Linked Life Data

7765336

Source:http://linkedlifedata.com/resource/pubmed/id/7765336

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1994-4-15
pubmed:databankReference
pubmed:abstractText
We have investigated the aminopeptidase activities present in Streptomyces lividans strains. The majority of these activities proved to be intracellular with multiple active species. Two aminopeptidase P genes were identified to be responsible for the ability to hydrolyze amino terminal peptide bonds adjacent to proline residues. Two other broad spectrum aminopeptidases were found to display homology at both the DNA and protein levels. One showed significant homology to PepN proteins, particularly around the putative zinc-binding residues which are important for catalysis. The second broad spectrum activity was not analyzed in detail but showed a different spectrum of substrate specificity to that of PepN.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
B
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0169-4146
pubmed:author
pubmed:issnType
Print
pubmed:volume
13
pubmed:geneSymbol
pepG, pepP1, pepP2
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
24-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Intracellular aminopeptidases in Streptomyces lividans 66.
pubmed:affiliation
Cangene Corporation, Mississauga, Ontario, Canada.
pubmed:publicationType
Journal Article