• Publications
  • Influence
A Cold-Adapted Lipase of an Alaskan Psychrotroph,Pseudomonas sp. Strain B11-1: Gene Cloning and Enzyme Purification and Characterization
The enzyme showed a 1,3-positional specificity toward triolein and was stable between pH 6 and 9, and the optimal pH for the enzymatic hydrolysis of tributyrin was around 8.2, while the enzyme was unstable at temperatures higher than 45°C. Expand
Bacterial cysteine desulfurases: their function and mechanisms
  • H. Mihara, N. Esaki
  • Chemistry, Medicine
  • Applied Microbiology and Biotechnology
  • 4 September 2002
Enzymes capable of providing a variety of biosynthetic pathways for sulfur/selenium-containing biomolecules are probably applicable to the production of cofactors and the bioconversion of useful compounds. Expand
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
Selenocysteine lyase, a novel enzyme that specifically acts on selenocysteine. Mammalian distribution and purification and properties of pig liver enzyme.
A novel enzyme that exclusively decomposes L-selenocysteine into L-alanine and H2Se in various mammalian tissues is found, and it is the first proven enzyme that specifically acts on selenium compounds. Expand
Cysteine sulfinate desulfinase, a NIFS-like protein of Escherichia coli with selenocysteine lyase and cysteine desulfurase activities. Gene cloning, purification, and characterization of a novel
The Escherichia coli genome contains three genes with sequence homology to nifS, and a new enzyme catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L- Cysteine sulfinate desulfinase, and L-selenocystine to produce L-alanine is named. Expand
Crystal structure of L-2-haloacid dehalogenase from Pseudomonas sp. YL. An alpha/beta hydrolase structure that is different from the alpha/beta hydrolase fold.
The crystal structure of the homodimeric enzyme from Pseudomonas sp. Expand
Crystal Structure of a Homolog of Mammalian Serine Racemase from Schizosaccharomyces pombe*
The crystal-soaking experiment showed that the substrate serine was actually trapped in the active site of the modified enzyme, suggesting that the lysino-d-alanyl residue acts as a catalytic base in the same manner as inherent Lys-57 of the wild-type enzyme. Expand
Purification and characterization of thermostable and nonthermostable 2-haloacid dehalogenases with different stereospecificities from Pseudomonas sp. strain YL.
Two novel hydrolytic dehalogenases, thermostable L-2-haloacid dehalogenase (L-DEX) inducibly synthesized by 2-chloropropionate (2-CPA) and nonthermostable DL-2-haloacid dehalogenase (DL-DEX) inducedExpand
Cloning, heterologous expression, renaturation, and characterization of a cold-adapted esterase with unique primary structure from a psychrotroph Pseudomonas sp. strain B11-1.
A gene coding for an esterase of the psychrotrophic bacterium Pseudomonas sp. Expand
Kinetic and mutational studies of three NifS homologs from Escherichia coli: mechanistic difference between L-cysteine desulfurase and L-selenocysteine lyase reactions.
Three NifS homologs from Escherichia coli, CSD, CsdB, and IscS, that appear to be involved in iron-sulfur cluster formation and/or the biosynthesis of selenophosphate are purified, suggesting the presence of different rate-limiting steps or reaction mechanisms for L-cysteine desulfurization and the degradation of L-selenocysteine. Expand