d-Cycloserine Inactivation of d-Amino Acid Aminotransferase Leads to a Stable Noncovalent Protein Complex with an Aromatic Cycloserine-PLP Derivative-Reference-Cited by-同舟云学术

d-Cycloserine Inactivation of d-Amino Acid Aminotransferase Leads to a Stable Noncovalent Protein Complex with an Aromatic Cycloserine-PLP Derivative

Published:1998-02-07 Issue:10 Volume:120 Page:2268-2274
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Peisach Daniel¹,Chipman David M.¹,Van Ophem Peter W.¹,Manning James M.¹,Ringe Dagmar¹

Affiliation:

1. Contribution from the Departments of Biochemistry and Chemistry and the Rosenstiel Basic Medical Sciences Research Center, Brandeis University, 415 South Street, Waltham, Massachusetts 02254-9110, Department of Life Sciences, Ben Gurion University, Beer-Sheva, 84105, Israel, and Department of Biology, Northeastern University, Boston, Massachusetts 02215

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja973353f

Reference22 articles.

1. Different modes of action of inhibitors of bacterial D-amino acid transaminase. A target enzyme for the design of new antibacterial agents.

2. Braunstein, A. E.The Enzymes; 3rd ed.; Braunstein, A. E., Ed.; Academic Press: New York, 1973; Vol. 9, pp 440−448.

3. Crystal Structure of a D-Amino Acid Aminotransferase: How the Protein Controls Stereoselectivity

4. Accurate computation of the rotation matrices

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