Structural highlights
Function
FABH_STRLI Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Has some substrate preference for butyryl-CoA and can tolerate branched substrates. Can also prime acyl-CoA. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids. Involved in the biosynthesis of R1128 polyketide.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
See Also
References
- ↑ Meadows ES, Khosla C. In vitro reconstitution and analysis of the chain initiating enzymes of the R1128 polyketide synthase. Biochemistry. 2001 Dec 11;40(49):14855-61. PMID:11732905
