Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1993-10-21
pubmed:databankReference
pubmed:abstractText
A cDNA encoding phosphoenolpyruvate carboxykinase (PEPCK) from Ascaris suum was cloned by complementation of a strain of Escherichia coli deficient in PEPCK and malic enzyme. The product of this cDNA was enzymatically similar to a recombinant PEPCK obtained from Haemonchus contortus by the same method. Comparison of the predicted amino acid sequence of A. suum PEPCK with other PEPCKs showed that this enzyme is most closely related to the H. contortus enzyme. The two nematode enzymes share considerable homology in regions thought to be functionally involved in substrate binding and catalysis, some of which distinguish the nematode enzymes from PEPCKs from other organisms. This analysis suggests a structural explanation for the kinetic differences seen between nematode and vertebrate PEPCKs and supports the hypothesis that nematode PEPCK is a target for selective inhibition.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0014-4894
pubmed:author
pubmed:issnType
Print
pubmed:volume
77
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
155-61
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Ascaris suum: cloning of a cDNA encoding phosphoenolpyruvate carboxykinase.
pubmed:affiliation
Upjohn Laboratories, Upjohn Company, Kalamazoo, Michigan 49001.
pubmed:publicationType
Journal Article, Comparative Study