Linked Life Data

966249

Source:http://linkedlifedata.com/resource/pubmed/id/966249

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
1976-11-21
pubmed:abstractText
Derivatives of adenosine 5'-phosphate (AMP) have been synthesized in which the phosphoester (POCH2) grouping of AMP is replaced by PCH(R)CH2 where R is OC(O)Me, CH2NHCOMe, CH2NHCOEt, and CH2NHCOOR' (R' = Me, Et, and Pr). The 2',3'-O-isopropylidene and 2', 3'-di-O-acetyl derivatives of AMP were also prepared. All compounds were competitive inhibitors of rabbit muscle AMP aminohydrolase with enzyme-inhibitor dissociation constants (Ki values) of 330, 20, 17, 19, 16, 14, 260, and 105 muM, respectively. All compounds were substrates except those in which R was CH2NHCOEt and CH2NHCOOR' (R'=Me, Et, and Pr). The previously described allo and talo epimers of 5'-C-acetylaminomethyl-AMP and the allo epimer of 5'-C-propionylaminomethyl-AMP were substrates and competitive inhibitors with Ki values of 18, 47, and 42 muM, respectively. The talo epimer of 5'-C-propionylaminomethyl-AMP was not a substrate and was a noncompetitive inhibitor, Ki
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0022-2623
pubmed:author
pubmed:issnType
Print
pubmed:volume
19
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1029-33
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1976
pubmed:articleTitle
Design of substrate-site-directed irreversible inhibitors of adenosine 5'-phosphate aminohydrolase. Effect of substrate substituents on affinity for the substrate site.
pubmed:publicationType
Journal Article, In Vitro, Research Support, U.S. Gov't, P.H.S.