Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1998-11-20
pubmed:databankReference
pubmed:abstractText
D-Threonine dehydrogenase (EC 1.1.1) catalyses the oxidation of the 3-hydroxyl group of D-threonine. The nucleotide sequence of the structural gene, dtdS, for this enzyme from Pseudomonas cruciviae IFO 12047 was determined. The dtdS gene encodes a 292 amino acid polypeptide. The enzyme was overproduced in Escherichia coli cells; the activity was found in cell extracts of the clone. The enzyme showed high sequence similarity to 3-hydroxyisobutyrate dehydrogenases. This is the first example showing the primary structure of an enzyme catalysing the NADP(+)-dependent dehydrogenation of D-threo-3-hydroxyamino acids.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0378-1097
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
167
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
75-80
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Nucleotide sequence, cloning, and overexpression of the D-threonine dehydrogenase gene from Pseudomonas cruciviae.
pubmed:affiliation
Research Institute of Molecular Genetics, Kochi University, Japan.
pubmed:publicationType
Journal Article, Comparative Study