pH studies toward the elucidation of the auxiliary catalyst for pig heart aspartate aminotransferase
- 18 January 1983
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 22 (2), 375-382
- https://doi.org/10.1021/bi00271a022
Abstract
No abstract availableThis publication has 16 references indexed in Scilit:
- Catalytic activity in crystals of mitochondrial aspartate aminotransferase as detected by microspectrophotometryJournal of Biological Chemistry, 1978
- The mechanism of anion inhibition of pork heart aspartate aminotransferaseArchives of Biochemistry and Biophysics, 1978
- Solvent interactions with the active site of the pig heart cytosolic aspartate aminotransferaseArchives of Biochemistry and Biophysics, 1977
- Carbamylation of aspartate transaminase and the pK value of the active site lysyl residue.Journal of Biological Chemistry, 1976
- A Molecular Mechanism for Enzymatic TransaminationNature, 1966
- GLUTAMIC-ASPARTIC TRANSAMINASE .X. MECHANISM AND ORDER OF FORMATION OF ENZYME-SUBSTRATE CARBOXYLATE BONDS1966
- The Interaction of Aspartate Aminotransferase with α-Methylaspartic Acid*Biochemistry, 1966
- GLUTAMIC-ASPARTIC TRANSAMINASE .7. EQUILIBRIUM KINETICS WITH ERYTHRO-BETA-HYDROXYASPARTIC ACID1964
- A Kinetic and Equilibrium Analysis of the Glutamic Oxaloacetate Transaminase MechanismJournal of Biological Chemistry, 1962
- GLUTAMIC-ASPARTIC TRANSAMINASE .6. REACTION WITH CERTAIN BETA-SUBSTITUTED ASPARTIC ACID ANALOGUES1961