Molecular aspects of beta-ketoacyl synthase (KAS) catalysis |
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Authors: | von Wettstein-Knowles P Olsen J Arnvig Mcguire K Larsen S |
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Institution: | Genetics Department, Molecular Biology Institute, Copenhagen University, Oester Farimagsgade 2A, DK-1353 Copenhagen K, Denmark. knowles@biobase.dk |
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Abstract: | Crystal structure data for Escherichia coli beta-ketoacyl synthase (KAS) I with C(10) and C(12) 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. |
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