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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
|
| pubmed:dateCreated |
1983-9-20
|
| pubmed:abstractText |
Cells of Escherichia coli grown under physiological (noninducing) conditions have a low level of lysine decarboxylase activity. This activity differs from the enzyme found in induced cells in its sensitivity to putrescine (33% of control in the presence of 20 mM putrescine). It is also sensitive to spermidine (20% of control in the presence of 6 mM spermidine). A mixture of putrescine and spermidine completely eliminated lysine decarboxylase activity. This provides evidence for the existence of a biosynthetic enzyme and suggests a mechanism to explain the appearance of cadaverine in polyamine-depleted cells.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jul
|
| pubmed:issn |
0006-291X
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
29
|
| pubmed:volume |
114
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
882-8
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading | |
| pubmed:year |
1983
|
| pubmed:articleTitle |
Putrescine and spermidine sensitivity of lysine decarboxylase in Escherichia coli: evidence for a constitutive enzyme and its mode of regulation.
|
| pubmed:publicationType |
Journal Article
|