Linked Life Data

2487009

Source:http://linkedlifedata.com/resource/pubmed/id/2487009

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1991-3-4
pubmed:abstractText
Based on experimentally determined glycosidase molecular forms, their specificity and apparent Hill coefficients against trehalose (1.4) and sucrose (0.6), respectively, in honeybee haemolymph, a theoretical model is proposed involving differential types of non-random aggregation of a single enzyme protomer. This basic unit contains one trehalose-specific site and two asymmetrical subsites: one holds a catalytic zone and both share a proper affinity to any substrate non-specific binding zone. Then, the predicted aggregation possibilities of the promoter to dimers, trimers and tetramers very closely account for all the experimentally determined properties of the enzymes. Moreover, the hypothesis that the enzyme aggregation may be directed by the particular substrate present in major concentrations in the medium is supported by the observed differences in enzyme polymorphism following pre-incubation at high concentrations of either trehalose or sucrose in the medium.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0237-6261
pubmed:author
pubmed:issnType
Print
pubmed:volume
24
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
325-42
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Characterization of the honeybee haemolymph alpha-glycosidase specificity and apparent cooperativity as related to substrate-directed aggregation of enzyme asymmetric protomers.
pubmed:affiliation
Laboratory of Biochemistry, INRA, Montfavet, France.
pubmed:publicationType
Journal Article