rdf:type |
|
lifeskim:mentions |
umls-concept:C0001459,
umls-concept:C0001480,
umls-concept:C0006960,
umls-concept:C0007382,
umls-concept:C0014442,
umls-concept:C0016598,
umls-concept:C0060666,
umls-concept:C0205103,
umls-concept:C0332120,
umls-concept:C0441712,
umls-concept:C1522492
|
pubmed:issue |
13
|
pubmed:dateCreated |
1976-9-1
|
pubmed:abstractText |
Formyltetrahydrofolate synthetase from Clostridium cylindrosporum catalyzes phosphoryl transfer from carbamyl phosphate in ADP to form ATP. The phosphoryl transfer reaction has an obligatory requirement for tetrahydrofolate presumably as a cofactor for a proper conformation of the active site. Carbamyl phosphate is an analog of formyl phosphate-a potential intermediate in the normal enzymic reaction. The ability of the enzyme to promote synthesis of ATP from carbamyl phosphate and ADP supports a stepwise chemical reaction mechanism for the enzyme in which formyl phosphate participates as a tightly bound intermediate.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Jul
|
pubmed:issn |
0021-9258
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
10
|
pubmed:volume |
251
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
4159-61
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
|
pubmed:year |
1976
|
pubmed:articleTitle |
Formyltetrahydrofolate synthetase-catalyzed formation of ATP from carbamyl phosphate and ADP. Evidence for a formyl phosphate intermediate in the enzyme's catalytic mechanism.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|