Linked Life Data

1881875

Source:http://linkedlifedata.com/resource/pubmed/id/1881875

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1991-10-2
pubmed:abstractText
Plasmids containing wild-type and hybrid proteinase genes were constructed from DNA fragments of the prtP genes of Lactococcus lactis strains Wg2 and SK11. These plasmids were introduced into the plasmid-free strain L. lactis MG1363. The serine proteinases produced by these L. lactis strains were isolated, and their cleavage specificity and rate towards alpha s1- and beta-casein was investigated. The catalytic properties of both the SK11 and Wg2 proteinases, which differ in 44 out of 1902 amino acid residues, could be changed dramatically by the reciprocal exchange of specific fragments between the two enzymes. As a result, various L. lactis strains were constructed having new proteolytic properties that differ from those of the parental strains. Furthermore, two segments in the proteinase could be identified that contribute significantly to the cleavage specificity towards casein; within these two segments, several amino acid residues were identified that are important for substrate cleavage rate and specificity. The results also indicate that the lactococcal proteinase has an additional domain involved in substrate binding compared with the related subtilisins. This suggests that the 200 kd L. lactis proteinase may be the representative of a new subclass of subtilisin-like enzymes.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0269-2139
pubmed:author
pubmed:issnType
Print
pubmed:volume
4
pubmed:geneSymbol
prtM, prtP
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
479-84
pubmed:dateRevised
2008-11-24
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Engineering of the Lactococcus lactis serine proteinase by construction of hybrid enzymes.
pubmed:affiliation
Department of Biophysical Chemistry, Netherlands Institute for Dairy Research (NIZO), Ede.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't