[4] Site-directed mutagenesis: A tool for studying enzyme catalysis
- 1 January 1995
- book chapter
- Published by Elsevier
- Vol. 249, 91-119
- https://doi.org/10.1016/0076-6879(95)49032-9
Abstract
No abstract availableThis publication has 100 references indexed in Scilit:
- The structural consequences of exchanging tryptophan and tyrosine residues in B.stearothermophilus lactate dehydrogenaseProtein Engineering, Design and Selection, 1992
- Charge balance in the α‐hydroxyacid dehydrogenase vacuole: An acid testProtein Science, 1992
- Broønsted analysis of aspartate aminotransferase via exogenous catalysis of reactions of an inactive mutantProtein Science, 1992
- Escherichia coli aspartate carbamoyltransferase: the probing of crystal structure analysis via site-specific mutagenesisProtein Engineering, Design and Selection, 1991
- Structural plasticity broadens the specificity of an engineered proteaseNature, 1989
- Complex of N-phosphonacetyl-l-aspartate with aspartate carbamoyltransferaseJournal of Molecular Biology, 1988
- Dissection of the structure and activity of the tyrosyl-tRNA synthetase by site-directed mutagenesisBiochemistry, 1987
- Relationships between enzymatic catalysis and active site structure revealed by applications of site-directed mutagenesisChemical Reviews, 1987
- Internal thermodynamics of position 51 mutants and natural variants of tyrosyl-tRNA synthetaseBiochemistry, 1986
- The Formation of Anhydrochymotrypsin by Removing the Elements of Water from the Serine at the Active Site1Journal of the American Chemical Society, 1966