Purification and Characterization of NfrA1,a Bacillus subtilis Nitro/flavin Reductase Capable of Interacting with the Bacterial Luciferase

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概要

• 論文の詳細を見る

• ipa-43d is a hypothetical gene identified by the Bacillus subtilis genome project (Mol. Microbiol. 10,371-384 1993 ; Nature 390,249-256 1997). The ipa-43d protein overexpressed in E. coli was purified to homogeneity and its properties were analyzed biochemically. The ipa-43d protein was found to be tightly associated with FMN and to be capable of reducing both nitrofurazone and FMN effectively. Although the ipa-43d protein catalysis obeys the ping-pong Bi-Bi mechanism, catalysis mode was changed to the sequential mechanism upon coupling with the bioluminescent reaction. Database search showed that B. subtilis possessed four genes (ipa-44d, ytmO, yddN, and yvbT), encoding proteins similar in amino acid sequence to LuxA and LuxB of Photobacterium fischeri, and, in particular, ipa-44d is immediately adjacent to the ipa-43d gene on the chromosome.

• 社団法人日本農芸化学会の論文
• 1998-10-23

著者

• SAIGO Kaoru

  Department of Biochemistry, Kyushu University School of Medicine

• TANOKURA Masaru

  Biotechnology Research Center, The University of Tokyo

• Tanokura M

  Univ. Tokyo Tokyo Jpn

• Tanokura Masaru

  Department Of Applied Biological Chemistry Graduate School Of Agricultural And Life Sciences The Uni

• Saigo Kaoru

  Department Of Biophysics And Biochemistry Graduate School Of Science

• Kobori Toshiro

  Biotechnology Research Center University Of Tokyo

• Miyakawa Takuya

  Department Of Applied Biological Chemistry Graduate School Of Agricultural And Life Sciences Univers

• Tanokura Masaru

  Biotechnology Research Center The University Of Tokyo

• ZENNO Shuhei

  Department of Biophysics and Biochemistry, Graduate School of Science

• Zenno Shuhei

  Department Of Biophysics And Biochemistry Graduate School Of Science

• SAIGO Kaoru

  Department Biochemistry, Kyushu University 60 School of Medicine

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