Chitose Maruyama

Fukui Prefectural University

Author Statistics

Papers

Citation

H-Index

i-10 index

Research Trends

Author Order

Document Type

Co-Authors

Yoshimitsu Hamano

Fukui Prefectural University

Hajime Katano

Fukui Prefectural University

Tohru Dairi

Hokkaido University

Yasushi Ogasawara

Hokkaido University

Kazuya Yamanaka

Kansai University

Kazuo Shin‐ya

National Institute of Advanced Industrial Science and Technology

Kohei Uematsu

Fukui Prefectural University

Yasuharu Satoh

Hokkaido University

Shohei Hayashi

Shimane University

Yamato Takeuchi

Fukui Prefectural University

Cooperative Institutions

Fukui Prefectural University

Hokkaido University

Kyoto University

Osaka University

The University of Tokyo

Tokyo Institute of Technology

Tohoku University

National Institute of Advanced Industrial Science and Technology

Genomics Research Center, Academia Sinica

National Yang Ming Chiao Tung University

Author Statistics

Papers

Citation

H-Index

i-10 index

Research Field

The Assembly-Line Enzymology of Nonribosomal Peptide Biosynthesis

Methods in molecular biology (2023)

Chitose Maruyama Yoshimitsu Hamano

Nonribosomal peptide

Adenylylation

Thioesterase

Assembly line

Peptide Biosynthesis

10.1007/978-1-0716-3214-7_1

Cite

Citations (4)

Mutational analysis of the three tandem domains of ε-poly-l-lysine synthetase catalyzing the l-lysine polymerization reaction

Journal of Bioscience and Bioengineering (2012)

Naoko Kito Chitose Maruyama Kazuya Yamanaka Yuuki Imokawa Takashi Utagawa

Nonribosomal peptide

Tandem

10.1016/j.jbiosc.2012.11.020

Cite

Citations (14)

Construction of a Knockout Mutant of the Streptothricin-Resistance Gene in Streptomyces albulus by Electroporation

Actinomycetologica (2006)

Yoshimitsu Hamano Chitose Maruyama Hisashi Kimoto

Streptothricins (STs) produced by Streptomyces strains are broad-spectrum antibiotics. All STs consist of a carbamoylated D-gulosamine to which the β-lysine homopolymer (1 to 7 residues) and the amide form of the unusual amino acid streptolidine (streptolidine lactam) are attached. In a previous study, we successfully isolated a novel ST-resistance gene (sttH) from Streptomyces albulus by shotgun cloning with a heterologous host. In vitro analysis of SttH demonstrated that this enzyme catalyzes the hydrolysis of the amide bond of streptolidine lactam, thereby conferring ST resistance. We suggested that the true role of SttH may not be its involvement in resistance against STs; instead, it may catalyze the hydrolysis of naturally occurring cyclic amide compounds in the metabolism of S. albulus. In this study, we therefore constructed an sttH gene-knockout mutant to better understand the true biological role of SttH in S. albulus and to clarify whether or not S. albulus possesses different ST-resistance gene(s). The minimum inhibitory concentration MIC of STs in the sttH gene-knockout mutant was determined to be 6.25 μg/ml, whereas the MIC of STs in the S. albulus wild strain was determined to be >400 μg/ml. This result clearly demonstrated that sttH is the sole gene responsible for ST resistance in the S. albulus strain. Moreover, we developed a transformation system for S. albulus by electroporation in this study.

Gene knockout

Streptomyces albus

Streptomycetaceae

10.3209/saj.20.35

Cite

Citations (9)

Separation and Purification of ε-Poly-l-lysine with Its Colorimetric Determination Using Dipicrylamine

Analytical Sciences (2015)

Hajime Katano Yoshihiro Kasahara Kazunori Ushimaru Chitose Maruyama Yoshimitsu Hamano

A separation method for a biopolymer, ε-poly-L-lysine (εPL), with its colorimetric determination using a yellow anionic dye, dipicrylamine anion (DPA(-)), is presented. The εPL-producing culture broth was mixed with a NaDPA solution to precipitate the εPL in polycationic form with the DPA(-) anion. The precipitate was dissolved into acetonitrile (AN). The AN solution was yellowish, and gave an absorption maximum at around 420 nm. Thus, εPL in the culture broth can be assayed colorimetrically a with multiwell microtiter plate. By the addition of bis(triphenylphosphoranylidene)ammonium chloride, the polycationic εPL was precipitated from the AN solution as the hydrochloride salt. On the other hand, the DPA(-) anion remained in the AN solution as the quaternary ammonium salt. Thus, εPL larger than tetramer can be separated and purified after the high-throughput screening of the synthetic enzyme.

Colorimetry

10.2116/analsci.31.1273

Cite

Citations (11)

[Highly unusual non-ribosomal peptide synthetase producing an amino-acid homopolymer].

PubMed (2009)

Yoshimitsu Hamano Kazuya Yamanaka Chitose Maruyama Hiroshi Takagi

Source

Cite

Citations (0)

ε-Poly-L-lysine dispersity is controlled by a highly unusual nonribosomal peptide synthetase

Nature Chemical Biology (2008)

Kazuya Yamanaka Chitose Maruyama Hiroshi Takagi Yoshimitsu Hamano

Nonribosomal peptide

Adenylylation

10.1038/nchembio.125

Cite

Citations (155)

3P-261 Functional analysis of the antibiotic BD-12 biosynthetic genes

日本生物工学会大会講演要旨集 (2015)

Haruka Niikura Chitose Maruyama Miho Izumikawa Jun Ishikawa Haruo Ikeda

Source

Cite

Citations (0)

Voltammetric study of the transfer of ε-poly-L-lysine at nitrobenzene | water interface

Journal of Electroanalytical Chemistry (2014)

Kohei Uematsu Yuto Minami Chitose Maruyama Yoshimitsu Hamano Hajime Katano

Nitrobenzene

Interface (matter)

ITIES

10.1016/j.jelechem.2014.02.015

Cite

Citations (7)

Control Mechanism for cis Double‐Bond Formation by Polyunsaturated Fatty‐Acid Synthases

Angewandte Chemie (2019)

Shohei Hayashi Yasuharu Satoh Yasushi Ogasawara Chitose Maruyama Yoshimitsu Hamano

Abstract Polyunsaturated fatty acids (PUFAs) such as docosahexaenoic acid (DHA), eicosapentaenoic acid (EPA), and arachidonic acid (ARA) are essential fatty acids for humans. Some microorganisms biosynthesize these PUFAs through PUFA synthases composed of four subunits with multiple catalytic domains. These PUFA synthases each create a specific PUFA without undesirable byproducts, even though the multiple catalytic domains in each large subunit are very similar. However, the detailed biosynthetic pathways and mechanisms for controlling final‐product profiles are still obscure. In this study, the FabA‐type dehydratase domain (DH FabA ) in the C‐subunit and the polyketide synthase‐type dehydratase domain (DH PKS ) in the B‐subunit of ARA synthase were revealed to be essential for ARA biosynthesis by in vivo gene exchange assays. Furthermore, in vitro analysis with truncated recombinant enzymes and C 4 ‐ to C 8 ‐acyl ACP substrates showed that ARA and EPA synthases utilized two types of DH domains, DH PKS and DH FabA , depending on the carbon‐chain length, to introduce either saturation or cis double bonds to growing acyl chains.

10.1002/ange.201812623

Cite

Citations (3)

Bioavailability of Tauropine After Oral Ingestion in Mouse

Advances in experimental medicine and biology (2022)

Takashi Ito Khanh Hoang Nguyen Chitose Maruyama Yoshimitsu Hamano Shigeru Murakami

10.1007/978-3-030-93337-1_13

Cite

Citations (0)