| Entry |
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| Name |
very-long-chain-(3R)-3-hydroxyacyl-[acyl-carrier protein]:NADP+ oxidoreductase
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| Definition |
Very-long-chain (3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+ <=> Very-long-chain 3-oxoacyl-[acyl-carrier protein] + NADPH + H+
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| Equation |
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| Comment |
general reaction
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| Enzyme |
1.1.1.-
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| Brite |
Enzymatic reactions [BR:br08201]
1. Oxidoreductase reactions
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.-
R13263 Very-long-chain (3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+ <=> Very-long-chain 3-oxoacyl-[acyl-carrier protein] + NADPH + H+
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| Orthology |
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| Reference |
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| Authors |
Cohen-Gonsaud M, Ducasse S, Hoh F, Zerbib D, Labesse G, Quemard A. |
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| Title |
Crystal structure of MabA from Mycobacterium tuberculosis, a reductase involved in long-chain fatty acid biosynthesis. |
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| Journal |
J Mol Biol 320:249-61 (2002) |
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| Reference |
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| Authors |
Marrakchi H, Ducasse S, Labesse G, Montrozier H, Margeat E, Emorine L, Charpentier X, Daffe M, Quemard AK. |
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| Title |
MabA (FabG1), a Mycobacterium tuberculosis protein involved in the long-chain fatty acid elongation system FAS-II. |
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| Journal |
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| Reference |
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| Authors |
Veyron-Churlet R, Zanella-Cleon I, Cohen-Gonsaud M, Molle V, Kremer L. |
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| Title |
Phosphorylation of the Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein reductase MabA regulates mycolic acid biosynthesis. |
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| Journal |
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| Reference |
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| Authors |
Silva RG, de Carvalho LP, Blanchard JS, Santos DS, Basso LA. |
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| Title |
Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein (ACP) reductase: kinetic and chemical mechanisms. |
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| Journal |
Biochemistry 45:13064-73 (2006) |
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| LinkDB |
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