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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
|
| pubmed:dateCreated |
1983-3-11
|
| pubmed:abstractText |
Chemical modification of a histidine and lysine residue inactivates pea seed nucleoside diphosphate kinase (NDP kinase). Thus there seems to be a reactive lysine residue, at the active site of pea seed NDP kinase, in addition to the histidine residue phosphorylated by the substrate ATP as a consequence of the enzyme reaction. The presence of a reactive lysine at the active site of the enzyme could explain why a small amount of N-epsilon-phospholysine, as well as 1-phosphohistidine and 3-phosphohistidine, is formed on alkaline hydrolysis of the enzyme.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:issn |
0300-9734
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
87
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
243-50
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading | |
| pubmed:year |
1982
|
| pubmed:articleTitle |
Effect of chemical modification of a histidine and a lysine residue of pea seed nucleoside diphosphate kinase.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|