Linked Life Data

2211639

Source:http://linkedlifedata.com/resource/pubmed/id/2211639

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
29
pubmed:dateCreated
1990-11-21
pubmed:databankReference
pubmed:abstractText
Four forms of dihydrodipicolinate synthase (DHDPS), which catalyzes the first reaction in the lysine-specific biosynthetic pathway in higher plants, were purified to homogeneity from a suspension culture of wheat (Triticum aestivum). These polypeptides have similar N-terminal amino acid sequences. Two different cDNA clones were isolated by screening a wheat cDNA library with oligonucleotide probes based on these amino acid sequences. The predicted amino acid sequences indicate that both clones encode putative chloroplast transit peptides that have little homology to each other as well as the conserved mature protein portions of Mr 35,737 and 35,776 (94% identity). Mature wheat DHDPS has 30% amino acid identity to Escherichia coli DHDPS. One of the cloned cDNAs, which had been fused to bacterial transcription/translation signals, genetically complemented a strain of E. coli that lacks endogenous DHDPS activity. Moreover, the expression of wheat DHDPS cDNA in wild-type E. coli increased the enzymatic activity 10-fold in the transformed bacteria.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
265
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
17451-5
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Molecular cloning of wheat dihydrodipicolinate synthase.
pubmed:affiliation
Research Center for Cell and Tissue Culture, Faculty of Agriculture, Kyoto University, Japan.
pubmed:publicationType
Journal Article