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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
|
| pubmed:dateCreated |
1984-5-16
|
| pubmed:abstractText |
A method for preparation of homogeneous tyrosine phenol lyase (EC 4.199.2) from Citrobacter intermedius has been developed. The cells were cultivated in the media with a view to obtain a cell culture with a high activity of tyrosine phenol lyase. The isoelectric point for the enzyme lies at pH 4.9. Tyrosine phenol lyase is strictly stereospecific: it catalyzes the formation of pyruvate only from L-tyrosine, but not from D-tyrosine. Kinetic studies showed that K+ and NH4+ cations are non-competitive activators of the enzyme (Ka = 3.57 X 10(-3) and 1.34 X 10(-4) M, respectively).
|
| pubmed:language |
rus
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jan
|
| pubmed:issn |
0320-9725
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
49
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
32-7
|
| pubmed:dateRevised |
2007-7-23
|
| pubmed:meshHeading |
pubmed-meshheading:6704450-Chromatography, DEAE-Cellulose,
pubmed-meshheading:6704450-Citrobacter,
pubmed-meshheading:6704450-Enzyme Activation,
pubmed-meshheading:6704450-Isoelectric Point,
pubmed-meshheading:6704450-Kinetics,
pubmed-meshheading:6704450-Lyases,
pubmed-meshheading:6704450-Potassium,
pubmed-meshheading:6704450-Quaternary Ammonium Compounds,
pubmed-meshheading:6704450-Stereoisomerism,
pubmed-meshheading:6704450-Substrate Specificity,
pubmed-meshheading:6704450-Tyrosine Phenol-Lyase
|
| pubmed:year |
1984
|
| pubmed:articleTitle |
[Isolation and properties of tyrosine phenol-lyase from Citrobacter intermedius].
|
| pubmed:publicationType |
Journal Article,
English Abstract
|