Linked Life Data

2123487

Source:http://linkedlifedata.com/resource/pubmed/id/2123487

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
34
pubmed:dateCreated
1991-1-17
pubmed:databankReference
pubmed:abstractText
The cDNA for glutamine phosphoribosylpyrophosphate amidotransferase, the regulatory enzyme of de novo purine nucleotide biosynthesis, has been cloned for the first time from an animal. The derived amino acid sequence of the avian amidotransferase is homologous with amidotransferase sequences from bacteria and yeast. An 11-amino acid propeptide in Bacillus subtilis amidotransferase is conserved in the avian enzyme. Expression in Chinese hamster ovary (CHO) cells and Escherichia coli provides evidence for two post-translational maturation steps needed for synthesis of active enzyme: incorporation of an iron component and processing of the 11-amino acid propeptide. Functional complementation of a CHO amidotransferase mutant suggests that both maturation steps take place in CHO cells. In contrast, function in E. coli requires deletion of the sequence encoding the propeptide. Defective assembly of the iron component may restrict propeptide removal and activation of the avian amidotransferase in E. coli.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
265
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
21152-9
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Cloning and expression of avian glutamine phosphoribosylpyrophosphate amidotransferase. Conservation of a bacterial propeptide sequence supports a role for posttranslational processing.
pubmed:affiliation
Department of Biochemistry, Purdue University, West Lafayette, Indiana 47907.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S.