Linked Life Data

340460

Source:http://linkedlifedata.com/resource/pubmed/id/340460

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1978-3-21
pubmed:abstractText
A simple purification for the membrane-associated, flavin-linked, glycerol-3-phosphate dehydrogenase of Escherichia coli has been developed which yields homogeneous enzyme in a detergent-solubilized state. 1. The dissociated form of the enzyme has a molecular weight of 58,000 and contains 0.5 mol of FAD/mol of protein monomer. 2. The solubilized enzyme-catalyzed reaction has a pH profile and temperature dependence similar to that observed for the membrane-bound enzyme. 3. The most efficient electron acceptor is potassium ferricyanide but phenazine methosulfate, methylene blue, menadione, and dichlorophenolindophenol can also be utilized. 4. The reaction is competitively inhibited by dihydroxyacetone phosphate, phosphoenolpyruvate, phosphoglycolic acid, glyceraldehyde-3-phosphate, and D-2- and D-3-phosphoglyceric acid. 5. The activity of the enzyme is regulated in a complex manner by ATP and GTP. 6. Detergent-depleted enzyme can be functionally reconstituted with Escherichia coli membrane vesicles to support glycerol-3-phosphate-dependent active transport of L-proline. 7. Detergent-depleted enzyme requires exogenous phospholipid or nondenaturing detergent for electron transfer activity.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
253
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
783-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1978
pubmed:articleTitle
Chemical and functional properties of the native and reconstituted forms of the membrane-bound, aerobic glycerol-3-phosphate dehydrogenase of Escherichia coli.
pubmed:publicationType
Journal Article, Comparative Study