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

51 Citations (Scopus)

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

Fingerprint

Aldehyde Dehydrogenase
Esterases
Liver
Horses
Oxidoreductases
Enzymes
Esters
Acetates
Kinetics
Substrates

Cite this

@article{bd3c1d20cc284a549c0ac2dea41731bf,
title = "Rate limiting steps for the esterase and dehydrogenase reaction catalyzed by horse liver aldehyde dehydrogenase",
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.",
author = "H. Weiner and Hu, {J. H.J.} and Charles Sanny",
year = "1976",
month = "12",
day = "1",
language = "English",
volume = "251",
pages = "3853--3855",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "13",

}

Rate limiting steps for the esterase and dehydrogenase reaction catalyzed by horse liver aldehyde dehydrogenase. / Weiner, H.; Hu, J. H.J.; Sanny, Charles.

In: Journal of Biological Chemistry, Vol. 251, No. 13, 01.12.1976, p. 3853-3855.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Rate limiting steps for the esterase and dehydrogenase reaction catalyzed by horse liver aldehyde dehydrogenase

AU - Weiner, H.

AU - Hu, J. H.J.

AU - Sanny, Charles

PY - 1976/12/1

Y1 - 1976/12/1

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0017079051&partnerID=8YFLogxK

M3 - Article

C2 - 945270

AN - SCOPUS:0017079051

VL - 251

SP - 3853

EP - 3855

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 13

ER -