Please use this identifier to cite or link to this item: https://open.uns.ac.rs/handle/123456789/13943
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dc.contributor.authorTrivić S.en
dc.contributor.authorLeskovac V.en
dc.date.accessioned2020-03-03T14:54:19Z-
dc.date.available2020-03-03T14:54:19Z-
dc.date.issued1999-01-01en
dc.identifier.issn10399712en
dc.identifier.urihttps://open.uns.ac.rs/handle/123456789/13943-
dc.description.abstractIn the present work, we have determined the steady-state kinetic constants for yeast alcohol dehydrogenase-catalyzed oxidation of allyl alcohol (H2C=CH.CH2OH) and ethylene glycol (HOCH2.CH2OH) with NAD+, at pH 8.0; also, a kinetic mechanism for the former reaction was determined at the same pH. In addition, it was found that acrolein is a potent inhibitor of yeast alcohol dehydrogenase.en
dc.relation.ispartofBiochemistry and Molecular Biology Internationalen
dc.titleNovel substrates of yeast alcohol dehydrogenase - 4. Allyl alcohol and ethylene glycolen
dc.typeJournal/Magazine Articleen
dc.identifier.pmid47en
dc.identifier.scopus2-s2.0-0033064633en
dc.identifier.urlhttps://api.elsevier.com/content/abstract/scopus_id/0033064633en
dc.relation.lastpage8en
dc.relation.firstpage1en
dc.relation.issue1en
dc.relation.volume47en
item.fulltextNo Fulltext-
item.grantfulltextnone-
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