Linked Life Data

8117714

Source:http://linkedlifedata.com/resource/pubmed/id/8117714

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
1994-4-7
pubmed:abstractText
A novel GAR transformylase has been isolated and characterized from E. coli. The protein, a product of the purT gene, is a monomer of molecular weight 42 kDa and catalyzes the production of beta-formyl GAR from formate, ATP, and beta-GAR. As such it is an alternative to the formyl-folate utilizing purN GAR transformylase. No significant homology exists between the two transformylases. However, the purT protein shows significant homology to the purK protein, also involved in purine biosynthesis. Two different purT reactions have been characterized: one producing fGAR from ATP, beta-GAR, and formate and the other producing acetyl phosphate and ADP from acetate and ATP. The purT GAR transformylase is the first unknown de novo purine biosynthetic enzyme to be discovered in the last 30 years and represents another step forward in understanding cellular control of purine levels.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
8
pubmed:volume
33
pubmed:geneSymbol
purT
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2531-7
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Cloning and characterization of a new purine biosynthetic enzyme: a non-folate glycinamide ribonucleotide transformylase from E. coli.
pubmed:affiliation
Department of Chemistry, Pennsylvania State University, University Park 16802.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.