Irreversible inactivation of aspartate aminotransferases during transamination with L-propargylglycine
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference17 articles.
1. Evidence for the presence of a distinct subsite for binding the distal carboxyl group of dicarboxylate substrates and its role in the catalytic activity of aspartate aminotransferase
2. Formate-induced Labeling of the Active Site of Aspartate Aminotransferase by β-Chloro-l-alanine
3. Acetylenic enzyme inactivators. Inactivation of .gamma.-cystathionase, in vitro and in vivo by propargylglycine
4. Active site-directed inactivation of cystathionine γ-synthetase and glutamic pyruvic transaminase by propargylglycine
5. The Syntheses and Microbiological Properties of Acetylenic Amino Acids. Propargylglycine and 2-Amino-3-methyl-4-pentynoic Acid1
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