The influence of metal ions on the substrate binding pocket of human alcohol dehydrogenase β2β2 by molecular modeling

Hsuan Liang Liu; Yih Ho; Chia Ming Hsu

doi:10.1016/S0009-2614(03)00411-1

The influence of metal ions on the substrate binding pocket of human alcohol dehydrogenase β₂β₂ by molecular modeling

Hsuan Liang Liu
, Yih Ho
, Chia Ming Hsu

Department of Pharmaceutical Sciences

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

10 Citations (Scopus)

Abstract

Based on theoretical molecular modeling performed in this study, both structural and catalytic zinc ions, Zn^s and Zn^a, respectively, were shown to influence the structural integrity of the substrate binding pocket of human alcohol dehydrogenase β₂β₂ in the middle and outer regions. The replacement of both Zn^s and Zn^a with different metal ions restricts the access of bulky substrates to the bottom of the active site by narrowing the bottleneck formed between L116 and V294, whereas it does not affect substrate binding affinity since the accessible surface area of the substrate binding pocket remains more than 80% of the wild-type.

Original language	English
Pages (from-to)	249-254
Number of pages	6
Journal	Chemical Physics Letters
Volume	372
Issue number	1-2
DOIs	https://doi.org/10.1016/S0009-2614(03)00411-1
Publication status	Published - Apr 22 2003

ASJC Scopus subject areas

General Physics and Astronomy
Physical and Theoretical Chemistry

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10.1016/S0009-2614(03)00411-1

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title = "The influence of metal ions on the substrate binding pocket of human alcohol dehydrogenase β2β2 by molecular modeling",

abstract = "Based on theoretical molecular modeling performed in this study, both structural and catalytic zinc ions, Zns and Zna, respectively, were shown to influence the structural integrity of the substrate binding pocket of human alcohol dehydrogenase β2β2 in the middle and outer regions. The replacement of both Zns and Zna with different metal ions restricts the access of bulky substrates to the bottom of the active site by narrowing the bottleneck formed between L116 and V294, whereas it does not affect substrate binding affinity since the accessible surface area of the substrate binding pocket remains more than 80\% of the wild-type.",

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AU - Liu, Hsuan Liang

AU - Ho, Yih

AU - Hsu, Chia Ming

PY - 2003/4/22

Y1 - 2003/4/22

N2 - Based on theoretical molecular modeling performed in this study, both structural and catalytic zinc ions, Zns and Zna, respectively, were shown to influence the structural integrity of the substrate binding pocket of human alcohol dehydrogenase β2β2 in the middle and outer regions. The replacement of both Zns and Zna with different metal ions restricts the access of bulky substrates to the bottom of the active site by narrowing the bottleneck formed between L116 and V294, whereas it does not affect substrate binding affinity since the accessible surface area of the substrate binding pocket remains more than 80% of the wild-type.

AB - Based on theoretical molecular modeling performed in this study, both structural and catalytic zinc ions, Zns and Zna, respectively, were shown to influence the structural integrity of the substrate binding pocket of human alcohol dehydrogenase β2β2 in the middle and outer regions. The replacement of both Zns and Zna with different metal ions restricts the access of bulky substrates to the bottom of the active site by narrowing the bottleneck formed between L116 and V294, whereas it does not affect substrate binding affinity since the accessible surface area of the substrate binding pocket remains more than 80% of the wild-type.

UR - https://www.scopus.com/pages/publications/0037461204

UR - https://www.scopus.com/pages/publications/0037461204#tab=citedBy

U2 - 10.1016/S0009-2614(03)00411-1

DO - 10.1016/S0009-2614(03)00411-1

M3 - Article

AN - SCOPUS:0037461204

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VL - 372

SP - 249

EP - 254

JO - Chemical Physics Letters

JF - Chemical Physics Letters

IS - 1-2

ER -

The influence of metal ions on the substrate binding pocket of human alcohol dehydrogenase β₂β₂ by molecular modeling

Abstract

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