Linked Life Data

7037007

Source:http://linkedlifedata.com/resource/pubmed/id/7037007

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1982-4-22
pubmed:abstractText
Adenylosuccinate (succino-AMP) synthetase and succino-AMP lyase isolated from epimastigotes of Trypanosoma cruzi by chromatography on phosphocellulose. The synthetase was capable of catalyzing the condensation of aspartic acid with IMP and several IMP analogs. The reaction with allopurinol ribonucleotide is of potential chemotherapeutic interest. This analog was slowly converted to its corresponding succino-AMP analog with a Km' of 140 micrometers (cf. IMP at 10 micrometers) and a Vmax' of 0.3 per cent the rate with IMP. The comparable reaction with this analog does not occur with succino-AMP synthetase from a representative mammalian source [T. Spector and R. L. Miller, Biochim. biophys. Acta 455, 509 (1976)]. The protozoal succino-AMP lyase had a broad substrate which was characteristic of this enzyme from many sources. It catalyzed the rapid and efficient cleavage of all the succino-AMP analogs that were produced by succino-AMP synthetase. Thus, these two enzymes appear to be responsible for the selective amination of allopurinol ribonucleotide in T. cruzi. The metabolically produced AMP analog may be the agent or a precursor of the agent that accounts for the anti-growth activity of allopurinol in these organisms. Similar selective amination was observed previously with these enzymes from Leishmania donovani [T. Spector, T. E. Jones and G. B. Elion, J. biol. Chem. 254, 8422 (1979)]. Thiopurinol ribonucleotide was not a substrate of succino-AMP synthetase from T. cruzi, but it was an inhibitor with a K1 = 33 micrometers. Therefore, the weakness of thiopurinol's anti-growth activity with T. cruzi is not due to its inability to inhibit this enzyme.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0006-2952
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
31
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
225-9
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
Adenylosuccinate synthetase and adenylosuccinate lyase from Trypanosoma cruzi, Specificity studies with potential chemotherapeutic agents.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't