Linked Life Data

4000111

Source:http://linkedlifedata.com/resource/pubmed/id/4000111

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1985-7-11
pubmed:abstractText
The interaction of bifunctional ATP derivatives, Appp5'[NH-(CH2) n-NH]ppp5'A (n = 0 or 2-8) with tyrosyl-, valyl-, lysyl-, tryptophanyl-tRNA synthetases and creatine kinase was investigated. ATP derivatives don't inhibit the tRNA aminoacylation catalyzed by tyrosyl-tRNA synthetase. These derivatives behave as mixed-type inhibitors with respect to ATP in the case of valyl- and lysyl-tRNA-synthetases. In the case of the other enzymes all analogs of ATP manifest competitive inhibition towards ATP. The affinity of all ATP derivatives to tryptophanyl-tRNA synthetase does not differ significantly (Ki = 0.2 divided by 0.6 mM). The Ki values for these derivatives in the case of creatine kinase are also very similar with the exception of A5'ppp-NH-(CH2)3-NH-ppp5'A. The Ki value for this derivative is one order of magnitude lower than for other ones. The affinity reagents received by periodate oxidation of bifunctional ATP analogs derivatives of di-, tetra- and heptamethylenediamine modify non-identical subunits of creatine kinase with different velocities, but modification of M- and M'-subunits proceeds independently. An analogues derivative of trimethylenediamine interacts simultaneously with two centers of the dimeric form of kinase forming non-equivalent complexes. The covalent attachment of the reagent to one subunit of creatine kinase does not except the complex formation and covalent binding of bifunctional ATP analogs with the other subunit of the dimer, but results in a one order of magnitude decrease in affinity of the ATP derivative to the nonmodified centre of the enzyme. These data permit to evaluate the distance between ATP binding sites of creatine kinase in its dimeric form as 5-6 A approximately. Such a distance between active sites may be the reason for the higher activity of the M- and M'-creatine kinase subunits taken separately as compared to the enzyme dimeric form.
pubmed:language
rus
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0026-8984
pubmed:author
pubmed:issnType
Print
pubmed:volume
19
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
467-78
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:articleTitle
[Interaction of various nucleotide-dependent enzymes with bifunctional analogs of ATP, derivatives of polymethylene diamines].
pubmed:publicationType
Journal Article, In Vitro, English Abstract