Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
7
|
| pubmed:dateCreated |
1983-11-23
|
| pubmed:abstractText |
The substrate specificity of NAD-dependent formate dehydrogenase from the methylotrophic bacterium Achromobacter parvulus T1 was studied. The kinetic mechanism of S-formyl glutathione oxidation was determined. The initial velocity studies and inhibition analysis were carried out. It was shown that the kinetic mechanism for the enzyme with S-formyl glutathione as a substrate is similar to that with formate and is rapid-equilibrium random. Using independent methods, it was found that formate dehydrogenase forms a binary complex with S-formyl glutathione (Kd = 2.5 mM).
|
| pubmed:language |
rus
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jul
|
| pubmed:issn |
0320-9725
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
48
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
1172-80
|
| pubmed:dateRevised |
2007-7-23
|
| pubmed:meshHeading |
pubmed-meshheading:6615926-Alcaligenes,
pubmed-meshheading:6615926-Aldehyde Oxidoreductases,
pubmed-meshheading:6615926-Formate Dehydrogenases,
pubmed-meshheading:6615926-Glutathione,
pubmed-meshheading:6615926-Kinetics,
pubmed-meshheading:6615926-Mathematics,
pubmed-meshheading:6615926-Oxidation-Reduction,
pubmed-meshheading:6615926-Substrate Specificity
|
| pubmed:year |
1983
|
| pubmed:articleTitle |
[Bacterial formate dehydrogenase. Substrate specificity and kinetic mechanism of S-formyl glutathione oxidation].
|
| pubmed:publicationType |
Journal Article,
English Abstract
|