Enzyme catalysis: removing chemically ‘essential’ residues by site-directed mutagenesis
- 1 August 2001
- journal article
- review article
- Published by Elsevier in Trends in Biochemical Sciences
- Vol. 26 (8) , 497-503
- https://doi.org/10.1016/s0968-0004(01)01911-9
Abstract
No abstract availableKeywords
This publication has 47 references indexed in Scilit:
- Identification of the histidine and aspartic acid residues essential for enzymatic activity of a family I.3 lipase by site‐directed mutagenesisFEBS Letters, 2000
- Enzyme-Induced Strain/Distortion in the Ground-State ES Complex in β-Lactamase Catalysis Revealed by FTIRBiochemistry, 2000
- Substrate‐assisted catalysis: Molecular basis and biological significanceProtein Science, 2000
- From β‐glucanase to β‐glucansynthase: glycosyl transfer to α‐glycosyl fluorides catalyzed by a mutant endoglucanase lacking its catalytic nucleophileFEBS Letters, 1998
- Chemical Reactivity of Penicillins and Cephalosporins. Intramolecular Involvement of the Acyl-Amido Side ChainThe Journal of Organic Chemistry, 1998
- Dissecting histidine interactions of ribonuclease T1 with asparagine and glutamine replacements: analysis of double mutant cycles at one positionJournal of Molecular Biology, 1998
- Identification of Enzyme−Substrate and Enzyme−Product Complexes in the Catalytic Mechanism of Glucoamylase from Aspergillus awamoriBiochemistry, 1996
- A Proficient EnzymeScience, 1995
- Site-Directed Mutagenesis of the Catalytic Base Glutamic Acid 400 in Glucoamylase from Aspergillus niger and of Tyrosine 48 and Glutamine 401, Both Hydrogen-Bonded to the .gamma.-Carboxylate Group of Glutamic Acid 400Biochemistry, 1994
- Functional Interactions among the His40, Glu58 and His92 Catalysts of Ribonuclease T1 as Studied by Double and Triple MutantsJournal of Molecular Biology, 1993