Abstract:
:The crystal structure of the ternary complex citrate synthase-oxaloacetate-carboxymethyl coenzyme A has been solved to a resolution of 1.9 A and refined to a conventional crystallographic R factor of 0.185. The structure resembles a proposed transition state of the condensation reaction and suggests that the condensation reaction proceeds through a neutral enol rather than an enolate intermediate. A mechanism for the condensation reaction is proposed which involves the participation of three key catalytic groups (Asp 375, His 274, and His 320) in two distinct steps. The proposed mechanism invokes concerted general acid-base catalysis twice to explain both the energetics of the reaction and the experimentally observed inversion of stereochemistry at the attacking carbon atom.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Karpusas M,Branchaud B,Remington SJsubject
Has Abstractpub_date
1990-03-06 00:00:00pages
2213-9issue
9eissn
0006-2960issn
1520-4995journal_volume
29pub_type
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