Linked Life Data

708698

Source:http://linkedlifedata.com/resource/pubmed/id/708698

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
20
pubmed:dateCreated
1979-1-26
pubmed:abstractText
Postproline cleaving enzyme [EC 3.4.21.-] has recently been purified from lamb kidney and tentatively identified as a serine endopeptidase with a high specificity for proline-containing peptides. The interaction of postproline cleaving enzyme with peptide substrates and competitive inhibitors has been studied in an effort to explore the size and stereospecificity of the active site of the protease. The substrates and inhibitors included proline-containing peptide amides, p-nitrophenyl esters, and free acids with increasing numbers of amino acid residues and residues of L and D configuration. Oligopeptides of alanine, which can also be recognized by the protease, were also tested as substrates. This series included Ala3, Ala-D-Ala-Ala, Ala-Ala-D-Ala,Z-(Ala)3, Ala4 through Ala6. The contribution of each of the three amino acid residues flanking the primary specificity site (S1) of postproline enzyme to such kinetic parameters as Km, Kcat, and Kcat/Km in the case of substrates and Ki with inhibitors was determined. The results suggest that postproline cleaving enzyme has an extended substrate binding region in addition to the primary specificity site, S1. It seems to be comprised of three sites located at the amino-terminal site (S1, S2, and S3) and two sites at the carboxyl site from the catalytic point (S1', S2'). High stereospecificity was observed for subsites S1, S2, and S1'.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
3
pubmed:volume
17
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4139-44
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1978
pubmed:articleTitle
Postproline cleaving enzyme: kinetic studies of size and stereospecificity of its active site.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.