The structural feature of S1′ subsite of carboxypeptidase A

Dong H. Kim; Yong Soon Shin; Kyung Bo Kim

doi:10.1016/S0960-894X(01)80816-7

The structural feature of S₁′ subsite of carboxypeptidase A

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

Pharmaceutical Sciences

Research output: Contribution to journal › Article › peer-review

8 Scopus citations

Abstract

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.

Original language	English
Pages (from-to)	317-322
Number of pages	6
Journal	Bioorganic and Medicinal Chemistry Letters
Volume	1
Issue number	6
DOIs	https://doi.org/10.1016/S0960-894X(01)80816-7
State	Published - 1991

Bibliographical note

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.

ASJC Scopus subject areas

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

Access to Document

10.1016/S0960-894X(01)80816-7

Cite this

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title = "The structural feature of S1′ subsite of carboxypeptidase A",

abstract = "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 {\AA} × 7.1 {\AA}. 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 {\AA} × 7.1 {\AA}.",

author = "Kim, {Dong H.} and Shin, {Yong Soon} and Kim, {Kyung Bo}",

note = "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.",

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language = "English",

volume = "1",

pages = "317--322",

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T1 - The structural feature of S1′ subsite of carboxypeptidase A

AU - Kim, Dong H.

AU - Shin, Yong Soon

AU - Kim, Kyung Bo

N1 - 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.

PY - 1991

Y1 - 1991

N2 - 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.

AB - 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.

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JO - Bioorganic and Medicinal Chemistry Letters

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