Site-directed mutagenesis reveals transition-state stabilization as a general catalytic mechanism for aminoacyl-tRNA synthetases

Biochemistry ◽  
1987 ◽  
Vol 26 (23) ◽  
pp. 7246-7250 ◽  
Author(s):  
Thor J. Borgford ◽  
Tamara E. Gray ◽  
Nigel J. Brand ◽  
Alan R. Fersht
Keyword(s):  
Transition State ◽  
Catalytic Mechanism ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Trna Synthetases ◽  
Aminoacyl Trna Synthetases ◽  
Transition State Stabilization

Functional tyrosine residue in the active center of human dipeptidyl peptidase III

2008 ◽  
Vol 389 (2) ◽  
pp. 163-167 ◽  
Author(s):  
Branka Salopek-Sondi ◽  
Bojana Vukelić ◽  
Jasminka Špoljarić ◽  
Šumski Šimaga ◽  
Dušica Vujaklija ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Transition State ◽  
Active Site ◽  
Functional Role ◽  
Dipeptidyl Peptidase ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Tyrosine Residue ◽  
Transition State Stabilization ◽  
Endogenous Defense

Abstract Human dipeptidyl peptidase III (DPP III) is a member of the metallopeptidase family M49 with an implied role in the pain-modulatory system and endogenous defense against oxidative stress. Here, we report the heterologous expression of human DPP III and the site-directed mutagenesis results which demonstrate a functional role for Tyr318 at the active site of this enzyme. The substitution of Tyr318 to Phe decreased k cat by two orders of magnitude without altering the binding affinity of substrate, or of a competitive hydroxamate inhibitor designed to interact with S1 and S2 subsites. The results indicate that the conserved tyrosine could be involved in transition state stabilization during the catalytic action of M49 peptidases.

Site-directed mutagenesis of active site contact residues in a hydrolytic abzyme: evidence for an essential histidine involved in transition state stabilization

1997 ◽  
Vol 267 (5) ◽  
pp. 1247-1257 ◽  
Author(s):  
Hideaki Miyashita ◽  
Tomoko Hara ◽  
Ryuji Tanimura ◽  
Shiro Fukuyama ◽  
Christine Cagnon ◽  
...  
Keyword(s):  
Transition State ◽  
Active Site ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Transition State Stabilization ◽  
Contact Residues

scholarly journals Transition state stabilization by the ‘high’ motif of class I aminoacyl-tRNA synthetases: the case ofEscherichia colimethionyl-tRNA synthetase

1995 ◽  
Vol 23 (23) ◽  
pp. 4793-4798 ◽  
Author(s):  
Emmanuelle Schmitt ◽  
Michel Panvert ◽  
Sylvain Blanquet ◽  
Yves Mechulam
Keyword(s):  
Transition State ◽  
Trna Synthetase ◽  
Class I ◽  
Trna Synthetases ◽  
Aminoacyl Trna Synthetases ◽  
Transition State Stabilization

β-Amyrin biosynthesis: catalytic mechanism and substrate recognition

2017 ◽  
Vol 15 (14) ◽  
pp. 2869-2891 ◽  
Author(s):  
Tsutomu Hoshino
Keyword(s):  
Catalytic Mechanism ◽  
Substrate Recognition ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
The Past ◽  
Substrate Analog ◽  
Analog Experiments

In the past five years, there have been remarkable advances in the study of β-amyrin synthase. This review outlines the catalytic mechanism and substrate recognition in β-amyrin biosynthesis, which have been attained by the site-directed mutagenesis and substrate analog experiments.

Probing the Catalytic Mechanism of Prephenate Dehydratase by Site-Directed Mutagenesis of theEscherichia coliP-Protein Dehydratase Domain†

Biochemistry ◽  
2000 ◽  
Vol 39 (16) ◽  
pp. 4722-4728 ◽  
Author(s):  
Sheng Zhang ◽  
David B. Wilson ◽  
Bruce Ganem
Keyword(s):  
Catalytic Mechanism ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Prephenate Dehydratase

Catalytic Mechanism of theStreptomycesK15dd-Transpeptidase/Penicillin-Binding Protein Probed by Site-Directed Mutagenesis and Structural Analysis†,‡

Biochemistry ◽  
2003 ◽  
Vol 42 (10) ◽  
pp. 2895-2906 ◽  
Author(s):  
Noureddine Rhazi ◽  
Paulette Charlier ◽  
Dominique Dehareng ◽  
Danièle Engher ◽  
Marcel Vermeire ◽  
...  
Keyword(s):  
Structural Analysis ◽  
Catalytic Mechanism ◽  
Binding Protein ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Penicillin Binding Protein
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