Linked Life Data

10625703

Source:http://linkedlifedata.com/resource/pubmed/id/10625703

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2000-2-18
pubmed:databankReference
pubmed:abstractText
This work contains the first description of a guanidino kinase in a flagellar unicellular parasite. The enzyme phosphorylates L-arginine and was characterized in preparations from Trypanosoma cruzi, the ethiological agent of Chagas' disease. The activity requires ATP and a divalent cation. Under standard assay conditions (1 mM L-arginine), the presence of 5-fold higher concentrations of canavanine or histidine produced a greater than 50% enzyme inhibition. The base sequence of this enzyme revealed an open reading frame of 357 amino acids and a molecular weight of 40,201. The amino acid sequence shows all of the characteristic consensus blocks of the ATP:guanidino phosphotransferase family and a putative "actinin-type" actin-binding domain. The highest amino acid identities of the T. cruzi sequence, about 70%, were with arginine kinases from Arthropoda. Southern and chromosome blots revealed that the kinase is encoded by a single-copy gene. Moreover, Northern blot analysis showed an mRNA subpopulation of about 2.0 kilobases, and Western blotting of T. cruzi-soluble polypeptides revealed a 40-kDa band. The finding in the parasite of a phosphagen and its biosynthetic pathway, which are totally different from those in mammalian host tissues, points out this arginine kinase as a possible chemotherapy target for Chagas' disease.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
14
pubmed:volume
275
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1495-501
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:10625703-Amino Acid Sequence, pubmed-meshheading:10625703-Amino Acids, pubmed-meshheading:10625703-Animals, pubmed-meshheading:10625703-Arginine Kinase, pubmed-meshheading:10625703-Base Sequence, pubmed-meshheading:10625703-Cations, Divalent, pubmed-meshheading:10625703-Chromatography, Affinity, pubmed-meshheading:10625703-Chromosome Mapping, pubmed-meshheading:10625703-Cloning, Molecular, pubmed-meshheading:10625703-Genomic Library, pubmed-meshheading:10625703-Humans, pubmed-meshheading:10625703-Kinetics, pubmed-meshheading:10625703-Molecular Sequence Data, pubmed-meshheading:10625703-Phylogeny, pubmed-meshheading:10625703-Recombinant Proteins, pubmed-meshheading:10625703-Sequence Alignment, pubmed-meshheading:10625703-Sequence Homology, Amino Acid, pubmed-meshheading:10625703-Trypanosoma cruzi
pubmed:year
2000
pubmed:articleTitle
Trypanosoma cruzi arginine kinase characterization and cloning. A novel energetic pathway in protozoan parasites.
pubmed:affiliation
Instituto de Investigaciones en Ingeniería Genética y Biología Molecular, Consejo Nacional de Investigaciones Científicas y Técnicas, and Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Buenos Aires, Argentina.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't