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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
|
| pubmed:dateCreated |
1981-6-23
|
| pubmed:abstractText |
The binding of substrate analogues including potential alternative substrates, to glutamate synthase (NADH) (L-glutamate: NAD+ oxidoreductase (transaminating) E.C. 1.4.1.14) has been investigated by studying competitive inhibition with respect ot 2-oxoglutarate. Binding requires two terminal carboxyl groups on a C5 straight chain molecule although some C4 molecules bind weakly. Bulky substituents at C2 decrease or prevent binding. Glutarate, the most potent inhibitor, binds much less tightly than the substrate. A 2-oxo group in a molecule other than the substrate does not appear to contribute significantly to binding. None of the analogues was able to act as an alternative substrate.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Feb
|
| pubmed:issn |
0006-3002
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
13
|
| pubmed:volume |
657
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
539-42
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:7213762-Glutamate Synthase,
pubmed-meshheading:7213762-Ketoglutaric Acids,
pubmed-meshheading:7213762-Kinetics,
pubmed-meshheading:7213762-NAD,
pubmed-meshheading:7213762-Oxidation-Reduction,
pubmed-meshheading:7213762-Plants,
pubmed-meshheading:7213762-Structure-Activity Relationship,
pubmed-meshheading:7213762-Transaminases
|
| pubmed:year |
1981
|
| pubmed:articleTitle |
Glutamate synthase (NADH) from lupin nodules. Specificity of the 2-oxoglutarate site.
|
| pubmed:publicationType |
Journal Article
|