Linked Life Data

6243987

Source:http://linkedlifedata.com/resource/pubmed/id/6243987

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1980-5-14
pubmed:abstractText
The precise localization of adenylate kinase (ATP:AMP phosphotransferase, EC 2.7.4.3) has been studied in pig heart mitochondria. This enzyme, which was distinct from the cytoplasmic enzyme, was insensitive towards SH reagents and exhibited a relatively weak inhibition by the specific inhibitor P1, P5-diadenosine-5'-pentaphosphate. The enzyme has been partially purified from isolated mitochondria. In the forward reaction adenylate kinase was very specific for AMP and less specific for the ATP site. Kinetic studies showed that in the forward direction, KMgATP and KAMP the dissociation constants of the substrates from the binary complexes were lower than the dissociation constants from the ternary complexes. In the reverse direction KMgADP was higher than KADP, but these values were not modified by the binding of the other substrate. In the forward direction, the enzyme was inhibited by excess of substrate when AMP concentrations were greater than 1 mM. This inhibition could prevent the phosphorylation of AMP to ADP and thus decrease the amount of adenine nucleotides available for oxidative phosphorylations.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
14
pubmed:volume
611
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
299-308
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1980
pubmed:articleTitle
General and kinetic properties of pig heart mitochondrial adenylate kinase.
pubmed:publicationType
Journal Article