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ENZYME entry: EC 2.3.1.300
Accepted Name |
branched-chain beta-ketoacyl-[acyl-carrier-protein] synthase.
|
Reaction catalysed |
- 3-methylbutanoyl-CoA + H(+) + malonyl-[ACP] <=> 5-methyl-3-oxohexanoyl-[ACP] + CO2 + CoA
- 2-methylpropanoyl-CoA + H(+) + malonyl-[ACP] <=> 4-methyl-3-oxopentanoyl-[ACP] + CO2 + CoA
- (2S)-2-methylbutanoyl-CoA + H(+) + malonyl-[ACP] <=> (4S)-4-methyl-3-oxohexanoyl-[ACP] + CO2 + CoA
|
Comment(s) |
- The enzyme is responsible for initiating branched-chain fatty acid
biosynthesis by the dissociated (or type II) fatty-acid biosynthesis
system (FAS-II) in some bacteria, using molecules derived from
degradation of the branched-chain amino acids L-leucine, L-valine,
and L-isoleucine to form the starting molecules for elongation by the
FAS-II system.
- In some organisms the enzyme is also able to use acetyl-CoA, leading
to production of a mix of branched-chain and straight-chain fatty
acids (cf. EC 2.3.1.180).
|
Cross-references |
BRENDA | 2.3.1.300 |
EC2PDB | 2.3.1.300 |
ExplorEnz | 2.3.1.300 |
PRIAM enzyme-specific profiles | 2.3.1.300 |
KEGG Ligand Database for Enzyme Nomenclature | 2.3.1.300 |
IUBMB Enzyme Nomenclature | 2.3.1.300 |
IntEnz | 2.3.1.300 |
MEDLINE | Find literature relating to 2.3.1.300 |
MetaCyc | 2.3.1.300 |
Rhea expert-curated reactions | 2.3.1.300 |
UniProtKB/Swiss-Prot |
|
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ENZYME /
UniProtKB/Swiss-Prot entries corresponding to 2.3.1.-
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