schliessen

Filtern

 

Bibliotheken

The stereochemical course of amino acid activation by methionyl- and tyrosyl-tRNA synthetases

Stereochemical analysis has long been recognised as a powerful tool for elucidating the mechanisms of chemical and enzyme-catalysed reactions. Although much is known about the stereochemical course of reactions at saturated carbon, phosphate and thiophosphate esters whose ligands to phosphorus are a... Full description

Journal Title: Nature (London) 1979-09-27, Vol.281 (5729), p.320-321
Main Author: Langdon, Simon P
Other Authors: Lowe, Gordon
Format: Electronic Article Electronic Article
Language: English
Subjects:
Publisher: England
ID: ISSN: 0028-0836
Link: https://www.ncbi.nlm.nih.gov/pubmed/399325
Zum Text:
SendSend as email Add to Book BagAdd to Book Bag
Staff View
recordid: cdi_proquest_miscellaneous_75000650
title: The stereochemical course of amino acid activation by methionyl- and tyrosyl-tRNA synthetases
format: Article
creator:
  • Langdon, Simon P
  • Lowe, Gordon
subjects:
  • Amino Acyl-tRNA Synthetases - metabolism
  • Binding Sites
  • Catalysis
  • Escherichia coli - enzymology
  • Methionine-tRNA Ligase - metabolism
  • Phosphates
  • Stereoisomerism
  • Transfer RNA Aminoacylation
  • Tyrosine-tRNA Ligase - metabolism
ispartof: Nature (London), 1979-09-27, Vol.281 (5729), p.320-321
description: Stereochemical analysis has long been recognised as a powerful tool for elucidating the mechanisms of chemical and enzyme-catalysed reactions. Although much is known about the stereochemical course of reactions at saturated carbon, phosphate and thiophosphate esters whose ligands to phosphorus are also tetrahedrally disposed, are capable in principle of revealing sterochemical information about events at the active site of enzymes that transform such substrates. Nucleotidyl transferases are a group of enzymes which in general selectively use one of the diastereoisomers of a nucleoside 5'(1-thiotriphosphate), such as isomers A and B of adenosine 5'(1-thiotriphosphate), designated ATP alpha S-A and ATP alpha S-B, and allow investigation of the stereochemical course of nucleotidyl transfer. We have developed a simple method based on 31P nuclear magnetic resonance spectroscopy for determining the stereochemical course of these reactions, and using this method show here that the nucleotidyl transfer step in two aminoacyl-tRNA synthetases from Escherichia coli occurs with inversion of configuration at phosphorus. These observations greatly constrain the mechanistic possibilities for these enzymes, and are interpreted most simply as a direct 'in line' transfer from ATP to the amino acid.
language: eng
source:
identifier: ISSN: 0028-0836
fulltext: no_fulltext
issn:
  • 0028-0836
  • 1476-4687
  • 1476-4687
url: Link


@attributes
NO1
SEARCH_ENGINEprimo_central_multiple_fe
SEARCH_ENGINE_TYPEPrimo Central Search Engine
RANK1.4103911
LOCALfalse
PrimoNMBib
record
control
sourceidproquest_cross
recordidTN_cdi_proquest_miscellaneous_75000650
sourceformatXML
sourcesystemPC
sourcerecordid75000650
originalsourceidFETCH-LOGICAL-c230t-f4fb2bb31440a35191522543850cbc1d22a932d586ef2b53352234d3aedde6c80
addsrcrecordideNptkEtLxDAQx4P4WlfBDyCSk3jpmkfTdo_L4gsWBVmPUtJ0SiNtsyap0G9vtOsexMs8mP_8mPkjdE7JjBKe3bCMckYk2UMTGqdJFCdZuo8mhLAsIhlPjtGJc--EEEHT-Agd8vmcMzFBb-sasPNgwagaWq1kg5XprQNsKixb3RkslS5D8PpTem06XAy4BV-HcmgiLLsS-8EaFxr_8rTAbuh8DV46cKfooJKNg7NtnqLXu9v18iFaPd8_LherSDFOfFTFVcGKgtM4JpILOqeCMRHzTBBVKFoyJsO1pcgSqFghOA9jHpdcQllCojIyRVcjd2PNRw_O5612CppGdmB6l6cifJ6EMEXXo1CFg52FKt9Y3Uo75JTk30bmv0YG6cWW2RctlDvh6FwYz_6QlPY__ngrdfMf73Jc6KTvLex4O8EX3dyGdg
sourcetypeAggregation Database
isCDItrue
recordtypearticle
pqid75000650
display
typearticle
titleThe stereochemical course of amino acid activation by methionyl- and tyrosyl-tRNA synthetases
creatorLangdon, Simon P ; Lowe, Gordon
creatorcontribLangdon, Simon P ; Lowe, Gordon
descriptionStereochemical analysis has long been recognised as a powerful tool for elucidating the mechanisms of chemical and enzyme-catalysed reactions. Although much is known about the stereochemical course of reactions at saturated carbon, phosphate and thiophosphate esters whose ligands to phosphorus are also tetrahedrally disposed, are capable in principle of revealing sterochemical information about events at the active site of enzymes that transform such substrates. Nucleotidyl transferases are a group of enzymes which in general selectively use one of the diastereoisomers of a nucleoside 5'(1-thiotriphosphate), such as isomers A and B of adenosine 5'(1-thiotriphosphate), designated ATP alpha S-A and ATP alpha S-B, and allow investigation of the stereochemical course of nucleotidyl transfer. We have developed a simple method based on 31P nuclear magnetic resonance spectroscopy for determining the stereochemical course of these reactions, and using this method show here that the nucleotidyl transfer step in two aminoacyl-tRNA synthetases from Escherichia coli occurs with inversion of configuration at phosphorus. These observations greatly constrain the mechanistic possibilities for these enzymes, and are interpreted most simply as a direct 'in line' transfer from ATP to the amino acid.
identifier
0ISSN: 0028-0836
1ISSN: 1476-4687
2EISSN: 1476-4687
3DOI: 10.1038/281320a0
4PMID: 399325
languageeng
publisherEngland
subjectAmino Acyl-tRNA Synthetases - metabolism ; Binding Sites ; Catalysis ; Escherichia coli - enzymology ; Methionine-tRNA Ligase - metabolism ; Phosphates ; Stereoisomerism ; Transfer RNA Aminoacylation ; Tyrosine-tRNA Ligase - metabolism
ispartofNature (London), 1979-09-27, Vol.281 (5729), p.320-321
lds50peer_reviewed
citedbyFETCH-LOGICAL-c230t-f4fb2bb31440a35191522543850cbc1d22a932d586ef2b53352234d3aedde6c80
citesFETCH-LOGICAL-c230t-f4fb2bb31440a35191522543850cbc1d22a932d586ef2b53352234d3aedde6c80
links
openurl$$Topenurl_article
thumbnail$$Usyndetics_thumb_exl
backlink$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/399325$$D View this record in MEDLINE/PubMed
search
creatorcontrib
0Langdon, Simon P
1Lowe, Gordon
title
0The stereochemical course of amino acid activation by methionyl- and tyrosyl-tRNA synthetases
1Nature (London)
addtitleNature
descriptionStereochemical analysis has long been recognised as a powerful tool for elucidating the mechanisms of chemical and enzyme-catalysed reactions. Although much is known about the stereochemical course of reactions at saturated carbon, phosphate and thiophosphate esters whose ligands to phosphorus are also tetrahedrally disposed, are capable in principle of revealing sterochemical information about events at the active site of enzymes that transform such substrates. Nucleotidyl transferases are a group of enzymes which in general selectively use one of the diastereoisomers of a nucleoside 5'(1-thiotriphosphate), such as isomers A and B of adenosine 5'(1-thiotriphosphate), designated ATP alpha S-A and ATP alpha S-B, and allow investigation of the stereochemical course of nucleotidyl transfer. We have developed a simple method based on 31P nuclear magnetic resonance spectroscopy for determining the stereochemical course of these reactions, and using this method show here that the nucleotidyl transfer step in two aminoacyl-tRNA synthetases from Escherichia coli occurs with inversion of configuration at phosphorus. These observations greatly constrain the mechanistic possibilities for these enzymes, and are interpreted most simply as a direct 'in line' transfer from ATP to the amino acid.
subject
0Amino Acyl-tRNA Synthetases - metabolism
1Binding Sites
2Catalysis
3Escherichia coli - enzymology
4Methionine-tRNA Ligase - metabolism
5Phosphates
6Stereoisomerism
7Transfer RNA Aminoacylation
8Tyrosine-tRNA Ligase - metabolism
issn
00028-0836
11476-4687
21476-4687
fulltextfalse
rsrctypearticle
creationdate1979
recordtypearticle
recordideNptkEtLxDAQx4P4WlfBDyCSk3jpmkfTdo_L4gsWBVmPUtJ0SiNtsyap0G9vtOsexMs8mP_8mPkjdE7JjBKe3bCMckYk2UMTGqdJFCdZuo8mhLAsIhlPjtGJc--EEEHT-Agd8vmcMzFBb-sasPNgwagaWq1kg5XprQNsKixb3RkslS5D8PpTem06XAy4BV-HcmgiLLsS-8EaFxr_8rTAbuh8DV46cKfooJKNg7NtnqLXu9v18iFaPd8_LherSDFOfFTFVcGKgtM4JpILOqeCMRHzTBBVKFoyJsO1pcgSqFghOA9jHpdcQllCojIyRVcjd2PNRw_O5612CppGdmB6l6cifJ6EMEXXo1CFg52FKt9Y3Uo75JTk30bmv0YG6cWW2RctlDvh6FwYz_6QlPY__ngrdfMf73Jc6KTvLex4O8EX3dyGdg
startdate19790927
enddate19790927
creator
0Langdon, Simon P
1Lowe, Gordon
scope
0CGR
1CUY
2CVF
3ECM
4EIF
5NPM
6AAYXX
7CITATION
87X8
sort
creationdate19790927
titleThe stereochemical course of amino acid activation by methionyl- and tyrosyl-tRNA synthetases
authorLangdon, Simon P ; Lowe, Gordon
facets
frbrtype5
frbrgroupidcdi_FETCH-LOGICAL-c230t-f4fb2bb31440a35191522543850cbc1d22a932d586ef2b53352234d3aedde6c80
rsrctypearticles
prefilterarticles
languageeng
creationdate1979
topic
0Amino Acyl-tRNA Synthetases - metabolism
1Binding Sites
2Catalysis
3Escherichia coli - enzymology
4Methionine-tRNA Ligase - metabolism
5Phosphates
6Stereoisomerism
7Transfer RNA Aminoacylation
8Tyrosine-tRNA Ligase - metabolism
toplevelpeer_reviewed
creatorcontrib
0Langdon, Simon P
1Lowe, Gordon
collection
0Medline
1MEDLINE
2MEDLINE (Ovid)
3MEDLINE
4MEDLINE
5PubMed
6CrossRef
7MEDLINE - Academic
jtitleNature (London)
delivery
delcategoryRemote Search Resource
fulltextno_fulltext
addata
au
0Langdon, Simon P
1Lowe, Gordon
formatjournal
genrearticle
ristypeJOUR
atitleThe stereochemical course of amino acid activation by methionyl- and tyrosyl-tRNA synthetases
jtitleNature (London)
addtitleNature
date1979-09-27
risdate1979
volume281
issue5729
spage320
epage321
pages320-321
issn
00028-0836
11476-4687
eissn1476-4687
abstractStereochemical analysis has long been recognised as a powerful tool for elucidating the mechanisms of chemical and enzyme-catalysed reactions. Although much is known about the stereochemical course of reactions at saturated carbon, phosphate and thiophosphate esters whose ligands to phosphorus are also tetrahedrally disposed, are capable in principle of revealing sterochemical information about events at the active site of enzymes that transform such substrates. Nucleotidyl transferases are a group of enzymes which in general selectively use one of the diastereoisomers of a nucleoside 5'(1-thiotriphosphate), such as isomers A and B of adenosine 5'(1-thiotriphosphate), designated ATP alpha S-A and ATP alpha S-B, and allow investigation of the stereochemical course of nucleotidyl transfer. We have developed a simple method based on 31P nuclear magnetic resonance spectroscopy for determining the stereochemical course of these reactions, and using this method show here that the nucleotidyl transfer step in two aminoacyl-tRNA synthetases from Escherichia coli occurs with inversion of configuration at phosphorus. These observations greatly constrain the mechanistic possibilities for these enzymes, and are interpreted most simply as a direct 'in line' transfer from ATP to the amino acid.
copEngland
pmid399325
doi10.1038/281320a0