Purification and characterization of the first archaeal glutamate decarboxylase from Pyrococcus horikoshii

Biosci Biotechnol Biochem. 2009 Jan;73(1):224-7. doi: 10.1271/bbb.80583. Epub 2009 Jan 7.


Glutamate decarboxylase (GAD) from the archaeon Pyrococcus horikoshii was successfully expressed and purified, with the aim of developing a hyperthermostable GAD for industrial applications. Its biochemical properties were different from those reported for other GADs. The enzyme had broad substrate specificity, and its optimum pH and temperature were pH 8.0 and > 97 degrees C.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Enzyme Stability
  • Glutamate Decarboxylase / isolation & purification*
  • Hot Temperature
  • Hydrogen-Ion Concentration
  • Pyrococcus horikoshii / enzymology*
  • Substrate Specificity
  • Technology


  • Glutamate Decarboxylase