Faculty Profiles - KANZAKI Hiroshi

MISC - KANZAKI Hiroshi

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Microorganisms with homocysteine thiolactone hydrolase: Screening and stereospecificity - Abstracts

Shozo Honda, Teruhiko Nitoda, Hiroshi Kanzaki

JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC 42 ( 3-4 ) 126 - 127 2006.11

Further proof for wide substrate specificity of cyclo(Leu-Phe) oxidase from an actinomycete: Enzymatic conversion of cyclic dipeptides containing non-aromatic amino acids - Abstracts

Rie Hirata, Teruhiko Nitoda, Hiroshi Kanzaki

JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC 42 ( 3-4 ) 127 - 128 2006.11

Cloning and expression of cyclo(Leu-Phe) oxidase gene from an actinomycete Streptomyces albulus K023

Machiko Nagao, Atsushi Morimoto, Takashi Tamura, Tohru Dairi, Hiroshi Kanzaki

JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC 42 ( 3-4 ) 126 - 126 2006.11

Inhibitory specificity of a novel β-N-acetylglucosaminidase inhibitor HU-1

USUKI Hirokazu, NITODA Teruhiko, KANZAKI Hiroshi

31 81 - 81 2006.3

Structure elucidation of a novel β-N-acetylglucosaminidase inhibitor HU-1

USUKI Hirokazu, NITODA Teruhiko, YAMAJI Nahoko, IWASHITA Takashi, KOMURA Hajime, KANZAKI Hiroshi

31 82 - 82 2006.3

抗がん活性化合物の酵素合成

神崎浩

ケミカルエンジニアリング 50, 902-906 2005

2D15-5 Synthesis of novel fluoro analogs of albonoursin by precursor-directed biosynthesis

KANZAKI Hiroshi, TAKEDA Chikahiro, FUKATANI Yoshimi, NITODA Teruhiko

17 135 - 135 2005

2J13-4 Thionation of a cell cycle inhibitor dehydrophenylahistin

KANZAKI Hiroshi, IKEDA Banri, TAMURA Takashi, NITODA Teruhiko

16 237 - 237 2004

デヒドロアミノ酸残基を含む生理活性環状ジペプチド類

神崎浩

生物工学会誌 81, 396-399 ( 9 ) 396 - 399 2003

Enzymatic synthesis of a cell cycle inhibitor dehydrophenylahistin

Kanzaki Hiroshi, Ikeda Banri, Morimoto Atsushi, Nitoda Teruhiko

15 60 - 60 2003

Chemical information-guided enzymatic synthesis of bioactive compounds

KANZAKI Hiroshi

Nippon Nōgeikagaku Kaishi 76, 539-541 ( 6 ) 539 - 541 2002

環状ジペプチド脱水素酵素で新規生理活性物質を作る

神崎浩

バイオサイエンスとインダストリー 60, 26-29 2002

649 Purification and characterization of dipeptidase from a cyclic dipeptide-assimilating bacterium

Kanzaki Hiroshi, Miyoshi Kazuyuki, Nitoda Teruhiko

14 107 - 107 2002

1 Production of Bioactive Compounds by Biosynthetic Enzymes of Dehydro Cyclic Dipeptides

Kanzaki Hiroshi, Yanagisawa Satohiro, Akazawa Kazumi, Ikeda Banri, Morimoto Atsushi, Nitoda Teruhiko

( 43 ) 1 - 5 2001.9

Language：Japanese Publisher：Symposium on the chemistry of natural products

Cyclic dipeptides (CDPs, diketopiperazines) and their derivatives are widely distributed in nature as secondary metabolites. Although some of dehydro-CDPs are known as cell cycle inhibitors, their effective syntheses have not been reported. We found that Streptomyces albulus KO23, an albonoursin-producing actinomycete, had a biosynthetic pathway from cyclo (Leu-Phe) to albonoursin, cyclo (ΔLeu-ΔPhe) by the fed-batch culture and the resting-cell experiments. And this enzyme activity was found to be effectively extracted in the cell-free extract of this actinomycete. This is the first report for the dehydrogenation of amino acid residues at α,β-positions in CDPs. Furthermore, this enzyme system enables us to synthesize several didehydro- and tetradehydro-CDPs from the corresponding CDPs. Among dehydro-CDPs prepared, the tetradehydro-CDPs exhibited cytotoxicity, while the didehydro-CDPs had no activity, indicating that dehydrogenation at α,β-positions of both amino acid residues in CDPs is required for cytotoxicity. Based on the above results, we speculated that a tetradehydro-CDP prepared from a didehydro-CDP exhibiting cytotoxicity might be a potent cytotoxic compound. Dehydrophenylahistin synthesized by this enzyme system from (-)-phenylahistin, which was recently reported to be a new cell cycle inhibitor, exhibited 1000 times higher inhibitory activity toward the first cleavage of sea urchin embryo than (-)-phenylahistin, and thus, would be a promising lead compound for antitumor agents.

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Production of Bioactive Compounds by Microbial Diketopiperazine-Metabolizing Enzymes

KANZAKI HIROSHI

79(3), 71-77 ( 3 ) 71 - 77 2001

Language：Japanese

iketopiperazines(DKPs)and their derivatives are widely distributed in nature as secondary metabolites.Although some dehydroDKPs are known as cell cycle inhibitors, their effective synthesis has not been reported. We found that the cell-free extract from an albonoursin-producing actinomycete, Streptomyces albulus KO23, catalyzed the conversion of cyclo(Leu-Phe)to albonoursin. This is the first report on the dehydrogenation of amino acid residues at the α, β-positions in DKPs. Furthermore, this enzyme system enabled us to synthesize several didehydro- and tetradehydro- DKPs from the corresponding DKPs. Among the dehydroDKPs prepared, dehydrophenylahistin from (-)-phenylahistin, which was recently reported to be a new cell cycle inhibitor, exhibited 1000 times higher inhibitory activity toward the first clevage of sea urchin embrvo than (-)-phenylahistin, and would thus be a promising lead compound for antitumor agents. Agrobacterium radiobacter NM 5-3 isolated from soil hydrolyzed CGL to from dipeptides(i.e., Leu-Gly and Gly-Leu)and amino acids(i.e., Leu and Gly). This CGL hydrolysis was catalyzed by two distinct enzymes, CGLase and dipeptidase, which were separated by anion-exchange column chromatography. The CGLase was found to catalyze the hydrolysis of CGDL, CGG, CAG, and CDAG. On the other hand, the dipeptidase exhibited L-specific substrate specificity.

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Other Link： http://dl.ndl.go.jp/info:ndljp/pid/10513850

Effective production of dehydro cyclic dipeptide albonoursin exhibiting pronuclear fusion inhibitory activity II. Biosynthetic and bioconversion studies

Hiroshi Kanzaki, Daisuke Imura, Teruhiko Nitoda, Kazuyoshi Kawazu

Journal of Antibiotics 53 ( 1 ) 58 - 62 2000

Language：English Publisher：Japan Antibiotics Research Association

Albornoursin production was greatly enhanced when cycle (r-Leu-L-Phe) (CFL), a tetrahydro derivative of albonoursin, was added to the 2-day culture of an albonoursin-producing actinomycete, Streptomyces albulus KO-23. The increase in albonoursin production paralleled the amount of CFL added. Furthermore, the resting cells of the strain catalyzed the bioconversion of CFL to albonoursin. The optimum pH and temperature for the conversion were found to be pH 10.0 and 50°C. The feeding experiments and the resting-cell reactions revealed that albonoursin is biosynthesized by dehydrogenation of CFL in the actinomycete. This is the first report for a dehydrogenation of amino acid residues at the α,β-positions in cyclic dipeptides.

DOI： 10.7164/antibiotics.53.58

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A novel microbial enzyme system for hydrolyzing a cyclic dipeptide, cyclo(Gly-Leu)

Kanzaki Hiroshi, Miyoshi Kazuyuki, Mizuta Naoki, Nitoda Teruhiko

12 210 - 210 2000

Improved bioassay method for Spodoptera litura chitinase inhibitors using a colloidal chitin powder with a uniform particle size as substrate

T Nitoda, H Kurumatani, H Kanzaki, K Kawazu

PESTICIDE SCIENCE 55 ( 5 ) 563 - 565 1999.5

Language：English Publisher：JOHN WILEY & SONS LTD

A previously reported bioassay method for Spodoptera litura chitinase inhibitors has been improved by use of colloidal chitin powder with a uniform particle size. This improvement made the assay four times more sensitive. Detection of three active supernatants by screening of supernatants and cell extracts from 135 fermentation broths has proved the efficiency of this improved method. (C) 1999 Society of Chemical Industry.

DOI： 10.1002/(SICI)1096-9063(199905)55:5<563::AID-PS972>3.0.CO;2-#

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Enzymatic dehydrogenation of cyclo(L-Phe-L-Leu) to a bioactive derivative, albonoursin

H Kanzaki, D Imura, T Nitoda, K Kawazu

JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC 6 ( 3 ) 265 - 270 1999.3

Language：English Publisher：ELSEVIER SCIENCE BV

The cell-free extract of Streptomyces sp. KO-2388, an albonoursin-producing strain, was found to catalyze the conversion of cyclo(L-Phe-L-Leu) to albonoursin. The conversion activity was simply determined by measuring the increase in ultraviolet (UV) absorption of the reaction mixture at 317 nm, lambda(max) (epsilon 25,400) of albonoursin, where cyclo(L-Phe-L-Leu) had no absorption. The optimum pH and temperature of this bioconversion using the cell-free extract were determined to be pH 8.0-9.5 and 60 degrees C, respectively. Under the optimum conditions, 620 mg/l of albonoursin was obtained with a conversion ratio of 62% after 24 h incubation. (C) 1999 Elsevier Science B.V. All rights reserved.

DOI： 10.1016/S1381-1177(98)00079-4

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Inhibition of plant transformation by phytolaccoside b from phytolacca americana callus

Hiroshi Kanzaki, Toshihiko Kagemori, Yoko Yamachika, Teruhiko Nitoda, Kazuyoshi Kawazu

Bioscience, Biotechnology and Biochemistry 63 ( 9 ) 1657 - 1659 1999.1

Language：English

The newly established GUS expression bioassay on the callus extracts of 22 species of plants revealed that the methanol extract of Phytolacca americana callus had the most potent inhibitory activity against agrobacterial plant transformation. A triterpene glycoside phytolaccoside B was isolated from the extract as a genuine plant transformation inhibitor having neither antiagrobacterial nor phytotoxic activity. This compound is promising for use as a biochemical probe for studies on the plant transformation mechanism. © 1999, Taylor &amp
Francis Group, LLC. All rights reserved.

DOI： 10.1271/bbb.63.1657

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