Linked Life Data

2724298

Source:http://linkedlifedata.com/resource/pubmed/id/2724298

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1989-7-11
pubmed:abstractText
The reaction between peptide aldehydes and acylhydrazones affords derivatives that represent potential prodrugs for selective inhibition of lysosomal enzymes. BzPheal = Ala, obtained from the reaction between N-benzoyl-L-phenylalaninal and N-acetyl-L-alanine hydrazide, has been most carefully studied. When BzPheal = Ala is introduced into ongoing reactions catalyzed by alpha-chymotrypsin or papain, the rate of these reactions diminishes more rapidly with time than do those of controls lacking BzPheal = Ala. Furthermore, the disparity between run and control is much greater at pH 5 than at pH 7. The extent of inhibition (defined as explained in the text) at pH 5 can exceed that at pH 7 by 25-40-fold. The data are quantitatively explained by a reaction scheme that recognizes three important properties of BzPheal = Ala: (1) It undergoes hydrolysis at pH 5-7 to regenerate N-benzoyl-L-phenylalaninal; (2) the aldehyde thus liberated is a far more potent inhibitor for serine or cysteine proteases than is BzPheal = Ala; and (3) the rate constant for hydrolysis of BzPheal = Ala at pH 5 greatly exceeds that at pH 7.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0022-2623
pubmed:author
pubmed:issnType
Print
pubmed:volume
32
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1253-9
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Acid-sensitive latent inhibitors for proteolytic enzymes: synthesis and characterization.
pubmed:affiliation
Department of Chemistry, Amherst College, Massachusetts 01002.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S.