Rate limiting steps for the esterase and dehydrogenase reaction catalyzed by horse liver aldehyde dehydrogenase

H. Weiner, J. H.J. Hu, Charles Sanny

Research output: Contribution to journalArticle

53 Scopus citations

Abstract

Horse liver aldehyde dehydrogenase, like other aldehyde dehydrogenases, is capable by hydrolyzing esters such as nitrophenyl acetate. Pre steady state and burst kinetics were performed using substrate levels of enzyme to determine whether the rate limiting step occurred prior to or after the formation of an acyl enzyme intermediate. A burst was found by both techniques for the dehydrogenase reaction, but no burst was found for the esterase reaction. These data show that the rate limiting step for the two reactions catalyzed by the enzyme differs. For dehydrogenase it occurs after the formation of the acyl intermediate, but for esterase it occurs prior to its formation.

Original languageEnglish
Pages (from-to)3853-3855
Number of pages3
JournalJournal of Biological Chemistry
Volume251
Issue number13
StatePublished - 1 Dec 1976

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