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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1-2
|
| pubmed:dateCreated |
1988-2-17
|
| pubmed:abstractText |
We have elaborated a kinetic method which allows us to evaluate whether a Michaelis-Menten-type enzyme acting on two different substrates has one or two active sites. This method has been used with the rat liver L-threonine dehydratase, which catalyzes the dehydrative deamination of both serine and threonine. The experimental data can be fitted to the theoretical plot obtained for the case of a single active site.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Dec
|
| pubmed:issn |
0014-2956
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
30
|
| pubmed:volume |
170
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
179-83
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| pubmed:dateRevised |
2007-7-23
|
| pubmed:meshHeading |
pubmed-meshheading:3121321-Animals,
pubmed-meshheading:3121321-Binding Sites,
pubmed-meshheading:3121321-Kinetics,
pubmed-meshheading:3121321-Liver,
pubmed-meshheading:3121321-Male,
pubmed-meshheading:3121321-Mathematics,
pubmed-meshheading:3121321-Rats,
pubmed-meshheading:3121321-Rats, Inbred Strains,
pubmed-meshheading:3121321-Serine,
pubmed-meshheading:3121321-Substrate Specificity,
pubmed-meshheading:3121321-Threonine,
pubmed-meshheading:3121321-Threonine Dehydratase
|
| pubmed:year |
1987
|
| pubmed:articleTitle |
A kinetic method for distinguishing whether an enzyme has one or two active sites for two different substrates. Rat liver L-threonine dehydratase has a single active site for threonine and serine.
|
| pubmed:affiliation |
Institute of Enzymology, Hungarian Academy of Sciences, Budapest.
|
| pubmed:publicationType |
Journal Article
|