Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1982-10-29
pubmed:abstractText
In human liver, the oxidation of corticosteroids to 20-hydroxy-21-oic acids proceeds via the formation and oxidation of aldol (20-hydroxy-21-aldehyde) intermediates. Human liver aldehyde dehydrogenases E1 and E2, which we have previously purified to homogeneity, catalyzed the oxidation of the aldol isomer of cortisol (isocortisol) or of 11-deoxycorticosterone (isoDOC) by E1 and E2 respectively, were identified by the criteria of chromatographic mobility, derivatization, and reverse isotope dilution of 4-14C labeled acid end products. Both enzymes showed broad substrate specificity and oxidized both 17-hydroxy and 17-deoxy steroids, though at widely varying rates. Kinetic analysis of the course of oxidation of isocortisol and isoDOC by NAD+ gave intersecting initial velocity plots that conform with a sequential mechanism. The inhibition patterns for both enzymes with thionicotinamide adenine dinucleotide or chloral hydrate were consistent with random sequential behavior.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0022-4731
pubmed:author
pubmed:issnType
Print
pubmed:volume
17
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
41-9
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
Oxidation of the 17-aldol (20 beta hydroxy-21-aldehyde) intermediate of corticosteroid metabolism to hydroxy acids by homogeneous human liver aldehyde dehydrogenases.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.