Linked Life Data

8448129

Source:http://linkedlifedata.com/resource/pubmed/id/8448129

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
1993-4-13
pubmed:abstractText
Stopped-flow kinetic studies of the reductive half-reaction of methylamine dehydrogenase from Paracoccus denitrificans yielded kinetic constants for the reversible formation of the imine intermediate formed between the substrate and the tryptophan tryptophylquinone (TTQ) prosthetic group and for the hydrogen abstraction step which occurs concomitantly with TTQ reduction. When CD3NH2 was used as a substrate, deuterium kinetic isotope effects of 4.2 and 3.8, respectively, were measured for the rate constants that correspond to the formation and dissociation of the iminoquinone intermediate. A deuterium kinetic isotope effect of 17.2 was measured for the hydrogen abstraction step. The maximum deuterium kinetic isotope effect which was measured in steady-state kinetic experiments was 3.0. These data are discussed in relation to the reaction mechanism of methylamine dehydrogenase and the similar large deuterium kinetic isotope effect for hydrogen abstraction which has been observed for another quinoprotein, plasma amine oxidase.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
16
pubmed:volume
32
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2725-9
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Deuterium kinetic isotope effect and stopped-flow kinetic studies of the quinoprotein methylamine dehydrogenase.
pubmed:affiliation
Department of Biochemistry, University of Mississippi Medical Center, Jackson 39216-4505.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.