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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.
Observations could be explained in terms of a decrease in active-site flexibility brought about by the mutation and were consistent with the hypothesis that cold activity and thermolability arise from local flexibility around the active site of the enzyme. Expand
Cold-Active Serine Alkaline Protease from the Psychrotrophic Bacterium Shewanella Strain Ac10: Gene Cloning and Enzyme Purification and Characterization
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. Expand
Cloning of formate dehydrogenase gene from a methanol-utilizing bacterium Mycobacterium vaccae N10
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 byExpand
Synthesis of optically active amino acids from alpha-keto acids with Escherichia coli cells expressing heterologous genes
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. Expand
Cold-Adapted Alanine Dehydrogenases from Two Antarctic Bacterial Strains: Gene Cloning, Protein Characterization, and Comparison with Mesophilic and Thermophilic Counterparts
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. Expand
Cold-active DnaK of an Antarctic psychrotroph Shewanella sp. Ac10 supporting the growth of dnaK-null mutant of Escherichia coli at cold temperatures
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. Expand
Improvement of thermostability of cold-active serine alkaline protease from the psychrotrophic bacterium Shewanella sp. strain Ac10 by rational mutagenesis
Abstract A serine alkaline protease (SapSh) from a psychrophilic bacterium Shewanella sp. strain Ac10 is a cold-active subtilase with low thermostability [Appl. Environ. Microbiol. 65 (1999)Expand
Purification and characterization of alanine dehydrogenase from a marine bacterium, Vibrio proteolyticus
Abstract Alanine dehydrogenase of Vibrio proteolyticus DSM 30189 shows high activity toward β-hydroxypyruvate, and the enzyme is applicable to the production of l -serine. We have cloned the enzymeExpand
Conversion of α-keto acids to d-amino acids by coupling of four enzyme reactions
Abstract We developed a new procedure for stereospecific conversion of various α-keto acids to the corresponding d -amino acids with four thermostable enzymes: d -amino acid aminotransferase, alanineExpand
Construction of a new leucine dehydrogenase with preferred specificity for NADP+ by site-directed mutagenesis of the strictly NAD+-specific enzyme.
A mutant LeuDH with a new coenzyme specificity preferring NADP+ which is highly active (specific activity, 19 micromol/mg/min) is constructed. Expand