Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1986-2-12
pubmed:abstractText
The signal peptide generated during the maturation of prolipoprotein by the purified prolipoprotein signal peptidase can be isolated in substrate amounts (Dev, I. K., and Ray, P. H. (1984) J. Biol. Chem. 259, 11114-11120). This signal peptide is degraded predominantly from the carboxyl terminus by cell-free extracts of Escherichia coli. The signal peptide is degraded (at least 300-fold) more rapidly than other cellular proteins in E. coli. Greater than 90% of the signal peptide hydrolase activity is localized in the cytoplasm. Two enzymes from the cytoplasmic fraction responsible for the degradation of the signal peptide have been identified and purified to near homogeneity. The major activity is associated with a monomeric protein with a molecular weight of 68,000 (S.E. 3,400) as determined by gel filtration and by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. This enzyme appears to be similar to the oligopeptidase (Vimr, E. R., Green, L., and Miller, C. G. (1983) J. Bacteriol. 153, 1259-1265) that hydrolyzes N-acetyl tetra alanine. The second protein represents approximately 5% of the total cytoplasmic activity and has been shown to be a dimer with a monomer molecular weight of 81,000 (S.E. 5,300). This enzyme is similar to protease So (Chung, H. C., and Goldberg, A. L. (1983) J. Bacteriol. 154, 231-238).
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
261
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
420-7
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1986
pubmed:articleTitle
Localization and purification of two enzymes from Escherichia coli capable of hydrolyzing a signal peptide.
pubmed:publicationType
Journal Article