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The structural feature of S1′ subsite of carboxypeptidase A

  • Dong H. Kim
  • , Yong Soon Shin
  • , Kyung Bo Kim

Producción científica: Articlerevisión exhaustiva

8 Citas (Scopus)

Resumen

The study on the structural feature of carboxypeptidase A using transition state analog inhibitors suggests that the principal substrate recognition subsite of the enzyme is a pocket-shaped cavity having a rectangular opening with effective dimensions of 3.5 Å × 7.1 Å. The principal substrate recognition subsite (S1 ′ subsite) of Carboxypeptidase A is a pocket-shaped cavity having a rectangular opening with effective dimensions of 3.5 Å × 7.1 Å.

Idioma originalEnglish
Páginas (desde-hasta)317-322
Número de páginas6
PublicaciónBioorganic and Medicinal Chemistry Letters
Volumen1
N.º6
DOI
EstadoPublished - 1991

Nota bibliográfica

Funding Information:
AchowledgmenAt:u thors thank the Ministry of Education,R epublico f Korea for the financial supporto f this workt hrough the Basic ScienceI nstitute at POSTECH. Acknowledgemiesn ta lso duet o Prof. KwangS ooK im who provided molecular dimensions of naphthalenea nd helpful discussion.

Financiación

AchowledgmenAt:u thors thank the Ministry of Education,R epublico f Korea for the financial supporto f this workt hrough the Basic ScienceI nstitute at POSTECH. Acknowledgemiesn ta lso duet o Prof. KwangS ooK im who provided molecular dimensions of naphthalenea nd helpful discussion.

Financiadores
Ministry of Education,R epublico f Korea
Pohang University of Science and Technology

    ASJC Scopus subject areas

    • Biochemistry
    • Molecular Medicine
    • Molecular Biology
    • Pharmaceutical Science
    • Drug Discovery
    • Clinical Biochemistry
    • Organic Chemistry

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