title: Purification and characterization of the first archaeal glutamate decarboxylase from Pyrococcus horikoshii.
abstract: 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.
authors.affiliation: National Institute of Advanced Industrial Science and Technology (AIST), Ikeda, Osaka.
authors.forename: Han-Woo
authors.initials: HW
authors.lastname: Kim
authors.forename: Yasuhiro
authors.initials: Y
authors.lastname: Kashima
authors.forename: Kazuhiko
authors.initials: K
authors.lastname: Ishikawa
authors.forename: Naoko
authors.initials: N
authors.lastname: Yamano
mesh_terms: D004795:Enzyme Stability; D005968:Glutamate Decarboxylase / Q000302:isolation & purification*; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D043902:Pyrococcus horikoshii / Q000201:enzymology*; D013379:Substrate Specificity; D013672:Technology
chemical_list: D005968:Glutamate Decarboxylase