Linked Life Data

3651440

Source:http://linkedlifedata.com/resource/pubmed/id/3651440

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
13
pubmed:dateCreated
1987-11-16
pubmed:abstractText
Steady-state kinetic studies for the reaction of the flavocytochrome p-cresol methylhydroxylase with the reducing substrates (S) p-cresol, 4-ethylphenol, and their corresponding alpha-deuteriated analogues are presented. The results from these experiments and those from studies involving various reoxidizing substrates support the proposed apparent ping-pong mechanism. With phenazine methosulfate (PMS) as the reoxidant for studies at pH 7.6 and 6 or 25 degrees C, the isotope effects on kcat are lower than the intrinsic isotope effect. The values for D(kcat/KS) are equal to the intrinsic effect for p-cresol at 25 degrees C and for 4-ethylphenol at both 6 and 25 degrees C. However, the value for this steady-state parameter at 6 degrees C for p-cresol is lower than the intrinsic effect. The values for D(kcat/KPMS) are nearly equal to 1.0 under all conditions. In contrast, the steady-state kinetic analysis for the isolated flavoprotein subunit of p-cresol methylhydroxylase involving p-cresol and PMS as substrates indicates that a random-binding mechanism is operating. Additionally, several of the steady-state parameters yield values for the apparent intrinsic isotope effect for the flavoprotein. The results of stopped-flow kinetic studies are also reported. At pH 7.6 the intrinsic isotope effect (Dk2) for the reduction of the enzyme by 4-ethylphenol is 4.8-5.0 at 25 degrees C and 4.0 at 6 degrees C. This technique yields a value for Dk2 of 7.05 at 6 degrees C and pH 7.6 for p-cresol.(ABSTRACT TRUNCATED AT 250 WORDS)
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
26
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4107-17
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
Steady-state and stopped-flow kinetic measurements of the primary deuterium isotope effect in the reaction catalyzed by p-cresol methylhydroxylase.
pubmed:affiliation
Molecular Biology Division, Veterans Administration Medical Center, San Francisco, California 94121.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.