,6,10,14,19,23,27,31-octamethyl-3,30-bis(3-methylbut-2-en-1-yl)dotriaconta-4,6,8,10,12,14,16,18,20,22,24,26-dodecaene-2,31-diol
Other name(s): lbtA (gene name); lyeJ (gene name)
Systematic name: dimethylallyl-diphosphate:all-trans-lycopene dimethylallyltransferase (hydrating, dihydrobisanhydrobacterioruberin-forming)
Comments: The enzyme, characterized from the bacterium Dietzia sp. CQ4 and the halophilic archaea Halobacterium salinarum and Haloarcula japonica, is bifunctional. It catalyses the elongation of the C40 carotenoid all-trans-lycopene by attaching an isoprene unit at C-2 as well as the hydroxylation of the previous end of the molecule. The enzyme acts at both ends of the substrate, and combined with the action of EC 1.3.99.37, 1-hydroxy-2-isopentenylcarotenoid 3,4-desaturase, it forms the C50 carotenoid dihydrobisanhydrobacterioruberin. cf. EC 2.5.1.149, lycopene elongase/hydratase (flavuxanthin-forming).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Tao, L., Yao, H. and Cheng, Q. Genes from a Dietzia sp. for synthesis of C40 and C50 β-cyclic carotenoids. Gene 386 (2007) 90–97. [PMID: 17008032]
2.  Dummer, A.M., Bonsall, J.C., Cihla, J.B., Lawry, S.M., Johnson, G.C. and Peck, R.F. Bacterioopsin-mediated regulation of bacterioruberin biosynthesis in Halobacterium salinarum. J. Bacteriol. 193 (2011) 5658–5667. [PMID: 21840984]
3.  Yang, Y., Yatsunami, R., Ando, A., Miyoko, N., Fukui, T., Takaichi, S. and Nakamura, S. Complete biosynthetic pathway of the C50 carotenoid bacterioruberin from lycopene in the extremely halophilic archaeon Haloarcula japonica. J. Bacteriol. 197 (2015) 1614–1623. [DOI] [PMID: 25712483]
[EC 2.5.1.150 created 2018]
 
 


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