Chemical structure of the active site of pig heart mitochondrial aspartate aminotransferase labeled with beta-chloro-l-alanine.
Open Access
- 1 January 1978
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 253 (1) , 252-256
- https://doi.org/10.1016/s0021-9258(17)38297-2
Abstract
No abstract availableThis publication has 28 references indexed in Scilit:
- Catalytic function of a histidyl residue in cytosolic aspartate aminotransferase-catalyzed reactionsBiochemical and Biophysical Research Communications, 1975
- Homology of the primary structures of cytoplasmic and mitochondrial aspartate aminotransferases from pig heartFEBS Letters, 1974
- Sequence Analysis of Fluorescamine‐Stained Peptides and Proteins Purified on a Nanomole ScaleEuropean Journal of Biochemistry, 1974
- Labeling of the active site of cytoplasmic aspartate aminotransferase by β-chloro-L-alanineBiochemical and Biophysical Research Communications, 1973
- The complete amino acid sequence of cytoplasmic aspartate aminotransferase from pig heartFEBS Letters, 1973
- Selective modification of the mitochondrial isozyme of aspartate aminotransferase by .beta.-bromopropionate. I. Inactivation process and properties of inactivated enzymeBiochemistry, 1972
- 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 aminotransferaseBiochemical and Biophysical Research Communications, 1972
- A comparative study on the affinity labelling of aspartate aminotransferase isozymes by β-bromopyruvateBiochemical and Biophysical Research Communications, 1970
- Crystallization of 2-oxoglutarate L-aspartate transaminases from mitochondrial and soluble fractions of beef liverBiochemical and Biophysical Research Communications, 1963
- A General Mechanism for Vitamin B6-catalyzed Reactions1Journal of the American Chemical Society, 1954