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763 results on '"SHIMIZU, Sakayu"'

32. Engineering cytochrome P450 BM-3 for oxidation of polycyclic aromatic hydrocarbons

Author

Li, Qing-Shan, Ogawa, Jun, Schmid, Rolf D., and Shimizu, Sakayu

Subjects
Biodegradation -- Research, Polycyclic aromatic hydrocarbons -- Research, Microbial genetic engineering -- Research, Biological sciences
Abstract

Researchers have created a bioengineered form of cytochrome P450 BM-3 from Bacillus megaterium that has higher activity against polycyclic aromatic hydrocarbons than the native enzyme. The mutant enzyme could be used to degrade these compounds in polluted soil.

Published
2001

33. Purification, characterization, and gene cloning of purine nucleosidase from Ochrobactrum anthropi

Author

Ogawa, Jun, Takeda, Sou, Xie, Sheng-Xue, Hatanaka, Haruyo, Ashikari, Toshihiko, Amachi, Teruo, and Shimizu, Sakayu

Subjects
Nucleotidases -- Research, Microbial enzymes -- Research, Biological sciences
Abstract

A purine nucleosidase isolated from Ochrobactrum anthropi appears to be homologous to nucleosidases from protozoan parasites. It has a molecular weight of 170,000, has four identical subunits, and catalyzes the N-riboside hydrolysis of purine nucleosides.

Published
2001

34. Conjugated linoleic acid accumulation via 10-hydroxy-12-octadecaenoic acid during microaerobic transformation of linoleic acid by Lactobacillus acidophilus

Author

Ogawa, Jun, Matsumura, Kenji, Kishino, Shigenobu, Omura, Yoriko, and Shimizu, Sakayu

Subjects
Linoleic acids -- Research, Microbial metabolism -- Research, Biological sciences
Abstract

Conjugated linoleic acid can be produced by Lactobacillus acidophilus from linoleic acid. Animal studies have shown that conjugated linoleic acid has substantial health benefits, and the cis-9, trans-11-octadecadienoic acid isomer appears to be the most important isomer from a health standpoint.

Published
2001

39. A novel amidase (half-amidase) for half-amide hydrolysis involved in the bacterial metabolism of cyclic imides

Author

Soong, Chee-Leong, Ogawa, Jun, and Shimizu, Sakayu

Subjects
Bacteria -- Physiological aspects, Protein engineering -- Research, Cyclic compounds -- Physiological aspects, Enzymes -- Physiological aspects, Histidine -- Physiological aspects, Amides -- Physiological aspects, Biological sciences
Abstract

An amidase, named 'half-amidase,' that catalyzes the second step of cyclic imide transformation has been reported. It is involved in the half-amide hydrolysis that is part of the bacterial metabolism of cyclic imides, for which it is highly specific.

Published
2000

40. Purification and characterization of monovalent cation-activated levodione reductase from Corynebacterium aquaticum M-13

Author

Wada, Masaru, Yoshizumi, Ayumi, Nakamori, Shigeru, and Shimizu, Sakayu

Subjects
Cations -- Research, Enzymes -- Research, Oxidation-reduction reaction -- Research, Biological sciences
Abstract

Monovalent cation-activated levodione reductase of Corynebacterium aquaticum M-13, not previously reported, is discussed. The reductase was isolated from a cell extract of the soil isolate C. aquaticum. The enzyme required certain cofactors, but catalyzed reversible oxidoreduction between actinol and levodione, activated by monovalent cations. The enzyme is in the short-chain alcohol dehydrogenase/reductase family.

Published
1999

41. Identification of an NADH-cytochrome b5 reductase gene from an arachidonic acid-producing fungus, Mortierella alpina 1S-4, by sequencing of the encoding cDNA and heterologous expression in a fungus, Aspergillus oryzae

Author

Sakuradani, Eiji, Kobayashi, Michihiko, and Shimizu, Sakayu

Subjects
Aspergillus -- Genetic aspects, Circular DNA -- Research, Cytochromes -- Research, Fungi -- Genetic aspects, Biological sciences
Abstract

The isolation and characterization of the NADH-cytochrome b5 reductases (CbR) gene from Mortierella alpina 1S-4 and the purification of the CbR expressed in Aspergillus oryzae are described. It was found that the purified CbR used NADH but not NADPH as an electron donor. When NADH was utilized as the electron donor, DCPIP was observed to be reduced by the purified CbR. Results provide support for the hypothesis that the cDNA cloned is definitely a CbR gene.

Published
1999

42. Cyclic-imide-hydrolyzing activity of D-hydantoinase from Blastobacter sp. strain A17p-4

Author

Soong, Chee-Leong, Ogawa, Jun, Honda, Michinari, and Shimizu, Sakayu

Subjects
Hydrolysis -- Research, Enzymes -- Structure-activity relationship, Pyrimidines -- Research, Biological sciences
Abstract

A study of the cyclic-imide-hydrolyzing activity of a prokaryotic cyclic-ureide-hydrolyzing enzyme, D-hydantoinase, revealed that its structure, physico-chemical properties and NH2-terminal amino acid sequence similar to other reported bacterial D-hydantoinases. It showed the highest catalytic efficiency toard dihydropyrimidines and was induced by dihydropyrimidines. These imply that the cyclic-imide-hydrolyzing activity of D-hydantoinase might likewise be a general property of bacterial D-hydantoinases identical to dihydropyrimidinase.

Published
1999

50. Gene cloning, nucleotide sequencing, and purification and characterization of the low-specificity L-threonine aldolase from Pseudomonas sp. strain NCIMB 10558

Author

Liu, Ji-Quan, Ito, Saeko, Dairi, Tohru, Itoh, Nobuya, Kataoka, Michihiko, Shimizu, Sakayu, and Yamada, Hideaki

Subjects
Escherichia coli -- Genetic aspects, Threonine -- Research, Pseudomonas -- Genetic aspects, Enzymes -- Genetic aspects, Amino acid sequence -- Research, Mutagenesis -- Usage, Biological sciences
Abstract

Site-directed mutagenesis was used to investigate the cloning, sequencing and overexpression in Escherichia coli cells of the low-specificity L-threonine aldolase (L-TA) gene from the Pseudomonas strain NCIMB 10558, purification and characterization of the recombinant enzyme and the identification of the active-site lysine residue of the enzyme. The amino acid sequence displayed less than 20% identity with those of low-specificity L-TA from Saccharomyces cerevisiae, L-allo-threonine aldolase from Aeromonas jandaei and other hypothetical proteins from other microorganisms.

Published
1998

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