Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1983-3-24
pubmed:abstractText
1. Inhibition of the Rhynchosciara americana midgut trehalase (alpha, alpha'-trehalose glucohydrolase, EC 3.2.1.28) by the competitive inhibitor dioxane have been studied. 2. Determinations of the Ki of dioxane at different pH provided the true pKa values of the prototropic groups of the trehalase active site (pKa 5.2 and 8.2), which are in agreement with those determined previously from kinetic and chemical modification data. 3. Dioxane only changes the enzyme pKa values if bound at the enzyme active site. 4. Gluconic acid does not inhibit the trehalase, in contrast to delta-gluconolactone which is a simple intersecting linear inhibitor. 5. Multiple inhibition analyses showed that delta-gluconolactone and Tris bind at the same site in the trehalase active center, whereas dioxane binds closer to delta-gluconolactone than to Tris. 6. The data support the assumption that dioxane binds at the middle portion of the trehalase active site.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0020-711X
pubmed:author
pubmed:issnType
Print
pubmed:volume
15
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
143-6
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
1983
pubmed:articleTitle
Inhibition of an insect midgut trehalase by dioxane and delta-gluconolactone: enzyme pKa values and geometric relationships at the active site.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't