dc.contributor.author |
Vangnai, Alisa |
|
dc.contributor.author |
Promden, Worrawat |
|
dc.contributor.author |
De-Eknamkul, Wanchai |
|
dc.contributor.author |
Matsushita, Kazunobu |
|
dc.contributor.author |
Toyama, Hirohide |
|
dc.date.accessioned |
2018-03-28T07:33:47Z |
|
dc.date.available |
2018-03-28T07:33:47Z |
|
dc.date.issued |
2009-06 |
|
dc.identifier.citation |
Biochemistry (Moscow), 2010, Vol. 75, No. 4, pp. 452-459 |
en_US |
dc.identifier.isbn |
0006 2979 |
|
dc.identifier.uri |
http://dspace.bru.ac.th/xmlui/handle/123456789/4100 |
|
dc.description.abstract |
The quinate dehydrogenase (QDH) from Gluconobacter oxydans IFO3244 exhibits high affinity for quinate, sug gesting its application in shikimate production. Nucleotide sequence analysis of the qdh gene revealed a full length of 2475 bp encoding an 824 amino acid protein. The qdh gene has the unusual TTG translation initiation codon. Conserved regions and a signature sequence for the quinoprotein family were observed. Phylogenetic analysis demonstrated relatedness of QDH from G. oxydans to other quinate/shikimate dehydrogenases with the highest similarity (56%) with that of Acinetobacter calcoaceticus ADP1 and lower similarity (36%) with a membrane bound glucose dehydrogenase of Escherichia coli. The function of the gene coding for QDH was confirmed by heterologous gene expression in pyrroloquinoline quinone synthesizing Pseudomonas putida HK5. |
en_US |
dc.language.iso |
en_US |
en_US |
dc.publisher |
มหาวิทยาลัยราชภัฏบุรีรัมย์ |
en_US |
dc.subject |
Quinate Dehydrogenase |
en_US |
dc.subject |
Gluconobacter oxydans |
en_US |
dc.title |
Molecular Characterization and Heterologous Expression of Quinate Dehydrogenase Gene from Gluconobacter oxydans IFO3244 |
en_US |
dc.title.alternative |
Molecular Characterization and Heterologous Expression of Quinate Dehydrogenase Gene from Gluconobacter oxydans IFO3244 |
en_US |
dc.type |
Article |
en_US |