Linked Life Data

6187559

Source:http://linkedlifedata.com/resource/pubmed/id/6187559

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1983-5-5
pubmed:abstractText
The naturally occurring dithiol, dihydrolipoamide (DHL), has been found to be 6-10 times as potent as the synthetic dithiol, dithiothreitol, in stimulating iodothyronine outer ring monodeiodinase activity in the rat kidney. In the presence of NADH, the oxidized form is also active in stimulating the enzymatic activity in whole homogenates and in the postnuclear and mitochondrial, but not in the microsomal fraction. The covalently bound lipoamide in the mitochondrial alpha-keto acid dehydrogenase complexes, when reduced with substrates or NADH, was, however, ineffective. The activation of the enzyme by DHL was very similar to that obtained with dithiothreitol in respect to temperature dependence and inhibition by propylthiouracil and by dicoumarol, suggesting that these thiols activate the same enzyme through similar mechanisms. The higher potency of DHL cannot be explained on the basis of its greater lipophilicity or relatively proximal dithiol structure. The occurrence of DHL in mitochondria raises the possibility of a role as a thiol cofactor in enzymatic outer ring deiodination of T4 or rT3, although attempts to stimulate deiodination in mitochondrial preparations by reducing endogenous bound lipoamide were unsuccessful.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0013-7227
pubmed:author
pubmed:issnType
Print
pubmed:volume
112
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1180-7
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1983
pubmed:articleTitle
Stimulation of iodothyronine outer ring monodeiodinase by dihydrolipoamide.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.