Linked Life Data

2532042

Source:http://linkedlifedata.com/resource/pubmed/id/2532042

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1990-1-29
pubmed:abstractText
In contrast to previously studied ATP analogs, the two-substituted ATP analogs, 2-N3 ATP and 2-Cl ATP were good substrates for dynein ATPase. The Vmax for hydrolysis of both analogs was significantly higher than for ATP and the Km for both analogs was comparable to ATP. The higher hydrolytic rate for the analogs might be explained by a faster dissociation rate of the diphosphate product. This interpretation is supported by measurements of the dissociation rate of the inhibitor, vanadate. The estimate dissociation rate of vanadate with the analogs as substrate is approx. 2-fold higher than with ATP as substrate. These data together with previous studies on a variety of ATP analogs suggest that the 6-amino group on adenine is important for recognition by dynein and that the anti-conformation of the adenine, favored by 2-substituents, is the favored conformation of the nucleotide.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
999
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
221-4
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
ATP analogs substituted on the 2-position as substrates for dynein ATPase activity.
pubmed:affiliation
Program in Genetics and Cell Biology, Washington State University, Pullman 99164-4350.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.