Purification and characterization of the first archaeal glutamate decarboxylase from Pyrococcus horikoshii.
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.
Kim
Han-Woo
HW
National Institute of Advanced Industrial Science and Technology (AIST), Ikeda, Osaka.
Kashima
Yasuhiro
Y
Ishikawa
Kazuhiko
K
Yamano
Naoko
N
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
D005968:Glutamate Decarboxylase