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Electronic Journal of Biotechnology
Universidad Católica de Valparaíso
ISSN: 0717-3458
Vol. 4, No. 3, 2001, pp. 154-159
Bioline Code: ej01028
Full paper language: English
Document type: Research Article
Document available free of charge

Electronic Journal of Biotechnology, Vol. 4, No. 3, 2001, pp. 154-159

 en Molecular dynamics simulations of active site mutants of rat liver arginase
Canales, Mauricio; Westermeyer, Linda & Carvajal, 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→Phe and His 141→Asn. The simulations show that mutation His141→Asn gives the greatest divergence from the atomic coordinates, when compared with the control native enzyme. The mutant Asp128→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.

arginase, arginine, molecular dynamics, optimization

© 2001 by Universidad Católica de Valparaíso -- Chile
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