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Investigation of the reaction mechanisms catalyzed by 4-hydroxybenzoyl-coenzyme A thioesterase and 4-chlorobenzoyl-coenzyme A dehalogenase of the Pseudomonas sp. strain CBS3

Posted on:1997-09-30Degree:Ph.DType:Dissertation
University:University of Maryland, College ParkCandidate:Taylor, Kimberly LouiseFull Text:PDF
GTID:1461390014983721Subject:Chemistry
Abstract/Summary:
Analysis of substrate analogs for 4-HBA-CoA thioesterase indicated that the hydroxylbenzoyl group plays and the nucleotide portion of the CoA moiety function in substrate binding and recognition Analysis of the k;The substrate specificity of 4-CBA-CoA dehalogenase is shown to be governed by the sizes of the para substituent on the benzoyl ring, and the conformation of the substrate/product analog free in solution. UV-visible, ;Catalytic residues functioning in the dehalogenase enzyme active site were probed using chemical modification and site-directed mutagenesis techniques. Three residues, Trp137, and His90 and His81, were identified. UV-vis and...
Keywords/Search Tags:Dehalogenase
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