Linked Life Data

6766356

Source:http://linkedlifedata.com/resource/pubmed/id/6766356

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1980-4-26
pubmed:abstractText
For a number of alkyl beta-D-xylopyranosides having branched-chain, cyclic, and substituted aglycon groups, and binding to beta-D-xylosidase from B. pumilus PRL B12, the binding constant Ki and (for some of them) the thermodynamic equilibrium parameters delta H0, delta S0, and delta G0 have been determined. Although the aglycon is bound through hydrophobic forces, no simple relationships between the binding parameters and the relative hydrophobicity of the alkyl beta-D-xylopyranosides could be demonstrated. All of the available evidence suggests that the aglycon sub-site has a highly specific structure which forces the atoms of the aglycon group to occupy well-defined positions. The supplementary energy-requirements resulting from the imposed restrictions seem to be the main reason for the irregular way in which the binding parameters depend on the aglycon structure.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0008-6215
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
78
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
317-26
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1980
pubmed:articleTitle
Binding of alkyl beta-D-xylopyranosides, containing branched-chain, cyclic, and substituted aglycon groups, to beta-D-xylosidase from Bacillus pumilus PRL B12.
pubmed:publicationType
Journal Article