A Model for Enzyme−Substrate Interaction in Alanine Racemase-Reference-Cited by-同舟云学术

A Model for Enzyme−Substrate Interaction in Alanine Racemase

Published:2001-03-01 Issue:12 Volume:123 Page:2830-2834
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Ondrechen Mary Jo¹,Briggs James M.¹,McCammon J. Andrew¹

Affiliation:

1. Contribution from the Department of Chemistry, Northeastern University, Boston, Massachusetts 02115-5000, Department of Biology and Biochemistry, University of Houston, Houston, Texas 77204-5513, and Department of Chemistry and Biochemistry, University of California San Diego, and Howard Hughes Medical Institute, La Jolla, California 92093-0365

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja0029679

Reference26 articles.

1. Tyrosine 265 of Alanine Racemase Serves as a Base Abstracting -Hydrogen from L-Alanine: The Counterpart Residue to Lysine 39 Specific to D-Alanine

2. Transamination as a Side-Reaction Catalyzed by Alanine Racemase of Bacillus stearothermophilus

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