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

Biotechnol Lett. 2009 Dec;31(12):1937-41. doi: 10.1007/s10529-009-0089-z. Epub 2009 Aug 19.

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

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Monophosphate / metabolism
  • Cloning, Molecular
  • Cobalt / pharmacology
  • Coenzymes / pharmacology
  • Dimerization
  • Enzyme Stability
  • Escherichia coli / genetics
  • Gene Expression
  • Glyceric Acids / metabolism
  • Guanosine Triphosphate / metabolism
  • Hydrogen-Ion Concentration
  • Molecular Weight
  • Phosphotransferases (Alcohol Group Acceptor) / chemistry
  • Phosphotransferases (Alcohol Group Acceptor) / genetics*
  • Phosphotransferases (Alcohol Group Acceptor) / isolation & purification
  • Phosphotransferases (Alcohol Group Acceptor) / metabolism*
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Recombinant Proteins / isolation & purification
  • Recombinant Proteins / metabolism
  • Sulfolobus / enzymology*
  • Sulfolobus / genetics*
  • Temperature

Substances

  • Coenzymes
  • Glyceric Acids
  • Recombinant Proteins
  • 2-phosphoglycerate
  • Cobalt
  • Adenosine Monophosphate
  • glyceric acid
  • Guanosine Triphosphate
  • Phosphotransferases (Alcohol Group Acceptor)
  • glycerate kinase