Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1988-6-2
pubmed:abstractText
The kinetic mechanism of two major monomeric 17 beta-hydroxysteroid dehydrogenases from mouse liver cytosol was studied at pH 7 in both directions with NADP(H) and three steroid substrates: testosterone, 5 beta-androstane-3 alpha, 17 17 beta-diol, and estradiol-17 beta. In each case the reaction mechanism of the two enzymes was sequential, and inhibition patterns by-products and dead-end inhibitors were consisted with an ordered bi bi mechanism with the coenzyme binding to the free enzyme, although there was difference in affinity and maximum velocity for the steroidal substrates between the two enzymes. Binding studies of the coenzyme and substrate indicate the binding of coenzyme to the free enzyme, in which 1 mol of NADPH binds to 1 mol of each monomeric enzyme. The 4-pro-R-hydrogen atom of NADPH was transferred to the alpha-face of the steroid molecule by the two enzymes.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-924X
pubmed:author
pubmed:issnType
Print
pubmed:volume
102
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1585-92
pubmed:dateRevised
2007-12-19
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
Kinetic and stereochemical studies on reaction mechanism of mouse liver 17 beta-hydroxysteroid dehydrogenases.
pubmed:affiliation
Department of Biochemistry, Gifu Pharmaceutical University.
pubmed:publicationType
Journal Article, Comparative Study