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A psychrotrophic bacterium producing a cold-adapted lipase upon growth at low temperatures was isolated from Alaskan soil and identified as a Pseudomonas strain. The lipase gene (lipP) was cloned from the strain and sequenced. The amino acid sequence deduced from the nucleotide sequence of the gene (924 bp) corresponded to a protein of 308 amino acid(More)
Selenocysteine lyase (EC 4.4.1.16) exclusively decomposes selenocysteine to alanine and elemental selenium, whereas cysteine desulfurase (NIFS protein) of Azotobacter vinelandii acts indiscriminately on both cysteine and selenocysteine to produce elemental sulfur and selenium respectively, and alanine. These proteins exhibit some sequence homology. The(More)
L-Lysine alpha-oxidase from Trichoderma viride Y244-2 has been purified to homogeneity. The enzyme shows absorption maxima at 277, 388, and 466 nm and a shoulder around 490 nm and contains 2 mol of FAD/mol of enzyme. The enzyme has a molecular weight of approximately 116,000 and consists of two subunits identical in molecular weight (about 56,000). In(More)
L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation of L-2-haloalkanoic acids to yield the corresponding D-2-hydroxyalkanoic acids. The crystal structure of the homodimeric enzyme from Pseudomonas sp. YL has been determined by a multiple isomorphous replacement method and refined at 2.5 A resolution to a crystallographic R-factor of 19.5%. The(More)
The distribution of bacterial L-methionine gamma-lyase (L-methionine methanethiollyase (deaminating) (EC 4.4.1.11) was investigated, and Pseudomonas ovalis (IFO 3738) was found to have the highest activity of enzyme, which was inducibly formed by addition of L-methionine to the medium. L-Methionine gamma-lyase, purified to homogeneity from Ps. ovalis, has a(More)
The distribution of bacterial leucine dehydrogenase (L-leucine:NAD+ oxidoreductase, deaminating, EC 1.4.1.9) was investigated, and Bacillus sphaericus (IFO 3525) was found to have the highest activity of the enzyme. Leucine dehydrogenase, which was purified to homogeneity and crystallized from B. sphaericus, has a molecular weight of about 245,000 and(More)
We have found a novel enzyme that exclusively decomposes L-selenocysteine into L-alanine and H2Se in various mammalian tissues, and have named it selenocysteine lyase. The enzyme from pig liver has been purified to homogeneity. It has a molecular weight of approximately 85,000, and contains pyridoxal 5'-phosphate as a coenzyme. Its maximum reactivity is at(More)
Poly-gamma-glutamic acid (gamma-PGA) is a very promising biodegradable polymer that is produced by Bacillus subtilis. Gamma-PGA is water-soluble, anionic, biodegradable, and edible. This paper reviews the production of a strain of gamma-PGA and recent developments with respect to applications in terms of Ca absorption, moisturizing properties, gamma-PGA(More)
Over the last decade, amino acid dehydrogenases such as alanine dehydrogenase (Ala DH), leucine dehydrogenase (Leu DH), and phenylalanine dehydrogenase (Phe DH) have been applied to the enantiomer-specific synthesis and analysis of various amino acids. In perticular, amino acid dehydrogenases from thermophiles have received much attention because of their(More)
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) induced by 2-chloroacrylate, were purified to homogeneity from Pseudomonas sp. strain YL. DL-DEX consisted of a monomer with a molecular weight of about 36,000 and(More)