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rdf:type |
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|
lifeskim:mentions |
|
|
pubmed:issue |
1-6
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pubmed:dateCreated |
1978-3-10
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|
pubmed:abstractText |
Kynureninase was purified to homogeneity from the extracts of Pseudomonas marginalis and Neurospora crassa. The active kynureninase containing pyridoxal 5'-phosphate transaminates with L-ornithine or L-alanine to form the inactive pyridoxamine 5'-phosphate form of enzyme and delta1-pyrroline-2-carboxylate or pyruvate. This inactive enzyme transaminates with pyruvate to restore the active pyridoxal 5'-phosphate enzyme and L-alanine. The activity of kynureninase is regulated in this manner by transamination of the coenzyme moiety.
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pubmed:language |
eng
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|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
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pubmed:chemical |
|
|
pubmed:status |
MEDLINE
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pubmed:issn |
0300-8924
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pubmed:author |
|
|
pubmed:issnType |
Print
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pubmed:volume |
29
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pubmed:owner |
NLM
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|
pubmed:authorsComplete |
Y
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pubmed:pagination |
335-8
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
|
|
pubmed:year |
1975
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|
pubmed:articleTitle |
Regulation of the activity of microbial kynureninase by transamination of the enzyme-bound coenzyme.
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pubmed:publicationType |
Journal Article
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