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.
Publication Abstract from PubMed
ZhuH is a priming ketosynthase that initiates the elongation of the polyketide chain in the biosynthetic pathway of a type II polyketide, R1128. The crystal structure of ZhuH in complex with the priming substrate acetyl-CoA reveals an extensive loop region at the dimer interface that appears to affect the selectivity for the primer unit. Acetyl-CoA is bound in a 20 A-long channel, which placed the acetyl group against the catalytic triad. Analysis of the primer unit binding site in ZhuH suggests that it can accommodate acyl chains that are two to four carbons long. Selectivity and primer unit size appear to involve the side chains of three residues on the loops close to the dimer interface that constitute the bottom of the substrate binding pocket.
Crystal structure of the priming beta-ketosynthase from the R1128 polyketide biosynthetic pathway.,Pan H, Tsai S, Meadows ES, Miercke LJ, Keatinge-Clay AT, O'Connell J, Khosla C, Stroud RM Structure. 2002 Nov;10(11):1559-68. PMID:12429097[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
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
- ↑ Pan H, Tsai S, Meadows ES, Miercke LJ, Keatinge-Clay AT, O'Connell J, Khosla C, Stroud RM. Crystal structure of the priming beta-ketosynthase from the R1128 polyketide biosynthetic pathway. Structure. 2002 Nov;10(11):1559-68. PMID:12429097
