Active-Site Engineering of Benzaldehyde Lyase Shows That a Point Mutation Can Confer Both New Reactivity and Susceptibility to Mechanism-Based Inhibition-Reference-Cited by-同舟云学术

Active-Site Engineering of Benzaldehyde Lyase Shows That a Point Mutation Can Confer Both New Reactivity and Susceptibility to Mechanism-Based Inhibition

Published:2009-12-23 Issue:2 Volume:132 Page:438-439
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Brandt Gabriel S.¹,Kneen Malea M.¹,Petsko Gregory A.¹,Ringe Dagmar¹,McLeish Michael J.¹

Affiliation:

1. Department of Biochemistry, Brandeis University, Waltham, Massachusetts 02454, and Department of Chemistry and Chemical Biology, Indiana University-Purdue University Indianapolis, Indianapolis, Indiana 46202

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja907064w

Reference20 articles.

1. [89] Benzoylformate decarboxylase (Pseudomonas putida)

2. Benzaldehyde lyase, a novel thiamine PPi-requiring enzyme, from Pseudomonas fluorescens biovar I

3. A new perspective on thiamine catalysis

4. Structural and Kinetic Analysis of Catalysis by a Thiamin Diphosphate-Dependent Enzyme, Benzoylformate Decarboxylase

5. Active site generated analogs of reactive intermediates in enzymic reactions. Potent inhibition of pyruvate dehydrogenase by a phosphonate analog of pyruvate

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