About: Conserved cysteine and histidine residues in the structures of the tyrosyl and methionyl-tRNA synthetases

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About: Conserved cysteine and histidine residues in the structures of the tyrosyl and methionyl-tRNA synthetases Goto Sponge NotDistinct Permalink

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scientific article published on 01 August 1982

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в серпні 1982 (uk) im August 1982 veröffentlichter wissenschaftlicher Artikel (de) artículu científicu espublizáu n'agostu de 1982 (ast) scientific article published on 01 August 1982 (en)
publication date	wds:Q71444958-90CFACF2-FE42-4237-ABF2-F950E14B57C9
publication date	1982-08-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q71444958-C29DD7BD-AC5A-4FC1-9725-BC89C87A6DE2
language of work or name	English
cites work	wds:Q71444958-00C70FAA-C709-4DEC-BF56-7EBF16A734C3 wds:Q71444958-22774708-8122-4ECA-BF0E-15D0D5B623FB wds:Q71444958-327F7D7B-F258-4608-A57C-9ECD5FE5460A wds:Q71444958-3548A191-6C73-4222-86FA-B56077E38762 wds:Q71444958-4D721F29-133D-48B4-8021-1FCB0294BCBE wds:Q71444958-5A92983D-65C5-4F5D-B954-5DFBC96BBB58 wds:Q71444958-5B4AE2A7-9E38-4449-8C86-11E6BC7C0E38 wds:Q71444958-5F03207A-F385-47CE-B822-34A78697C52C wds:Q71444958-67830F01-1A56-4046-8718-0F9F4CAAD628 wds:Q71444958-699E53C6-0A4F-43B9-A43B-FEE8FAB8AA0E wds:Q71444958-748597A7-E9F6-4AF2-AC2E-E50BA3BAF3A1 wds:Q71444958-78B652EA-CF51-474F-814E-D1C0EFE4DD8C wds:Q71444958-7D757ED0-D078-45A5-9FBC-5A7E8D4A9EF0 wds:Q71444958-7DE69F23-2413-4C49-B019-A2347B954D64 wds:Q71444958-7EB1E624-11CD-48E9-8012-A2AB802AA10A wds:Q71444958-8CA0F9BF-BFB0-4798-A575-AE86009DA23D wds:Q71444958-9BCE50AF-56E9-495B-85E4-7B3EBE0A8090 wds:Q71444958-AD1220F3-2A3D-4FB2-B709-6E6ACE52FCAD wds:Q71444958-AE6926C4-FA1D-46C4-9081-F7AD2B20550E wds:Q71444958-BFE66025-4070-4ED5-8BF0-8E37D5814EDF wds:Q71444958-C52DFE7E-7012-40CD-A045-F1CEE10E7315 wds:Q71444958-CD6138EC-AF04-4DC9-A2F4-D43144255691 wds:Q71444958-CE2E208A-667E-42F4-89B8-29586AC5A5BB
cites work	Primary structure of a large aminoacyl-tRNA synthetase. Crystal structure of yeast tRNAAsp Labelling of L-isoleucine tRNA ligase from Escherichia coli with L-isoleucyl-bromomethyl ketone The mechanism of action of methionyl-tRNA synthetase from Escherichia coli. Mechanism of the amino-acid activation reaction catalyzed by the native and the trypsin-modified enzymes. Methionyl-tRNA synthetase shows the nucleotide binding fold observed in dehydrogenases Tests for comparing related amino-acid sequences. Cytochrome c and cytochrome c551 Aminoacyl-tRNA Synthetases: General Features and Recognition of Transfer RNAs Crystal structure of Escherichia coli methionyl-tRNA synthetase at 2.5 A resolution Repeating sequences in aminoacyl-tRNA synthetases. Glycyl transfer ribonucleic acid synthetase from Escherichia coli: purification, properties, and substrate binding Modification of phenylalanyl-tRNA synthetase from Escherichia coli by histidine-specific reagents. Effects on structure and function Structural organization of complexes of transfer RNAs with aminoacyl transfer RNA synthetases Demonstration of two reaction pathways for the aminoacylation of tRNA. Application of the pulsed quenched flow technique Yeast phenylalanyl-tRNA synthetase. Properties of the histidyl residues Role of sulfhydryl groups in activating enzymes. Properties of Escherichia coli lysine-transfer ribonucleic acid synthetase Amino acid activation in crystalline tyrosyl-tRNA synthetase from Bacillus stearothermophilus Affinity labelling of yeast phenylalanyl-tRNA synthetase with a 3'-oxidised tRNAPhe. Isolation and sequence of the labelled peptide Evidence for Essential Histidine Residues in Tryptophanyl-tRNA Synthetase Requirement of different sulfhydryl groups in the activation and transfer reactions of isoleucyl transfer ribonucleic acid synthetase Leucyl-tRNA synthetase. Two forms of the enzyme: role of sulfhydryl groups [Study of methionyl tRNA synthetase of Escherichia coli. 2. Selective and reversible inactivation of the capacity to activate tRNA] Yeast phenylalanyl-tRNA synthetase: Properties of the sulfhydryl groups; evidence for -SH requirement in tRNA acylation The amino acid sequence of tryptophanyl tRNA synthetase from Bacillus stearothermophilus
author name string	wds:Q71444958-90F9086A-2593-4C93-99D9-F2096C0E595E wds:Q71444958-C977BF83-A905-4C34-98A6-45767809A979
author name string	Winter G Barker DG
rdfs:label	Conserved cysteine and histidine residues in the structures of the tyrosyl and methionyl-tRNA synthetases (en) Conserved cysteine and histidine residues in the structures of the tyrosyl and methionyl-tRNA synthetases (nl)
skos:prefLabel	Conserved cysteine and histidine residues in the structures of the tyrosyl and methionyl-tRNA synthetases (en) Conserved cysteine and histidine residues in the structures of the tyrosyl and methionyl-tRNA synthetases (nl)
name	Conserved cysteine and histidine residues in the structures of the tyrosyl and methionyl-tRNA synthetases (en) Conserved cysteine and histidine residues in the structures of the tyrosyl and methionyl-tRNA synthetases (nl)
title	wds:Q71444958-50AC493E-1FA9-4CC2-937E-D81DB0831E0C
title	Conserved cysteine and histidine residues in the structures of the tyrosyl and methionyl-tRNA synthetases (en)
page(s)	wds:Q71444958-CEDDC534-E673-4CA6-8A4A-24A82B316612
page(s)	191-193
instance of	wds:Q71444958-CAA4E209-0E38-4B10-A961-96D41A5CC995
instance of	scholarly article
PubMed ID	wds:Q71444958-3B0EBFFE-D230-4559-ABD1-652BA7B1D8DC
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/6751870
PubMed ID	6751870
published in	wds:Q71444958-D53993E5-D078-4EB0-940B-425A8CD2E6D6
published in	FEBS Letters
issue	wds:Q71444958-700C96C4-FC5F-40A5-A1BB-3AAC8835D5E5
volume	wds:Q71444958-3A9AE9E4-7E69-4CBD-BF3F-1EE11E46C5F1
issue	2
volume	145
number of pages	wds:Q71444958-4EB0256A-B89E-478F-BC20-D90987E745FE
number of pages	3 (xsd:decimal)
DOI	wds:Q71444958-396FEE46-8EE5-41F1-B24C-0FD3BEEEBDAD
DOI	http://dx.doi.org/10.1016/0014-5793(82)80165-8
DOI	10.1016/0014-5793(82)80165-8
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q71444958
is cites work of	The crystal structure of E. coli pantothenate synthetase confirms it as a member of the cytidylyltransferase superfamily Crystal Structure of Tryptophanyl-tRNA Synthetase Complexed with Adenosine-5′ Tetraphosphate: Evidence for Distributed Use of Catalytic Binding Energy in Amino Acid Activation by Class I Aminoacyl-tRNA Synthetases Sequence similarities among the family of aminoacyl-tRNA synthetases. Purification and properties of the lipoate protein ligase of Escherichia coli Modular arrangement of functional domains along the sequence of an aminoacyl tRNA synthetase Redesigning enzyme structure by site-directed mutagenesis: tyrosyl tRNA synthetase and ATP binding Homology of aspartyl- and lysyl-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 Structural homology in the amino-terminal domains of two aminoacyl-tRNA synthetases L-arginine recognition by yeast arginyl-tRNA synthetase Transition-state stabilization in the mechanism of tyrosyl-tRNA synthetase revealed by protein engineering Primary structures of both subunits of Escherichia coli glycyl-tRNA synthetase Transition state stabilization by a phylogenetically conserved tyrosine residue in methionyl-tRNA synthetase

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