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

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

Research output: Contribution to journalArticle

7 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)307-313
Number of pages7
JournalInternational Journal of Biological Macromolecules
Volume20
Issue number4
DOIs
StatePublished - Jul 1 1997

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Alcohol Dehydrogenase
Kinetics
Enzymes
Substrates
NAD
Zinc
Catalytic Domain
Ions
Ligands
4,4'-dipyridyl disulfide

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Biochemistry
  • Molecular Biology

Cite this

Zheng, Siyang ; Xu, Dong ; Wang, Hong Rui ; Li, Jian ; Zhou, Hai Meng. / Kinetics of irreversible inhibition of yeast alcohol dehydrogenase during modification by 4,4'-dithiodipyridine. In: International Journal of Biological Macromolecules. 1997 ; Vol. 20, No. 4. pp. 307-313.
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Kinetics of irreversible inhibition of yeast alcohol dehydrogenase during modification by 4,4'-dithiodipyridine. / Zheng, Siyang; Xu, Dong; Wang, Hong Rui; Li, Jian; Zhou, Hai Meng.

In: International Journal of Biological Macromolecules, Vol. 20, No. 4, 01.07.1997, p. 307-313.

Research output: Contribution to journalArticle

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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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