Linked Life Data

3890845

Source:http://linkedlifedata.com/resource/pubmed/id/3890845

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1985-7-8
pubmed:abstractText
The kinetic parameters Km and kcat and the resulting proteolytic coefficients kcat/Km for the hydrolysis of blocked alanine peptide esters (X(Ala)nOMe) and -p-nitroanilides (X(Ala)n-pNA) of variable length (n = 1 to 5 alanine residues) by the cationic, microbial serine protease thermitase are determined in order to delineate the number of subsites involved in catalysis. Thermitase has at least five secondary subsites (S1 to S5) being hydrophobic in S1 to S4. Arrhenius plots for both, esterase and amidase activity were biphasic with a break at 30 degrees C, followed by a downward bend. The influence of dimethylformamide, solute for many substrates, on the thermitase-catalyzed esterolysis of Z(Ala)2OMe was also investigated. In contrast to the kcat values being unaffected by 5 to 30% dimethylformamide, the Km values increased logarithmically with enhancing its concentration.
pubmed:language
ger
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0232-766X
pubmed:author
pubmed:issnType
Print
pubmed:volume
44
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
175-83
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1985
pubmed:articleTitle
[The kinetics of hydrolysis of alanine peptide esters and -p-nitroanilides by thermitase, a thermostable serine protease from Thermoactinomyces vulgaris: secondary specificity, influence of temperature and solute].
pubmed:publicationType
Journal Article, English Abstract