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Cold-active esterase from Psychrobacter sp. Ant300: gene cloning, characterization, and the effects of Gly-->Pro substitution near the active site on its catalytic activity and stability.
Cold-Active Serine Alkaline Protease from the Psychrotrophic Bacterium Shewanella Strain Ac10: Gene Cloning and Enzyme Purification and Characterization
- L. Kulakova, A. Galkin, T. Kurihara, T. Yoshimura, N. Esaki
- BiologyApplied and Environmental Microbiology
- 1 February 1999
The recombinant SapSh (rSapSh) was found to have a molecular weight of about 44,000 and to be highly active in the alkaline region (optimum pH, around 9.0) when azocasein and synthetic peptides were used as substrates, but was far less stable than the subtilisin.
Synthesis of optically active amino acids from alpha-keto acids with Escherichia coli cells expressing heterologous genes
- A. Galkin, L. Kulakova, T. Yoshimura, K. Soda, N. Esaki
- Biology, EngineeringApplied and environmental microbiology
- 1 December 1997
A simple method for enzymatic synthesis of L and D amino acids from alpha-keto acids with Escherichia coli cells which express heterologous genes is described and optic pure D enantiomers of glutamate and leucine were obtained.
Cloning of formate dehydrogenase gene from a methanol-utilizing bacterium Mycobacterium vaccae N10
- A. Galkin, L. Kulakova, V. Tishkov, N. Esaki, K. Soda
- Biology, EngineeringApplied Microbiology and Biotechnology
- 1 December 1995
The gene of NAD+-dependent formate dehydrogenase (FDH) from Mycobacterium vaccae N10 was cloned into Escherichia coli by hybridization with digoxigenin-labeled DNA probes, which were prepared by…
Cold-Adapted Alanine Dehydrogenases from Two Antarctic Bacterial Strains: Gene Cloning, Protein Characterization, and Comparison with Mesophilic and Thermophilic Counterparts
- A. Galkin, L. Kulakova, H. Ashida, Y. Sawa, N. Esaki
- Biology, EngineeringApplied and Environmental Microbiology
- 1 September 1999
SheAlaDH and CarAla DH had features typical of cold-adapted enzymes; both the optimal temperature for catalytic activity and the temperature limit for retaining thermostability were lower than the values obtained for the mesophilic counterparts.
Cold-active DnaK of an Antarctic psychrotroph Shewanella sp. Ac10 supporting the growth of dnaK-null mutant of Escherichia coli at cold temperatures
- K. Yoshimune, A. Galkin, L. Kulakova, T. Yoshimura, N. Esaki
- Biology, EngineeringExtremophiles
- 1 April 2005
It is found that the Shewanella DNAK (SheDnaK) shows much higher ATPase activity at low temperatures than the DnaK of E. coli (EcoDNAK): a characteristic of a cold-active enzyme.
Purification and characterization of alanine dehydrogenase from a marine bacterium, Vibrio proteolyticus
Improvement of thermostability of cold-active serine alkaline protease from the psychrotrophic bacterium Shewanella sp. strain Ac10 by rational mutagenesis
Conversion of α-keto acids to d-amino acids by coupling of four enzyme reactions
Construction of a new leucine dehydrogenase with preferred specificity for NADP+ by site-directed mutagenesis of the strictly NAD+-specific enzyme.
- A. Galkin, L. Kulakova, T. Ohshima, N. Esaki, K. Soda
- Biology, ChemistryProtein engineering
- 1 June 1997
A mutant LeuDH with a new coenzyme specificity preferring NADP+ which is highly active (specific activity, 19 micromol/mg/min) is constructed.