Kinetics of irreversible inhibition of yeast alcohol dehydrogenase during modification by 4,4'-dithiodipyridine

Si Yang Zheng; Dong Xu; Hong Rui Wang; Jian Li; Hai Meng Zhou

doi:10.1016/S0141-8130(97)00030-5

Kinetics of irreversible inhibition of yeast alcohol dehydrogenase during modification by 4,4'-dithiodipyridine

Si Yang Zheng, Dong Xu, Hong Rui Wang, Jian Li, Hai Meng Zhou

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

6 Scopus citations

Abstract

The course of inactivation of yeast alcohol dehydrogenase (YADH) using 4,4'-dithiodipyridine (DSDP) has been studied in this paper. The results show that the reaction mechanism between DSDP and YADH is a competitive, complexing inhibition. The microscopic constants for the inactivation of the free enzyme and the enzyme-substrate complex were determined. The presence of the substrate NAD⁺ offers strong protection for this enzyme against inactivation by DSDP. The above results suggest that two Cys residues are essential for activity and are situated at the active site. These essential Cys residues should be Cys-46 and Cys-174 which are ligands to the catalytic zinc ion. Another Cys residue, which can be modified by DSDP, is non-essential for activity of the enzyme.

Original language	English (US)
Pages (from-to)	307-313
Number of pages	7
Journal	International Journal of Biological Macromolecules
Volume	20
Issue number	4
DOIs	https://doi.org/10.1016/S0141-8130(97)00030-5
State	Published - Jul 1997

All Science Journal Classification (ASJC) codes

Structural Biology
Biochemistry
Molecular Biology

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10.1016/S0141-8130(97)00030-5

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@article{590edba87bd54661a751b67d83126c33,

title = "Kinetics of irreversible inhibition of yeast alcohol dehydrogenase during modification by 4,4'-dithiodipyridine",

abstract = "The course of inactivation of yeast alcohol dehydrogenase (YADH) using 4,4'-dithiodipyridine (DSDP) has been studied in this paper. The results show that the reaction mechanism between DSDP and YADH is a competitive, complexing inhibition. The microscopic constants for the inactivation of the free enzyme and the enzyme-substrate complex were determined. The presence of the substrate NAD+ offers strong protection for this enzyme against inactivation by DSDP. The above results suggest that two Cys residues are essential for activity and are situated at the active site. These essential Cys residues should be Cys-46 and Cys-174 which are ligands to the catalytic zinc ion. Another Cys residue, which can be modified by DSDP, is non-essential for activity of the enzyme.",

author = "Zheng, {Si Yang} and Dong Xu and Wang, {Hong Rui} and Jian Li and Zhou, {Hai Meng}",

note = "Funding Information: The present investigation was partly supported by the Pandeng Project of the China Commission for Science and Technology.",

year = "1997",

month = jul,

doi = "10.1016/S0141-8130(97)00030-5",

language = "English (US)",

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journal = "International Journal of Biological Macromolecules",

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T1 - Kinetics of irreversible inhibition of yeast alcohol dehydrogenase during modification by 4,4'-dithiodipyridine

AU - Zheng, Si Yang

AU - Xu, Dong

AU - Wang, Hong Rui

AU - Li, Jian

AU - Zhou, Hai Meng

N1 - Funding Information: The present investigation was partly supported by the Pandeng Project of the China Commission for Science and Technology.

PY - 1997/7

Y1 - 1997/7

N2 - The course of inactivation of yeast alcohol dehydrogenase (YADH) using 4,4'-dithiodipyridine (DSDP) has been studied in this paper. The results show that the reaction mechanism between DSDP and YADH is a competitive, complexing inhibition. The microscopic constants for the inactivation of the free enzyme and the enzyme-substrate complex were determined. The presence of the substrate NAD+ offers strong protection for this enzyme against inactivation by DSDP. The above results suggest that two Cys residues are essential for activity and are situated at the active site. These essential Cys residues should be Cys-46 and Cys-174 which are ligands to the catalytic zinc ion. Another Cys residue, which can be modified by DSDP, is non-essential for activity of the enzyme.

AB - The course of inactivation of yeast alcohol dehydrogenase (YADH) using 4,4'-dithiodipyridine (DSDP) has been studied in this paper. The results show that the reaction mechanism between DSDP and YADH is a competitive, complexing inhibition. The microscopic constants for the inactivation of the free enzyme and the enzyme-substrate complex were determined. The presence of the substrate NAD+ offers strong protection for this enzyme against inactivation by DSDP. The above results suggest that two Cys residues are essential for activity and are situated at the active site. These essential Cys residues should be Cys-46 and Cys-174 which are ligands to the catalytic zinc ion. Another Cys residue, which can be modified by DSDP, is non-essential for activity of the enzyme.

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SN - 0141-8130

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JO - International Journal of Biological Macromolecules

JF - International Journal of Biological Macromolecules

IS - 4

ER -

Kinetics of irreversible inhibition of yeast alcohol dehydrogenase during modification by 4,4'-dithiodipyridine

Abstract

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