The Crystal Structure of Phosphinothricin in the Active Site of Glutamine Synthetase Illuminates the Mechanism of Enzymatic Inhibition-Reference-Cited by-同舟云学术

The Crystal Structure of Phosphinothricin in the Active Site of Glutamine Synthetase Illuminates the Mechanism of Enzymatic Inhibition

Published:2001-01-27 Issue:7 Volume:40 Page:1903-1912
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Gill Harindarpal S.¹,Eisenberg David¹

Affiliation:

1. UCLA-DOE Lab of Structural Biology and Molecular Medicine, Departments of Chemistry and Biochemistry and Biological Chemistry, Box 951570, University of California, Los Angeles, California 90095-1570

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi002438h

Reference58 articles.

1. Studies on the Mechanism of Glutamine Synthesis: Evidence for the Formation of Enzyme-bound Activated Glutamic Acid

2. A stereochemical method for detection of ATP terminal phosphate transfer in enzymatic reactions. Glutamine synthetase.

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