Linked Life Data

786618

Source:http://linkedlifedata.com/resource/pubmed/id/786618

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1976-11-21
pubmed:abstractText
The Km and V values of the tRNA-charging reaction have been measured for L-phenylalanine:tRNA ligase and the geometric isomers of adenosine 5'-O-(1-thio)triphosphate, adenosine 5'-O-(2-thio)triphosphate and for 5'-O-(3-thio)triphosphate. All ATP analogs were found to be substrates with values of Km similar or (up to 10-fold) higher, and with values of V in the range of 10--30% compared with the natural substrate. The dissociation constants of the binary enzyme-nucleotide and ternary enzyme-nucleotide-L-phenylalaninol complexes were analysed as a function of the position of the sulfur atom indicating those phosphate groups which are involved in an enzyme-triphosphate interaction. The results are consistent with a participation of the beta and gamma-phosphate in the binary complex formation and an additional interaction at the positions of the alpha and beta-phosphate groups in the ternary complexes.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
67
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
171-6
pubmed:dateRevised
2007-7-23
pubmed:meshHeading
pubmed:year
1976
pubmed:articleTitle
L-Phenylalanine: tRNA ligase of Escherichia coli K10. The effect of O replaced by S substitution on substrate and ligand binding properties of ATP.
pubmed:publicationType
Journal Article