Molecular dynamics simulations of active site mutants of rat liver arginase

Molecular dynamics simulations of active site mutants of rat liver arginase

By using molecular dynamics (MD) simulations and crystallographic data for rat liver arginase, the substrate positions in the active sites of native and mutant forms of the enzyme, were compared and correlated with known kinetic consequences of mutations. The mutants compared were His 141<IMG SRC...

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Autores principales: Canales,Mauricio, Westermeyer,Linda, Carvajal,Nelson
Lenguaje:English
Publicado: Pontificia Universidad Católica de Valparaíso 2001
Acceso en línea:http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582001000300010
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spelling oai:scielo:S0717-345820010003000102003-08-18Molecular dynamics simulations of active site mutants of rat liver arginaseCanales,MauricioWestermeyer,LindaCarvajal,Nelson By using molecular dynamics (MD) simulations and crystallographic data for rat liver arginase, the substrate positions in the active sites of native and mutant forms of the enzyme, were compared and correlated with known kinetic consequences of mutations. The mutants compared were His 141<IMG SRC="/content/vol4/issue3/full/6/flecha2.gif" WIDTH=12 HEIGHT=9>Phe and His 141<IMG SRC="/content/vol4/issue3/full/6/flecha2.gif" WIDTH=12 HEIGHT=9>Asn. The simulations show that mutation His141<IMG SRC="/content/vol4/issue3/full/6/flecha2.gif" WIDTH=12 HEIGHT=9>Asn gives the greatest divergence from the atomic coordinates, when compared with the control native enzyme. The mutant Asp128<IMG SRC="/content/vol4/issue3/full/6/flecha2.gif" WIDTH=12 HEIGHT=9>Asn does not show a change in atomic coordinates in the substrate, in agreement with the concept that a change in the metal coordination is responsible for the loss of catalytic activity in this mutant. Results obtained agree with reported kinetic consequences of mutations in arginase.info:eu-repo/semantics/openAccessPontificia Universidad Católica de ValparaísoElectronic Journal of Biotechnology v.4 n.3 20012001-12-01text/htmlhttp://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582001000300010en
institution Scielo Chile
collection Scielo Chile
language English
description By using molecular dynamics (MD) simulations and crystallographic data for rat liver arginase, the substrate positions in the active sites of native and mutant forms of the enzyme, were compared and correlated with known kinetic consequences of mutations. The mutants compared were His 141<IMG SRC="/content/vol4/issue3/full/6/flecha2.gif" WIDTH=12 HEIGHT=9>Phe and His 141<IMG SRC="/content/vol4/issue3/full/6/flecha2.gif" WIDTH=12 HEIGHT=9>Asn. The simulations show that mutation His141<IMG SRC="/content/vol4/issue3/full/6/flecha2.gif" WIDTH=12 HEIGHT=9>Asn gives the greatest divergence from the atomic coordinates, when compared with the control native enzyme. The mutant Asp128<IMG SRC="/content/vol4/issue3/full/6/flecha2.gif" WIDTH=12 HEIGHT=9>Asn does not show a change in atomic coordinates in the substrate, in agreement with the concept that a change in the metal coordination is responsible for the loss of catalytic activity in this mutant. Results obtained agree with reported kinetic consequences of mutations in arginase.
author Canales,Mauricio
Westermeyer,Linda
Carvajal,Nelson
spellingShingle Canales,Mauricio
Westermeyer,Linda
Carvajal,Nelson
Molecular dynamics simulations of active site mutants of rat liver arginase
author_facet Canales,Mauricio
Westermeyer,Linda
Carvajal,Nelson
author_sort Canales,Mauricio
title Molecular dynamics simulations of active site mutants of rat liver arginase
title_short Molecular dynamics simulations of active site mutants of rat liver arginase
title_full Molecular dynamics simulations of active site mutants of rat liver arginase
title_fullStr Molecular dynamics simulations of active site mutants of rat liver arginase
title_full_unstemmed Molecular dynamics simulations of active site mutants of rat liver arginase
title_sort molecular dynamics simulations of active site mutants of rat liver arginase
publisher Pontificia Universidad Católica de Valparaíso
publishDate 2001
url http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582001000300010
work_keys_str_mv AT canalesmauricio moleculardynamicssimulationsofactivesitemutantsofratliverarginase
AT westermeyerlinda moleculardynamicssimulationsofactivesitemutantsofratliverarginase
AT carvajalnelson moleculardynamicssimulationsofactivesitemutantsofratliverarginase
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