4jrh: Difference between revisions
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/FABF_VIBCH FABF_VIBCH]] Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Has a preference for short chain acid substrates and may function to supply the octanoic substrates for lipoic acid biosynthesis (By similarity). | [[http://www.uniprot.org/uniprot/FABF_VIBCH FABF_VIBCH]] Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Has a preference for short chain acid substrates and may function to supply the octanoic substrates for lipoic acid biosynthesis (By similarity). | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> |
Revision as of 12:14, 15 November 2017
Crystal structure of beta-ketoacyl-ACP synthase II (FabF) from Vibrio Cholerae (space group P43) at 2.2 AngstromCrystal structure of beta-ketoacyl-ACP synthase II (FabF) from Vibrio Cholerae (space group P43) at 2.2 Angstrom
Structural highlights
Function[FABF_VIBCH] Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Has a preference for short chain acid substrates and may function to supply the octanoic substrates for lipoic acid biosynthesis (By similarity). |
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