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Crystal structure data for Escherichia coli P-ketoacyl synthase (KAS) I with C,, and C,, 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 11, the other for KAS I11 and chalcone synthase. A comparison of the structures of KAS I and KAS I1 does not reveal the basis of chain-length specificity. T h e structures of the Arabidopsis thaliana KAS family are compared.

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