Linked Life Data

12568809

Source:http://linkedlifedata.com/resource/pubmed/id/12568809

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2003-2-5
pubmed:abstractText
High concentrations of D-aspartate occur in blood shell Scapharca broughtonii (Mollusca) tissues. We purified aspartate racemase from the foot muscle of the bivalve to electrophoretic homogeneity. The molecular mass shown by sodium dodecyl sulfate polyacrylamide gel was 39 kDa, while that shown by gel filtration ranged from 51 to 63 kDa. Pyridoxal 5'-phosphate-dependency of the enzyme was demonstrated by its absorption spectrum as well as the effects of amino-oxyacetate and other reagents on the activity and spectrum. The enzyme is highly specific to aspartate and does not racemize L-alanine, L-serine and L-glutamate. It showed the highest activity at pH 8 both in the conversion of L- to D- and D- to L-aspartate, and the optimal temperature was 25 degrees C. V(max) and K(m) values for L-aspartate were 7.39 micromolmin(-1)mg(-1) and 60.4 mM and those for D-aspartate were 22.6 micromolmin(-1)mg(-1) and 159 mM, respectively.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
1096-4959
pubmed:author
pubmed:issnType
Print
pubmed:volume
134
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
307-14
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
Purification and characterization of aspartate racemase from the bivalve mollusk Scapharca broughtonii.
pubmed:affiliation
Department of Environmental Systems Engineering, Nagaoka University of Technology, Nagaoka, Niigata 940-2188, Japan.
pubmed:publicationType
Journal Article