A MOFRL family glycerate kinase from the thermophilic crenarchaeon, Sulfolobus tokodaii, with unique enzymatic properties.
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.
Liu
Bo
B
College of Food and Bioengineering, Shandong Institute of Light Industry, Jinan, 250353, People's Republic of China.
Wu
Lei
L
Liu
Tianming
T
Hong
Ye
Y
Shen
Yulong
Y
Ni
Jinfeng
J
D000249:Adenosine Monophosphate / Q000378:metabolism; D003001:Cloning, Molecular; D003035:Cobalt / Q000494:pharmacology; D003067:Coenzymes / Q000494:pharmacology; D019281:Dimerization; D004795:Enzyme Stability; D004926:Escherichia coli / Q000235:genetics; D015870:Gene Expression; D005988:Glyceric Acids / Q000378:metabolism; D006160:Guanosine Triphosphate / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D017853:Phosphotransferases (Alcohol Group Acceptor) / Q000737:chemistry / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism*; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D016944:Sulfolobus / Q000201:enzymology* / Q000235:genetics*; D013696:Temperature
D003067:Coenzymes; D005988:Glyceric Acids; D011994:Recombinant Proteins; C008885:2-phosphoglycerate; D003035:Cobalt; D000249:Adenosine Monophosphate; C042971:glyceric acid; D006160:Guanosine Triphosphate; D017853:Phosphotransferases (Alcohol Group Acceptor); C020670:glycerate kinase