Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1980-8-28
pubmed:abstractText
Peptidases which are specific for proline residues have been described and include endopeptidases (post-proline cleaving enzyme and proline specific endopeptidase), N-terminal exopeptidases (post-proline dipeptidyl aminopeptidase, proline iminopeptidase, aminopeptidase P), C-terminal exopeptidases (prolylcarboxypeptidase, and carboxypeptidase P) and dipeptidases (prolyl dipeptidase and proline dipeptidase). The properties, distinguishing charcteristics, and possible significance of these proline specific endo- and exopeptidases are discussed. In addition, reference is made to a series of enzymes which can hydrolyze proline containing peptide bonds, but which are not specific for proline.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0300-8177
pubmed:author
pubmed:issnType
Print
pubmed:day
18
pubmed:volume
30
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
111-27
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:6991912-Aminopeptidases, pubmed-meshheading:6991912-Angiotensin II, pubmed-meshheading:6991912-Animals, pubmed-meshheading:6991912-Binding Sites, pubmed-meshheading:6991912-Brain, pubmed-meshheading:6991912-Carboxypeptidases, pubmed-meshheading:6991912-Dipeptidases, pubmed-meshheading:6991912-Dipeptidyl-Peptidases and Tripeptidyl-Peptidases, pubmed-meshheading:6991912-Endopeptidases, pubmed-meshheading:6991912-Flavobacterium, pubmed-meshheading:6991912-Hydrogen-Ion Concentration, pubmed-meshheading:6991912-Kidney, pubmed-meshheading:6991912-Kinetics, pubmed-meshheading:6991912-Molecular Weight, pubmed-meshheading:6991912-Peptide Hydrolases, pubmed-meshheading:6991912-Proline, pubmed-meshheading:6991912-Serine Endopeptidases, pubmed-meshheading:6991912-Substrate Specificity
pubmed:year
1980
pubmed:articleTitle
Proline specific endo- and exopeptidases.
pubmed:publicationType
Journal Article, Review