Detection and Time Course of Formation of Major Thiamin Diphosphate-Bound Covalent Intermediates Derived from a Chromophoric Substrate Analogue on Benzoylformate Decarboxylase-Reference-Cited by-同舟云学术

Detection and Time Course of Formation of Major Thiamin Diphosphate-Bound Covalent Intermediates Derived from a Chromophoric Substrate Analogue on Benzoylformate Decarboxylase

Published:2009-01-13 Issue:5 Volume:48 Page:981-994
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Chakraborty Sumit¹,Nemeria Natalia S.¹,Balakrishnan Anand¹,Brandt Gabriel S.¹,Kneen Malea M.¹,Yep Alejandra¹,McLeish Michael J.¹,Kenyon George L.¹,Petsko Gregory A.¹,Ringe Dagmar¹,Jordan Frank¹

Affiliation:

1. Department of Chemistry, Rutgers University, Newark, New Jersey 07102, Department of Medicinal Chemistry, College of Pharmacy, University of Michigan, Ann Arbor, Michigan 48109, and Departments of Chemistry and Biochemistry, Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, Massachusetts 02454

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi801810h

Reference45 articles.

1. The Crystal Structure of Benzoylformate Decarboxylase at 1.6 Å Resolution: Diversity of Catalytic Residues in Thiamin Diphosphate-Dependent Enzymes,

2. Kinetics and mechanism of benzoylformate decarboxylase using carbon-13 and solvent deuterium isotope effects on benzoylformate and benzoylformate analogs

3. Current mechanistic understanding of thiamin diphosphate-dependent enzymatic reactions

4. Experimental observation of thiamin diphosphate-bound intermediates on enzymes and mechanistic information derived from these observations

5. Observation of a 2-.alpha.-enamine from a 2-(methoxyphenylmethyl)-3,4-dimethylthiazolium salt in water: implications for catalysis by thiamin diphosphate-dependent .alpha.-keto acid decarboxylases

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