Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adenosine Monophosphate / metabolism
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Cloning, Molecular
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Cobalt / pharmacology
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Coenzymes / pharmacology
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Dimerization
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Enzyme Stability
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Escherichia coli / genetics
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Gene Expression
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Glyceric Acids / metabolism
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Guanosine Triphosphate / metabolism
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Hydrogen-Ion Concentration
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Molecular Weight
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Phosphotransferases (Alcohol Group Acceptor) / chemistry
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Phosphotransferases (Alcohol Group Acceptor) / genetics*
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Phosphotransferases (Alcohol Group Acceptor) / isolation & purification
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Phosphotransferases (Alcohol Group Acceptor) / metabolism*
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / isolation & purification
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Recombinant Proteins / metabolism
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Sulfolobus / enzymology*
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Sulfolobus / genetics*
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Temperature
Substances
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Coenzymes
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Glyceric Acids
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Recombinant Proteins
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2-phosphoglycerate
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Cobalt
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Adenosine Monophosphate
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glyceric acid
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Guanosine Triphosphate
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Phosphotransferases (Alcohol Group Acceptor)
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glycerate kinase