About: Transition-state stabilization in the mechanism of tyrosyl-tRNA synthetase revealed by protein engineering

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About: Transition-state stabilization in the mechanism of tyrosyl-tRNA synthetase revealed by protein engineering Goto Sponge NotDistinct Permalink

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scientific article published on December 1985

Attributes	Values
rdf:type	Item
description	videnskabelig artikel (da) article científic (ca) articolo scientifico (it) artigo científico (pt) bilimsel makale (tr) vedecký článok (sk) vetenskaplig artikel (sv) vědecký článek (cs) wetenschappelijk artikel (nl) wissenschaftlicher Artikel (de) научни чланак (sr) article scientifique (fr) artículu científicu espublizáu en 1985 (ast) наукова стаття, опублікована в грудні 1985 (uk) 1985年學術文章 (zh) مقالة علمية نشرت في ديسمبر 1985 (ar) scientific article published on December 1985 (en)
publication date	wds:Q37537194-FF459CF7-F172-4F60-9703-E0C07E409EC6
publication date	1985-12-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q37537194-FB7B7C5E-72F9-49DF-9F74-D7A5E567E552
language of work or name	English
cites work	wds:Q37537194-09BB115D-9B47-4038-AEB5-F9887F8B746E wds:Q37537194-1B6F3BC7-FC91-449F-9F6E-F771FBA88025 wds:Q37537194-3BA1D2FF-9DE4-4A37-B721-EB49F6ACCA17 wds:Q37537194-5442908D-8405-47A7-8314-5EDBD53BD78B wds:Q37537194-59967D6C-7922-4AD2-8424-843947AA42C7 wds:Q37537194-67A57FE0-0BF4-4CEF-8FD9-1A90EEAE1F43 wds:Q37537194-7FF8FB31-F717-4BC3-8DE4-4EDCCA32A10C wds:Q37537194-8560A540-D273-4BB0-A420-FA110B8EBD61 wds:Q37537194-A1D7E7B7-1777-4AE3-AD40-3A343E85F7DB wds:Q37537194-B9DE67CB-F4A1-4C82-9FB0-6D8AE96F76A0 wds:Q37537194-BD600137-2AB6-498A-80DA-F811F7AC4E63 wds:Q37537194-CED8CD91-8B92-4824-ABD9-C864D0EDB84A wds:Q37537194-E3567452-B34F-4114-A509-5547E14D55DC
cites work	Entropic Contributions to Rate Accelerations in Enzymic and Intramolecular Reactions and the Chelate Effect Hydrogen bonding and biological specificity analysed by protein engineering Redesigning enzyme structure by site-directed mutagenesis: tyrosyl tRNA synthetase and ATP binding Binding Energy, Specificity, and Enzymic Catalysis: The Circe Effect The use of double mutants to detect structural changes in the active site of the tyrosyl-tRNA synthetase (Bacillus stearothermophilus) Site-directed mutagenesis as a probe of enzyme structure and catalysis: tyrosyl-tRNA synthetase cysteine-35 to glycine-35 mutation Conserved cysteine and histidine residues in the structures of the tyrosyl and methionyl-tRNA synthetases Deletion mutagenesis using an ‘M13 splint’: the N-terminal structural domain of tyrosyl-tRNA synthetase (B. stearothermophilus) catalyses the formation of tyrosyl adenylate Ligand binding and enzymic catalysis coupled through subunits in tyrosyl-tRNA synthetase Catalysis, binding and enzyme-substrate complementarity. Probing histidine-substrate interactions in tyrosyl-tRNA synthetase using asparagine and glutamine replacements Demonstration of two reaction pathways for the aminoacylation of tRNA. Application of the pulsed quenched flow technique Interaction of crystalline tyrosyl-tRNA synthetase with adenosine, adenosine monophosphate, adenosine triphosphate and pyrophosphate in the presence of tyrosinol
author name string	wds:Q37537194-F1DA54B0-6FF1-4A3E-90FC-F12EC60C3166 wds:Q37537194-FBF511EC-D358-4BF9-B3C6-2DD3BAD49428
author name string	Leatherbarrow RJ Winter G
rdfs:label	Transition-state stabilization in the mechanism of tyrosyl-tRNA synthetase revealed by protein engineering (en) Transition-state stabilization in the mechanism of tyrosyl-tRNA synthetase revealed by protein engineering (nl) Transition-state stabilization in the mechanism of tyrosyl-tRNA synthetase revealed by protein engineering (ast)
skos:prefLabel	Transition-state stabilization in the mechanism of tyrosyl-tRNA synthetase revealed by protein engineering (en) Transition-state stabilization in the mechanism of tyrosyl-tRNA synthetase revealed by protein engineering (nl) Transition-state stabilization in the mechanism of tyrosyl-tRNA synthetase revealed by protein engineering (ast)
name	Transition-state stabilization in the mechanism of tyrosyl-tRNA synthetase revealed by protein engineering (en) Transition-state stabilization in the mechanism of tyrosyl-tRNA synthetase revealed by protein engineering (nl) Transition-state stabilization in the mechanism of tyrosyl-tRNA synthetase revealed by protein engineering (ast)
author	wds:Q37537194-D2680E27-74F0-4479-B63B-439421F4D79F
author	Alan Fersht
title	wds:Q37537194-27B9346C-95CC-4B62-86A4-61FCD408D3A2
title	Transition-state stabilization in the mechanism of tyrosyl-tRNA synthetase revealed by protein engineering (en)
page(s)	wds:Q37537194-E5D0BF74-EC01-4323-B16D-8456F7C7BFDD
page(s)	7840-7844
instance of	wds:Q37537194-0C01CC21-9F95-4CAB-B28A-AEF5731D2EE4
instance of	scholarly article
PubMed ID	wds:Q37537194-04B12775-3147-4EEF-A13B-0EC5AAE27ECB
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/3865201
PubMed ID	3865201
published in	wds:Q37537194-7E44EC44-BCED-4CC1-B47E-26A325B2A58F
published in	Proceedings of the National Academy of Sciences of the United States of America
issue	wds:Q37537194-B7D8C907-FF60-4B79-B403-95E94D655607
volume	wds:Q37537194-B957C113-D94C-4F51-8D4B-34EAEA46FF04
issue	23
volume	82
DOI	wds:Q37537194-9D247803-EED3-4ACA-BD26-4CB4D6475190
DOI	http://dx.doi.org/10.1073/PNAS.82.23.7840
DOI	10.1073/PNAS.82.23.7840
ResearchGate publication ID	wds:Q37537194-A40DD377-6B6D-4708-976A-C9171F13BB72
ResearchGate publication ID	19297140
ADS bibcode	wds:Q37537194-205D1A77-4CB7-495B-9726-5C46F5A1BE42
ADS bibcode	1985PNAS...82.7840L
PMCID	wds:Q37537194-CA478397-3C88-4126-A2AA-57A16B18405D
PMCID	390865
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q37537194
is cites work of	Protein engineering. The design, synthesis and characterization of factitious proteins Crystal structure ofStaphylococcus aureustyrosyl-tRNA synthetase in complex with a class of potent and specific inhibitors Electrostatic origin of the catalytic power of enzymes and the role of preorganized active sites X-ray crystallography reveals a large conformational change during guanyl transfer by mRNA capping enzymes Identification of signalling and non-signalling binding contributions to enzyme reactivity. Alternative combinations of binding interactions provide for change in transition-state geometry in reactions of papain Aspartyl-tRNA synthetase from Escherichia coli: cloning and characterisation of the gene, homologies of its translated amino acid sequence with asparaginyl- and lysyl-tRNA synthetases. Enzyme catalysis: not different, just better Computer simulations of enzyme catalysis: finding out what has been optimized by evolution. CTP:phosphocholine cytidylyltransferase Quantitative analysis of structure–activity relationships in engineered proteins by linear free-energy relationships Importance of stalk segment S5 for intramolecular communication in the sarcoplasmic reticulum Ca2+-ATPase Structure of a complex between a cap analogue and mRNA guanylyl transferase demonstrates the structural chemistry of RNA capping

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