The glutamate dehydrogenase-encoding gene of the hyperthermophilic archaeon Pyrococcus furiosus: sequence, transcription and analysis of the deduced amino acid sequence.
Glutamate dehydrogenase (GDH) from the hyperthermophilic archaeon, Pyrococcus woesei, has been isolated, characterized and found to be very similar if not identical to the recently purified GDH from P. furiosus. Using a polymerase chain reaction, based on the N-terminal amino acid sequences of GDH, the P. furiosus gdh gene was identified, cloned into Escherichia coli and sequenced. The transcription start point of gdh has been mapped 1 nucleotide upstream from the ribosome-binding site. Using antiserum raised against purified GDH, expression of gdh was observed in E. coli. The deduced primary sequence of the P. furiosus GDH has been compared to various bacterial, archaeal and eukaryal GDHs and showed a high degree of similarity (32-52%).
Eggen
R I
RI
Department of Microbiology, Wageningen Agricultural University, The Netherlands.
Geerling
A C
AC
Waldkötter
K
K
Antranikian
G
G
de Vos
W M
WM
D000595:Amino Acid Sequence; D001105:Archaea / Q000201:enzymology*; D001483:Base Sequence; D003001:Cloning, Molecular; D004269:DNA, Bacterial; D004926:Escherichia coli; D005969:Glutamate Dehydrogenase / Q000235:genetics*; D008969:Molecular Sequence Data; D014158:Transcription, Genetic
D004269:DNA, Bacterial; D005969:Glutamate Dehydrogenase