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.
journal_name
Biochem Soc Transjournal_title
Biochemical Society transactionsauthors
von Wettstein-Knowles P,Olsen J,Arnvig Mcguire K,Larsen Sdoi
10.1042/0300-5127:0280601keywords:
subject
Has Abstractpub_date
2000-12-01 00:00:00pages
601-7issue
6eissn
0300-5127issn
1470-8752journal_volume
28pub_type
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