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Biochemistry|March 28, 1995
Decreasing the basicity of the active site base, Lys-258, of Escherichia coli aspartate aminotransferase by replacement with gamma-thialysineL M Gloss, J F KirschBiochemistry|September 26, 1995
Examining the structural and chemical flexibility of the active site base, Lys-258, of Escherichia coli aspartate aminotransferase by replacement with unnatural amino acidsL M Gloss, J F KirschBiochemistry|June 14, 1988
Role of arginine-292 in the substrate specificity of aspartate aminotransferase as examined by site-directed mutagenesisC N Cronin, J F KirschBiochemistry|July 30, 1991
Kinetics and equilibria for the reactions of coenzymes with wild type and the Y70F mutant of Escherichia coli aspartate aminotransferaseM D Toney, J F KirschBiochemistry|March 16, 1982
Investigation of diffusion-limited rates of chymotrypsin reactions by viscosity variationA C Brouwer, J F KirschAnalytical Biochemistry|November 14, 1997
A continuous coupled spectrophotometric assay for tyrosine aminotransferase activity with aromatic and other nonpolar amino acidsT N Luong, J F KirschBiochemistry|March 28, 1995
Use of site-directed mutagenesis and alternative substrates to assign the prototropic groups important to catalysis by Escherichia coli aspartate aminotransferaseL M Gloss, J F KirschProtein Science : a Publication of the Protein Society|September 1, 1995
Redesign of the substrate specificity of Escherichia coli aspartate aminotransferase to that of Escherichia coli tyrosine aminotransferase by homology modeling and site-directed mutagenesisJ J Onuffer, J F KirschBiochemistry|June 27, 1978
Effects of substituents on the rates of deacylation of substituted benzoyl papains. Role of a carboxylate residue in the catalytic mechanismV I Zannis, J F KirschPageof 42