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.
| Original language | English |
|---|---|
| Pages (from-to) | 249-254 |
| Number of pages | 6 |
| Journal | Chemical Physics Letters |
| Volume | 372 |
| Issue number | 1-2 |
| DOIs | |
| Publication status | Published - Apr 22 2003 |
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ASJC Scopus subject areas
- Physical and Theoretical Chemistry
- Spectroscopy
- Atomic and Molecular Physics, and Optics
Cite this
The influence of metal ions on the substrate binding pocket of human alcohol dehydrogenase β2β2 by molecular modeling. / Liu, Hsuan Liang; Ho, Yih; Hsu, Chia Ming.
In: Chemical Physics Letters, Vol. 372, No. 1-2, 22.04.2003, p. 249-254.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - The influence of metal ions on the substrate binding pocket of human alcohol dehydrogenase β2β2 by molecular modeling
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 - http://www.scopus.com/inward/record.url?scp=0037461204&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0037461204&partnerID=8YFLogxK
U2 - 10.1016/S0009-2614(03)00411-1
DO - 10.1016/S0009-2614(03)00411-1
M3 - Article
AN - SCOPUS:0037461204
VL - 372
SP - 249
EP - 254
JO - Chemical Physics Letters
JF - Chemical Physics Letters
SN - 0009-2614
IS - 1-2
ER -