β-Elimination of β-halo substrates by D-amino acid transaminase associated with inactivation of the enzyme. Trapping of a key intermediate in the reaction
- 8 August 1978
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 17 (16) , 3377-3384
- https://doi.org/10.1021/bi00609a031
Abstract
No abstract availableThis publication has 12 references indexed in Scilit:
- Chemical structure of the active site of pig heart mitochondrial aspartate aminotransferase labeled with beta-chloro-l-alanine.Journal of Biological Chemistry, 1978
- Inactivation of bacterial D-amino acid transaminase by beta-chloro-D-alanine.Journal of Biological Chemistry, 1977
- Inactivation of bacterial D-amino acid transaminases by the olefinic amino acid D-vinylglycine.Journal of Biological Chemistry, 1977
- Reactions of β-fluoroalanine and β-bromoalanine with D-amino acid oxidaseBiochemical and Biophysical Research Communications, 1976
- RELATIVE REACTIVITIES OF SULFHYDRYL GROUPS WITH N‐ACETYL DEHYDROALANINE AND N‐ACETYL DEHYDROALANINE METHYL ESTERInternational Journal of Peptide and Protein Research, 1976
- A new thiol-dependent transamination reaction catalyzed by the B protein of Escherichia coli tryptophan synthetaseBiochemistry, 1968
- Bromopyruvate Inactivation of 2-Keto-3-deoxy-6-phosphogluconic Aldolase. I. Kinetic Evidence for Active Site Specificity*Biochemistry, 1967
- D-ALANINE-D-GLUTAMATE TRANSAMINASE .I. PURIFICATION AND CHARACTERIZATION1965
- On the Isolation and Identification of 1,4-Thiazane-3-Carboxylic Acid S-Oxide from the Brown Alga Undaria pinnatifidaThe Journal of Biochemistry, 1963
- A STUDY OF BETA-HYDROXY-ALPHA-KETO ACIDS1946