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ENZYME

ENZYME entry: EC 2.3.1.293

Accepted Name
meromycolic acid 3-oxoacyl-(acyl carrier protein) synthase I
Alternative Name(s)
beta-ketoacyl-acyl carrier protein synthase KasA
Reaction catalysed
an ultra-long-chain mono-unsaturated fatty acyl-[ACP] + H(+) + malonyl-[ACP] <=> a 3-oxo-ultra-long-chain mono-unsaturated fatty acyl-[ACP] + CO2 + holo-[ACP]
Comment(s)
  • The enzyme is part of the fatty acid synthase (FAS) II system of mycobacteria, which extends modified products of the FAS I system, eventually forming meromycolic acids that are incorporated into mycolic acids.
  • Meromycolic acids consist of a long chain, typically 50-60 carbons, which is functionalized by different groups.Two 3-oxoacyl-(acyl carrier protein) synthases function within the FAS II system, encoded by the kasA and kasB genes.
  • The two enzymes share some sequence identity but function independently on separate sets of substrates.
  • KasA differs from KasB (EC 2.3.1.294), by preferring shorter (C-22 to C-36) and more saturated (only one double bond) substrates.
Cross-references
BRENDA2.3.1.293
EC2PDB2.3.1.293
ExplorEnz2.3.1.293
PRIAM enzyme-specific profiles2.3.1.293
KEGG Ligand Database for Enzyme Nomenclature2.3.1.293
IUBMB Enzyme Nomenclature2.3.1.293
IntEnz2.3.1.293
MEDLINEFind literature relating to 2.3.1.293
MetaCyc2.3.1.293
Rhea expert-curated reactions2.3.1.293
UniProtKB/Swiss-Prot
P63455, KASA_MYCBOQ9CBS7, KASA_MYCLEH8ESN0, KASA_MYCTE
P9WQD8, KASA_MYCTOP9WQD9, KASA_MYCTU

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All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.3.1.-
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