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Reaction mechanism of glutamate carboxypeptidase II revealed by mutagenesis, X-ray crystallography and computational methods

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F09%3A10001266" target="_blank" >RIV/00216208:11310/09:10001266 - isvavai.cz</a>

  • Alternative codes found

    RIV/61388963:_____/09:00326498

  • Result on the web

  • DOI - Digital Object Identifier

Alternative languages

  • Result language

    angličtina

  • Original language name

    Reaction mechanism of glutamate carboxypeptidase II revealed by mutagenesis, X-ray crystallography and computational methods

  • Original language description

    The peptide hydrolysis by GCPII was investigated in detail by carrying out the kinetic analysis of GCPII(E424A) using N-Ac-Asp-Glu as substrate. The crystal structure of GCPII(E424A) in complex with N-Ac-Asp-Glu was determined at 1.70 A resolution. The experimental data were then complemented by the QM/MM calculations which provided detailed information concerning the GCPII reaction mechanism.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    CE - Biochemistry

  • OECD FORD branch

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)

Others

  • Publication year

    2009

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Biochemistry

  • ISSN

    0006-2960

  • e-ISSN

  • Volume of the periodical

    48

  • Issue of the periodical within the volume

    19

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    13

  • Pages from-to

  • UT code for WoS article

    000266047400012

  • EID of the result in the Scopus database