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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
|
| pubmed:dateCreated |
1990-3-5
|
| pubmed:abstractText |
The carboxylesterase P4 produced by Yersinia pseudotuberculosis was purified 330-fold by gel permeation and DEAE-trisacryl chromatography with a final yield of 21%. The apparent molecular weight, as determined by fast-protein liquid chromatography, was 45 kDa. The hydrolytic activity of esterase P4 was higher with the 1-naphthyl esters than with the 2-naphthyl esters of acetic, propionic and butyric acids. The apparent Km values were identical for 1-naphthyl acetate and 1-naphthyl propionate (0.15 mM). The enzyme was unstable at pH values below 5, but retained 80% of its initial activity after 30 min at 65 degrees C. It was unaffected by EDTA, eserine, tosyl-L-lysine chloromethylketone, iodoacetamide or 4-hydroxymercuribenzoate, but was strongly inhibited by low concentrations of diisopropyl fluorophosphate, suggesting the presence of serine in its active site. The purified enzyme gave a single precipitin line on Ouchterlony double immunodiffusion with homologous antiserum. This antiserum cross-reacted with the esterase bands E3 and E5 of Y. enterocolitica biotype 1, whereas there was no cross-reaction with the esterase bands produced by Y. enterocolitica biotypes 2 to 5, Y. intermedia, Y. frederiksenii, Y. kristensenii or Y. aldovae. The carboxylesterase P4 produced by Y. pestis was physicochemically, biochemically and immunologically indistinguishable from Y. pseudotuberculosis carboxylesterase P4. The latter enzyme and carboxylesterase B of Escherichia coli showed some biochemical similarities, but were antigenically unrelated. Our data confirm the relevance of esterases to phylogenetic and taxonomic studies of Enterobacteria.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:issn |
0923-2508
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
140
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
221-34
|
| pubmed:dateRevised |
2008-11-21
|
| pubmed:meshHeading |
pubmed-meshheading:2694247-Carboxylesterase,
pubmed-meshheading:2694247-Carboxylic Ester Hydrolases,
pubmed-meshheading:2694247-Cross Reactions,
pubmed-meshheading:2694247-Escherichia coli,
pubmed-meshheading:2694247-Hot Temperature,
pubmed-meshheading:2694247-Hydrogen-Ion Concentration,
pubmed-meshheading:2694247-Isoelectric Point,
pubmed-meshheading:2694247-Kinetics,
pubmed-meshheading:2694247-Molecular Weight,
pubmed-meshheading:2694247-Species Specificity,
pubmed-meshheading:2694247-Substrate Specificity,
pubmed-meshheading:2694247-Yersinia,
pubmed-meshheading:2694247-Yersinia pseudotuberculosis
|
| pubmed:articleTitle |
Isolation and properties of carboxylesterase P4 from Yersinia pseudotuberculosis.
|
| pubmed:affiliation |
Laboratoire de Microbiologie, Faculté X. Bichat, Université Paris VII.
|
| pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|