guanosine-triphosphate and glyceric-acid

guanosine-triphosphate has been researched along with glyceric-acid* in 1 studies

Other Studies

1 other study(ies) available for guanosine-triphosphate and glyceric-acid

Article	Year
A MOFRL family glycerate kinase from the thermophilic crenarchaeon, Sulfolobus tokodaii, with unique enzymatic properties. Biotechnology letters, 2009, Volume: 31, Issue:12 A glycerate kinase gene (ST2037) from the hyperthermophilic crenarchaeon Sulfolobus tokodaii was cloned and expressed in Escherichia coli. The purified homodimeric protein (45 kDa) specifically catalyzed the formation of 2-phosphoglycerate with D-glycerate as substrate. The thermostable enzyme displayed maximum activity (over 20 min) at 90 degrees C and pH 4.5. The maximal activity was in the presence of Co(2+). The MOFRL family glycerate kinase used AMP as phosphate donor with maximal activity towards GTP. These characteristics of the enzyme suggested its potential in the catalytic production of 2-phosphoglycerate. Topics: Adenosine Monophosphate; Cloning, Molecular; Cobalt; Coenzymes; Dimerization; Enzyme Stability; Escherichia coli; Gene Expression; Glyceric Acids; Guanosine Triphosphate; Hydrogen-Ion Concentration; Molecular Weight; Phosphotransferases (Alcohol Group Acceptor); Recombinant Proteins; Sulfolobus; Temperature	2009

Article

Year

A MOFRL family glycerate kinase from the thermophilic crenarchaeon, Sulfolobus tokodaii, with unique enzymatic properties.

Biotechnology letters, 2009, Volume: 31, Issue:12

A glycerate kinase gene (ST2037) from the hyperthermophilic crenarchaeon Sulfolobus tokodaii was cloned and expressed in Escherichia coli. The purified homodimeric protein (45 kDa) specifically catalyzed the formation of 2-phosphoglycerate with D-glycerate as substrate. The thermostable enzyme displayed maximum activity (over 20 min) at 90 degrees C and pH 4.5. The maximal activity was in the presence of Co(2+). The MOFRL family glycerate kinase used AMP as phosphate donor with maximal activity towards GTP. These characteristics of the enzyme suggested its potential in the catalytic production of 2-phosphoglycerate.

Topics: Adenosine Monophosphate; Cloning, Molecular; Cobalt; Coenzymes; Dimerization; Enzyme Stability; Escherichia coli; Gene Expression; Glyceric Acids; Guanosine Triphosphate; Hydrogen-Ion Concentration; Molecular Weight; Phosphotransferases (Alcohol Group Acceptor); Recombinant Proteins; Sulfolobus; Temperature

2009