Linked Life Data

10567687

Source:http://linkedlifedata.com/resource/pubmed/id/10567687

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1999-12-28
pubmed:abstractText
Pantetheinase is an amidohydrolase involved in the dissimilative pathway of CoA, allowing the turnover of the pantothenate moiety. We have determined the N-terminal sequence as well as the sequences of a number of tryptic and chymotryptic peptides of the protein isolated from pig kidney. These sequence stretches were used as probes to search in the SwissProt database and significant similarities were found with a GPI-anchored protein (mouse vanin-1, with a suggested role in lymphocyte migration), with two putative proteins encoded by human cDNAs (VNN1 and VNN2) and with human biotinidase. On the basis of sequence similarity, we propose that vanin-1 and VNN1 should be identified as pantetheinase.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
19
pubmed:volume
461
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
149-52
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Is pantetheinase the actual identity of mouse and human vanin-1 proteins?
pubmed:affiliation
Dipartimento di Scienze Biochimiche 'A. Rossi Fanelli' and Centro di Biologia Molecolare del Consiglio Nazionale delle Ricerche Università La Sapienza, Piazzale Aldo Moro 5, 00185, Rome, Italy. bmaras@axrma.uniroma1.it
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't