|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
23
|
|
pubmed:dateCreated |
2000-12-20
|
|
pubmed:abstractText |
For (S)-thiirancarboxylic acid a second-order rate constant of k2nd = 222 M(-1) min(-1) for the irreversible inhibition of papain was determined. The ethyl and methyl ester do not inhibit the enzyme time-dependently. An improved synthesis of enantiomerically pure thiirancarboxylic acid is described. It is shown that thiirancarboxylates can be substrates for serine proteases (alpha-chymotrypsin) and esterases (pig liver esterase) and even for metallo proteases (thermolysin).
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Dec
|
|
pubmed:issn |
0960-894X
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
4
|
|
pubmed:volume |
10
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
2647-51
|
|
pubmed:dateRevised |
2009-1-8
|
|
pubmed:meshHeading |
|
|
pubmed:year |
2000
|
|
pubmed:articleTitle |
(S)-Thiirancarboxylic acid as a reactive building block for a new class of cysteine protease inhibitors.
|
|
pubmed:affiliation |
Institute for Pharmacy and Food Chemistry, University of Würzburg, Germany. schirmei@pharmazie.uni-wuerzburg.de
|
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|
