Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
18
pubmed:dateCreated
2004-9-2
pubmed:databankReference
pubmed:abstractText
Four orthologous genes (TK1108, TK1404, TK1777, and TK2185) that can be annotated as phosphomannomutase (PMM) genes (COG1109) have been identified in the genome of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1. We previously found that TK1777 actually encodes a phosphopentomutase. In order to determine which of the remaining three orthologues encodes a phosphoglucomutase (PGM), we examined the PGM activity in T. kodakaraensis cells and identified the gene responsible for this activity. Heterologous gene expression and purification and characterization of the recombinant protein indicated that TK1108 encoded a protein with high levels of PGM activity (690 U mg(-1)), along with high levels of PMM activity (401 U mg(-1)). Similar analyses of the remaining two orthologues revealed that their protein products exhibited neither PGM nor PMM activity. PGM activity and transcription of TK1108 in T. kodakaraensis were found to be higher in cells grown on starch than in cells grown on pyruvate. Our results clearly indicate that, among the four PMM gene orthologues in T. kodakaraensis, only one gene, TK1108, actually encodes a protein with PGM and PMM activities.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/15342576-10348846, http://linkedlifedata.com/resource/pubmed/commentcorrection/15342576-10788412, http://linkedlifedata.com/resource/pubmed/commentcorrection/15342576-11017041, http://linkedlifedata.com/resource/pubmed/commentcorrection/15342576-11562374, http://linkedlifedata.com/resource/pubmed/commentcorrection/15342576-11716469, http://linkedlifedata.com/resource/pubmed/commentcorrection/15342576-12065581, http://linkedlifedata.com/resource/pubmed/commentcorrection/15342576-12355162, http://linkedlifedata.com/resource/pubmed/commentcorrection/15342576-12426324, http://linkedlifedata.com/resource/pubmed/commentcorrection/15342576-12486058, http://linkedlifedata.com/resource/pubmed/commentcorrection/15342576-12813088, http://linkedlifedata.com/resource/pubmed/commentcorrection/15342576-15205420, http://linkedlifedata.com/resource/pubmed/commentcorrection/15342576-1532581, http://linkedlifedata.com/resource/pubmed/commentcorrection/15342576-16233297, http://linkedlifedata.com/resource/pubmed/commentcorrection/15342576-205363, http://linkedlifedata.com/resource/pubmed/commentcorrection/15342576-2231712, http://linkedlifedata.com/resource/pubmed/commentcorrection/15342576-7811092, http://linkedlifedata.com/resource/pubmed/commentcorrection/15342576-7984417, http://linkedlifedata.com/resource/pubmed/commentcorrection/15342576-8288525, http://linkedlifedata.com/resource/pubmed/commentcorrection/15342576-9116819, http://linkedlifedata.com/resource/pubmed/commentcorrection/15342576-9307027
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/2-deoxyribose 1-phosphate, http://linkedlifedata.com/resource/pubmed/chemical/Archaeal Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Coenzymes, http://linkedlifedata.com/resource/pubmed/chemical/DNA, Archaeal, http://linkedlifedata.com/resource/pubmed/chemical/Glucosephosphates, http://linkedlifedata.com/resource/pubmed/chemical/Mannosephosphates, http://linkedlifedata.com/resource/pubmed/chemical/Phosphoglucomutase, http://linkedlifedata.com/resource/pubmed/chemical/Phosphotransferases (Phosphomutases), http://linkedlifedata.com/resource/pubmed/chemical/Pyruvic Acid, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Ribosemonophosphates, http://linkedlifedata.com/resource/pubmed/chemical/Starch, http://linkedlifedata.com/resource/pubmed/chemical/glucose-1-phosphate, http://linkedlifedata.com/resource/pubmed/chemical/mannose 1-phosphate, http://linkedlifedata.com/resource/pubmed/chemical/phosphomannomutase
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0021-9193
pubmed:author
pubmed:issnType
Print
pubmed:volume
186
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6070-6
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed-meshheading:15342576-Amino Acid Sequence, pubmed-meshheading:15342576-Archaeal Proteins, pubmed-meshheading:15342576-Cloning, Molecular, pubmed-meshheading:15342576-Coenzymes, pubmed-meshheading:15342576-DNA, Archaeal, pubmed-meshheading:15342576-Enzyme Stability, pubmed-meshheading:15342576-Genes, Archaeal, pubmed-meshheading:15342576-Glucosephosphates, pubmed-meshheading:15342576-Kinetics, pubmed-meshheading:15342576-Mannosephosphates, pubmed-meshheading:15342576-Molecular Sequence Data, pubmed-meshheading:15342576-Phosphoglucomutase, pubmed-meshheading:15342576-Phosphotransferases (Phosphomutases), pubmed-meshheading:15342576-Phylogeny, pubmed-meshheading:15342576-Pyruvic Acid, pubmed-meshheading:15342576-Recombinant Proteins, pubmed-meshheading:15342576-Ribosemonophosphates, pubmed-meshheading:15342576-Sequence Alignment, pubmed-meshheading:15342576-Sequence Analysis, DNA, pubmed-meshheading:15342576-Sequence Homology, Amino Acid, pubmed-meshheading:15342576-Starch, pubmed-meshheading:15342576-Substrate Specificity, pubmed-meshheading:15342576-Temperature, pubmed-meshheading:15342576-Thermococcus
pubmed:year
2004
pubmed:articleTitle
Among multiple phosphomannomutase gene orthologues, only one gene encodes a protein with phosphoglucomutase and phosphomannomutase activities in Thermococcus kodakaraensis.
pubmed:affiliation
Department of Synthetic Chemistry and Biological Chemistry, Graduate School of Engineering, Kyoto University, Katsura, Nishikyo-ku, Kyoto 615-8510, Japan.
pubmed:publicationType
Journal Article