4wzu
From Proteopedia
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/FABH2_VIBCH FABH2_VIBCH]] 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. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids.[HAMAP-Rule:MF_01815] | [[http://www.uniprot.org/uniprot/FABH2_VIBCH FABH2_VIBCH]] 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. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids.[HAMAP-Rule:MF_01815] | ||
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| + | ==See Also== | ||
| + | *[[Acyl carrier protein synthase|Acyl carrier protein synthase]] | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 06:59, 3 June 2015
Crystal structure of beta-ketoacyl-(acyl carrier protein) synthase III-2 (FabH2) from Vibrio cholerae
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Categories: Anderson, W F | Structural genomic | Chordia, M D | Chruszcz, M | Cooper, D R | Hou, J | Minor, W | Zheng, H | Zimmerman, M D | Csgid | Fabh | Transferase
