Linked Life Data

16245349

Source:http://linkedlifedata.com/resource/pubmed/id/16245349

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2006-3-21
pubmed:abstractText
D-amino acid oxidase (DAO) is of considerable practical importance, such as bioconversion and enzymatic assay. In this study, we succeeded in obtaining a thermostable mutant DAO from porcine kidney by a single amino acid substitution. This mutant enzyme, F42C, was stable at 55 degrees C, while the wild-type enzyme was stable only up to 45 degrees C. The Km values of F42C for D-amino acids was about half of those of the wild-type enzyme. This mutant DAO with improved stability and affinity for its substrates is advantageous for the determination of D-amino acids.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0006-3592
pubmed:author
pubmed:copyrightInfo
(c) 2005 Wiley Periodicals, inc.
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
93
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1023-7
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:16245349-Amino Acid Substitution, pubmed-meshheading:16245349-Animals, pubmed-meshheading:16245349-Binding Sites, pubmed-meshheading:16245349-D-Amino-Acid Oxidase, pubmed-meshheading:16245349-Dimerization, pubmed-meshheading:16245349-Enzyme Stability, pubmed-meshheading:16245349-Escherichia coli, pubmed-meshheading:16245349-Genetic Vectors, pubmed-meshheading:16245349-Hot Temperature, pubmed-meshheading:16245349-Hydrogen-Ion Concentration, pubmed-meshheading:16245349-Kidney, pubmed-meshheading:16245349-Kinetics, pubmed-meshheading:16245349-Models, Molecular, pubmed-meshheading:16245349-Mutagenesis, Site-Directed, pubmed-meshheading:16245349-Protein Conformation, pubmed-meshheading:16245349-Protein Engineering, pubmed-meshheading:16245349-Recombinant Proteins, pubmed-meshheading:16245349-Swine, pubmed-meshheading:16245349-Temperature, pubmed-meshheading:16245349-Transfection
pubmed:year
2006
pubmed:articleTitle
Thermostabilization of porcine kidney D-amino acid oxidase by a single amino acid substitution.
pubmed:affiliation
Research and Development Division, Kikkoman Corporation, 399 Noda, Noda City, Chiba 278-0037, Japan. mbakke@mail.kikkoman.co.jp
pubmed:publicationType
Journal Article