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Characterization of a cryptic, pyrroloquinoline quinone-dependent dehydrogenase of Gluconobacter sp. strain CHM43.
Nguyen, Thuy Minh; Naoki, Kotone; Kataoka, Naoya; Matsutani, Minenosuke; Ano, Yoshitaka; Adachi, Osao; Matsushita, Kazunobu; Yakushi, Toshiharu.
Afiliação
  • Nguyen TM; Graduate School of Science and Technology for Innovation, Yamaguchi University, Yamaguchi, Japan.
  • Naoki K; Graduate School of Science and Technology for Innovation, Yamaguchi University, Yamaguchi, Japan.
  • Kataoka N; Graduate School of Science and Technology for Innovation, Yamaguchi University, Yamaguchi, Japan.
  • Matsutani M; Faculty of Agriculture, Yamaguchi University, Yamaguchi, Japan.
  • Ano Y; Research Center for Thermotolerant Microbial Resources, Yamaguchi University, Yamaguchi, Japan.
  • Adachi O; Graduate School of Science and Technology for Innovation, Yamaguchi University, Yamaguchi, Japan.
  • Matsushita K; Graduate School of Agriculture, Ehime University, Matsuyama, Japan.
  • Yakushi T; Graduate School of Science and Technology for Innovation, Yamaguchi University, Yamaguchi, Japan.
Biosci Biotechnol Biochem ; 85(4): 998-1004, 2021 Mar 24.
Article em En | MEDLINE | ID: mdl-33686415
We characterized the pyrroloquinoline quinone (PQQ)-dependent dehydrogenase 9 (PQQ-DH9) of Gluconobacter sp. strain CHM43, which is a homolog of PQQ-dependent glycerol dehydrogenase (GLDH). We used a plasmid construct to express PQQ-DH9. The expression host was a derivative strain of CHM43, which lacked the genes for GLDH and the membrane-bound alcohol dehydrogenase and consequently had minimal ability to oxidize primary and secondary alcohols. The membranes of the transformant exhibited considerable d-arabitol dehydrogenase activity, whereas the reference strain did not, even if it had PQQ-DH9-encoding genes in the chromosome and harbored the empty vector. This suggests that PQQ-DH9 is not expressed in the genome. The activities of the membranes containing PQQ-DH9 and GLDH suggested that similar to GLDH, PQQ-DH9 oxidized a wide variety of secondary alcohols but had higher Michaelis constants than GLDH with regard to linear substrates such as glycerol. Cyclic substrates such as cis-1,2-cyclohexanediol were readily oxidized by PQQ-DH9.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Oxirredutases / Gluconobacter / Cofator PQQ Idioma: En Ano de publicação: 2021 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Oxirredutases / Gluconobacter / Cofator PQQ Idioma: En Ano de publicação: 2021 Tipo de documento: Article