Linked Life Data

2015291

Source:http://linkedlifedata.com/resource/pubmed/id/2015291

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1991-5-23
pubmed:abstractText
Steady-state kinetic parameters of the human kidney aldehyde reductase-catalyzed reduction of para-substituted benzaldehydes by 3-acetyl pyridine dinucleotide phosphate (3-APADPH) were determined. The kcat of aldehyde reduction by 3-APADPH was 2- to 4-fold lower than by NADPH. The dissociation constant of 3-APADPH from the enzyme-coenzyme complex was higher (77 microM) than that of NADPH (5.3 microM). Primary deuterium kinetic isotope effects on both kcat and kcat/Km for para-substituted benzaldehyde reduction by 3-APADPH (with the exception of para-carboxybenzaldehyde) were equal and on average 2.82 +/- 0.21, suggesting that these reactions follow a rapid equilibrium-ordered reaction scheme in which the hydride transfer step is rate-limiting. Multiple regression analysis of the data suggests that benzaldehyde reduction depends upon electronic substituent effects, characterized by a rho value of 0.5. These data are consistent with a transition state in which the charge on the aldehyde carbonyl increases relative to the charge on this group in the ground state. A positive deviation of para-carboxybenzaldehyde from the linear correlation between other benzaldehydes and the substituent constant sigma + suggests a specific interaction of the carboxyl substituent of the substrate with the enzyme.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
8
pubmed:volume
1077
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
180-6
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Structure-activity correlations in human kidney aldehyde reductase-catalyzed reduction of para-substituted benzaldehyde by 3-acetyl pyridine adenine dinucleotide phosphate.
pubmed:affiliation
Department of Human Biological Chemistry and Genetics, University of Texas Medical Branch, Galveston 77550.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.