Linked Life Data

18229

Source:http://linkedlifedata.com/resource/pubmed/id/18229

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1977-9-22
pubmed:abstractText
The enthalpy of binding, deltaHb, of flavin adenine dinucleotide to the apoenzyme of D-amino acid oxidase was determined by flow calorimetry at pH 8.5 to be +3.8, -4.1 and -11.0 kcal mol-1 at 10 degrees, 25 degrees and 38 degrees, respectively. These values correspond to a heat capacity change, deltaCp, of -530 cal K-1 mol-1. From the binding constant reported by Dixon and Kleppe (1965a) and the above enthalpies, the standard free energy and standard entropy of binding are evaluated. These thermodynamic data are interpreted in terms of hydrophobic and vibrational contributions (Sturtevant, 1977). The product of the assay reaction (Fonda and Anderson, 1967), benzoylformic acid, is a non-competitive inhibitor of the enzyme with a value for KI of 1.4 X 10(-4)M at 25 degrees.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0303-2647
pubmed:author
pubmed:issnType
Print
pubmed:volume
8
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
247-53
pubmed:dateRevised
2009-10-27
pubmed:meshHeading
pubmed:year
1977
pubmed:articleTitle
Thermodynamics of the binding of flavin adenine dinucleotide to D-amino acid oxidase.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.