Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
|
| pubmed:dateCreated |
1978-6-28
|
| pubmed:abstractText |
An experimental study has been made of both the steady-state and the transient-phase (presteady-state) kinetics of the hydrolyses of several saturated aliphatic esters of p-nitrophenol catalyzed by wheat germ lipase. The analysis of the presteady- 1 Presented in part at the 173rd ACS National Meeting, New Orleans, L.A., U.S.A., March 20--25, 1977. 2 Correspondence should be addressed to M.H. Sadar, E.S.D., E.H.C., Health and Welfare Canada, Tunney's Pasture, Ottawa, Ontario, Canada, K1A OL2. 3 Department of Chemistry, University of Ottawa, Ottawa, Ontario, Canada. state part revealed two transients indicating that lipase-catalyzed reactions proceed via a two-intermediate mechanism suggested for other esterases. The possibility of more than one species of the enzyme engaged in catalytic activity is discussed and a reaction mechanism scheme is proposed accordingly.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:issn |
0360-1234
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
13
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
117-29
|
| pubmed:dateRevised |
2009-7-21
|
| pubmed:meshHeading | |
| pubmed:year |
1978
|
| pubmed:articleTitle |
Transient-phase and steady-state kinetics of lipase-catalyzed ester hydrolysis.
|
| pubmed:publicationType |
Journal Article
|