• Publications
  • Influence
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
Structural Insight into Arginine Degradation by Arginine Deiminase, an Antibacterial and Parasite Drug Target*
The crystal structure of ADI is determined from Pseudomonas aeruginosa by the multi-wavelength anomalous diffraction method at 2.45 Å resolution and the assumption that the substrate binding mode is similar to that of DDAH, an ADI catalytic mechanism is proposed. 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
Crystal structure of the YgfZ protein from Escherichia coli suggests a folate-dependent regulatory role in one-carbon metabolism.
The ygfZ gene product of Escherichia coli represents a large protein family conserved in bacteria to eukaryotes that lacks amino acid conservation at the folate site, which implies that YfZ is likely a folate-dependent regulatory protein involved in one-carbon metabolism. Expand
Crystal Structures Representing the Michaelis Complex and the Thiouronium Reaction Intermediate of Pseudomonas aeruginosa Arginine Deiminase*
Through the comparison of the structures of apoenzyme and substrate-bound enzyme, a substrate-induced conformational transition, which might play an important role in activity regulation, was discovered. Expand
Pilot scale production and isolation of recombinant NAD+- and NADP+-specific formate dehydrogenases.
The expression of the recombinant wild-type NAD+- and mutant NADP+-dependent formate dehydrogenases (EC, FDH) from the methanol-utilizing bacterium Pseudomonas sp. 101 in Escherichia coliExpand
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
Kinetic analysis of Pseudomonas aeruginosa arginine deiminase mutants and alternate substrates provides insight into structural determinants of function.
Results are interpreted to suggest that electrostatic interactions play a dominant role in PaADI catalysis, and insight into the evolution of the catalysts that form the GMSF is provided. Expand