Linked Life Data

2292683

Source:http://linkedlifedata.com/resource/pubmed/id/2292683

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1991-4-9
pubmed:abstractText
The molecular (1-Amino-2-phenylethyl)phosphonic acid is shown to inhibit the enzymatic activity of carboxypeptidase A. Through the spectroscopic investigation of the cobalt(II) substituted enzyme we propose that it binds the enzyme in the 1:1 ratio directly at the metal, probably through the phosphate group like phosphate itself. The aromatic group is proposed to sit in the so-called S1 hydrophobic pocket. This is a unique behavior among the inhibitors of the enzyme. The S'1 site is still available in the binary adduct so that a ternary complex can be obtained with molecules like L-Phenylalanine, which enter that site.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0162-0134
pubmed:author
pubmed:issnType
Print
pubmed:volume
40
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
227-35
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
The unusual behavior of the inhibitor S(+)(1-amino-2-phenylethyl)phosphonic acid towards carboxypeptidase A.
pubmed:affiliation
Institute of Chemistry, University of Wroclaw, Poland.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't