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Your search keyword '"Dunaway-Mariano, Debra"' showing total 5 results
Start Over Author "Dunaway-Mariano, Debra" Journal febs letters
5 results on '"Dunaway-Mariano, Debra"'

3. The YbgC protein encoded by the ybgC gene of the tol-pal gene cluster of Haemophilus influenzae catalyzes acyl-coenzyme A thioester hydrolysis

Author

Zhuang, Zhihao, Song, Feng, Martin, Brian M., and Dunaway-Mariano, Debra

Subjects
OPERONS, ESTERASES, PSEUDOMONAS
Abstract

This paper examines the catalytic function of the protein YbgC, encoded by the ybgC gene of the tol-pal gene cluster in Haemophilus influenzae. The YbgC protein, a homologue of the Pseudomonas sp. strain CBS3 4-hydroxybenzoyl-coenzyme A thioesterase, conserves the active site Asp residue associated with thioesterase activity. The H. influenzae ybgC gene was cloned and overexpressed in Escherichia coli. The recombinant protein was purified and tested for thioesterase activity towards acyl-CoA and acyl-N-acetylcysteamine thioesters. The YbgC protein catalyzes the hydrolysis of short chain aliphatic acyl-CoA thioesters, while the D18N YbgC mutant protein (prepared to serve as a control) does not. [Copyright &y& Elsevier]

Published
2002
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5. Determination of the catalytic pathway of C 4-leaf pyruvate, orthophosphate dikinase from maize

Author

Carroll, Lawrence J., Dunaway-Mariano, Debra, Smith, Christopher M., and Chollet, Raymond

Abstract

The mechanism of the maize pyruvate, phosphate dikinase-catalyzed conversion of adenosine 5'-triphosphate, orthophosphate and pyruvale to adenosine 5'-monophosphate, inorganic pyrophosphate and phosphoenolpyruvale. respectively, was determined by using transient kinetic techniques. The data obtained demonstrate that catalysis in the maize pyruvate. phosphate dikinasc active site involves initial transfer of the P βP-unit from adenosine 5'- triphosphate to the enzyme to form a pyrophosphorylenzyme intermediate. followed by sequential phosphoryl group transfer to orthophosphate (to form pyrophosphate and a phosphoenzyme intermediate) and pyruvate (to form phosphoenolpyruvate and free enzyme).

Published
1990
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