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.
journal_name
Int J Biol Macromoljournal_title
International journal of biological macromoleculesauthors
Zheng SY,Xu D,Wang HR,Li J,Zhou HMdoi
10.1016/s0141-8130(97)00030-5subject
Has Abstractpub_date
1997-07-01 00:00:00pages
307-13issue
4eissn
0141-8130issn
1879-0003pii
S0141-8130(97)00030-5journal_volume
20pub_type
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