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ENZYME entry: EC 2.3.1.179

Accepted Name
Beta-ketoacyl-[acyl-carrier-protein] synthase II.
Alternative Name(s)
3-oxoacyl-acyl carrier protein synthase I.
Beta-ketoacyl-ACP synthase II.
KAS II.
KASII.
Reaction catalysed
A (Z)-hexadec-9-enoyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein] <=> a (Z)-3-oxooctadec-11-enoyl-[acyl-carrier protein] + CO(2) + an [acyl-carrier protein]
Comment(s)
  • Involved in the dissociated (or type II) fatty acid biosynthesis system that occurs in plants and bacteria.
  • While the substrate specificity of this enzyme is very similar to that of EC 2.3.1.41, it differs in that palmitoleoyl-ACP is not a good substrate of EC 2.3.1.41 but is an excellent substrate of this enzyme.
  • The fatty-acid composition of Escherichia coli changes as a function of growth temperature, with the proportion of unsaturated fatty acids increasing with lower growth temperature.
  • Controls the temperature-dependent regulation of fatty-acid composition, with mutants lacking this acivity being deficient in the elongation of palmitoleate to cis-vaccenate at low temperatures.
Cross-references
PROSITEPDOC00529
BRENDA2.3.1.179
EC2PDB2.3.1.179
ExplorEnz2.3.1.179
PRIAM enzyme-specific profiles2.3.1.179
KEGG Ligand Database for Enzyme Nomenclature2.3.1.179
IUBMB Enzyme Nomenclature2.3.1.179
IntEnz2.3.1.179
MEDLINEFind literature relating to 2.3.1.179
MetaCyc2.3.1.179
Rhea expert-curated reactions2.3.1.179
UniProtKB/Swiss-Prot
O34340, FABF_BACSU;  Q83E37, FABF_COXBU;  P0AAI7, FABF_ECO57;  
P0AAI6, FABF_ECOL6;  P0AAI5, FABF_ECOLI;  P56902, FABF_RHIME;  
P0AAI8, FABF_SHIFL;  Q5HHA1, FABF_STAAC;  Q99VA6, FABF_STAAM;  
Q7A6F8, FABF_STAAN;  Q6GIA3, FABF_STAAR;  Q6GAU2, FABF_STAAS;  
Q5TKS0, FABF_STAAU;  Q8NXE1, FABF_STAAW;  P73283, FABF_SYNY3;  
Q9KQH9, FABF_VIBCH;  P55338, FABF_VIBHA;  

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