PMID- 10525154
OWN - NLM
STAT- MEDLINE
DCOM- 19991116
LR  - 20190610
IS  - 0006-3002 (Print)
IS  - 0006-3002 (Linking)
VI  - 1434
IP  - 2
DP  - 1999 Oct 12
TI  - The NAD-dependent glutamate dehydrogenase from the hyperthermophilic archaeon 
      Pyrobaculum islandicum: cloning, sequencing, and expression of the enzyme 
      gene(1).
PG  - 365-71
AB  - The NAD-dependent glutamate dehydrogenase (GluDH) gene from the hyperthermophilic 
      archaeon Pyrobaculum islandicum was cloned and expressed in Escherichia coli. 
      Analysis of the nucleotide sequence revealed an open reading frame of 1266 bp 
      encoding a protein of 421 amino acids with a molecular weight of 46,905. In the 
      alignment of the amino acid sequence with those of mesophilic Clostridium 
      symbiosum NAD-dependent GluDH and hyperthermophilic NADP-dependent enzymes from 
      Thermococcus profundus and Pyrococcus furiosus, substitutions in the residues 
      involved in dinucleotide binding were observed. On the other hand, the residues 
      involved in glutamate binding were well conserved. This is the first description 
      of the primary structure of NAD-dependent GluDH in hyperthermophilic archaea.
FAU - Kujo, C
AU  - Kujo C
AD  - Department of Biological Science and Technology, Faculty of Engineering, The 
      University of Tokushima, 2-1 Minamijosanjimacho, Tokushima, Japan.
FAU - Sakuraba, H
AU  - Sakuraba H
FAU - Nunoura, N
AU  - Nunoura N
FAU - Ohshima, T
AU  - Ohshima T
LA  - eng
SI  - GENBANK/AB027194
PT  - Comparative Study
PT  - Journal Article
PL  - Netherlands
TA  - Biochim Biophys Acta
JT  - Biochimica et biophysica acta
JID - 0217513
RN  - EC 1.4.1.2 (Glutamate Dehydrogenase)
RN  - EC 1.4.1.3 (glutamate dehydrogenase (NAD(P)+))
SB  - IM
MH  - Amino Acid Sequence
MH  - Base Sequence
MH  - Cloning, Molecular
MH  - Electrophoresis, Polyacrylamide Gel
MH  - Gene Expression
MH  - *Genes, Archaeal
MH  - Glutamate Dehydrogenase/chemistry/*genetics/isolation & purification
MH  - Molecular Sequence Data
MH  - Sequence Alignment
MH  - Thermoproteaceae/*enzymology
EDAT- 1999/10/19 00:00
MHDA- 1999/10/19 00:01
CRDT- 1999/10/19 00:00
PHST- 1999/10/19 00:00 [pubmed]
PHST- 1999/10/19 00:01 [medline]
PHST- 1999/10/19 00:00 [entrez]
AID - S0167483899001922 [pii]
AID - 10.1016/s0167-4838(99)00192-2 [doi]
PST - ppublish
SO  - Biochim Biophys Acta. 1999 Oct 12;1434(2):365-71. doi: 
      10.1016/s0167-4838(99)00192-2.