Purification, characterization, and application of a novel dye-linked L-proline dehydrogenase from a hyperthermophilic archaeon, Thermococcus profundus
Article Abstract:
Researchers describe a dye-linked dehydrogenase from a thermophilic bacterium that reduces 2,6-dichloroindophenol in the presence of L-proline. This enzyme could be useful in biosensors and may be more stable than its counterpart in mesophilic bacteria.
author: Sakuraba, Haruhiko, Takamatsu, Yoshinori, Satomura, Takenori, Kawakami, Ryushi, Ohshima, Toshihisa
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2001
Biosensors, Microbial enzymes, Dehydrogenases, Oxidoreductases
First archaeal inorganic polyphosphate/ATP-dependent NAD kinase, from hyperthermophilic archaeon pyrococcus horikoshii: Cloning, expression, and characterization
Article Abstract:
The gene (PH1074) encoding the NAD kinase of the hyperthermophilic archaeon Pyrococcus horikoshii was identified in the genome database, cloned and functionally expressed in Escherichia coli. The deduced amino acid sequence showed a low level of identity to those of Escherichia coli ATP-dependant NAD kinase and the inorganic polyphosphate/ATP-dependent NAD kinase from a hyperthermophilic archaeon.
author: Sakuraba, Haruhiko, Kawakami, Ryushi, Ohshima, Toshihisa
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2005
Analysis, Physiological aspects, Gel electrophoresis, Phosphorylation, NAD (Coenzyme), Nicotinamide adenine dinucleotide
Sequential aldol condensation catalyzed by hyperthermophilic 2-deoxy-D-ribose-5-phosphate aldolase
Article Abstract:
Genes encoding from 2-deoxy-D-ribose-5-phosphate aldolases (DERAs) from two hyperthermophiles, the archaeon Pyrobaculum aerophilum and the bacterium Thermotoga maritima, are compared with Escherichia coli DERA in terms of their capacity to catalyze aldol condensation. The two enzymes from hyperthermophiles are highly resistant to acetaldehyde and have displayed greater catalysis of sequential aldol condensation of three acetaldehydes than the Escherichia coli enzyme, even at room temperature.
author: Sakuraba, Haruhiko, Kawakami, Ryushi, Ohshima, Toshihisa, Yoneda, Kazunari, Yoshihara, Kumiko, Satoh, Kyoko, Uto, Yoshihiro, Tsuge, Hideaki, Takahashi, Katsuyuki, Hori, Hitoshi
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2007
Chemical properties, Fructosediphosphate aldolase, Aldolases, Hyperthermophiles
subjects list: Research, Bacteria, Thermophilic, Thermophiles, Genetic aspects
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