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- W2046507502 abstract "Crystal structure data for Escherichia coli β-ketoacyl synthase (KAS) I with C10 and C12 fatty acid substrates bound in conjunction with results from mutagenizing residues in the active site leads to a model for catalysis. Differences from and similarities to the other Claisen enzymes carrying out decarboxylations reveal two catalytic mechanisms, one for KAS I and KAS II, the other for KAS III and chalcone synthase. A comparison of the structures of KAS I and KAS II does not reveal the basis of chain-length specificity. The structures of the Arabidopsis thaliana KAS family are compared." @default.
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- W2046507502 date "2000-12-01" @default.
- W2046507502 modified "2023-10-18" @default.
- W2046507502 title "Molecular aspects of <i>β</i>-ketoacyl synthase (KAS) catalysis" @default.
- W2046507502 doi "https://doi.org/10.1042/bst0280601" @default.
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