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Constitutive expression of phosphoketolase, a key enzyme for metabolic shift from homo- to heterolactic fermentation in Enterococcus mundtii QU 25.
Nabeta, Keisuke; Watanabe, Satoru; Chibazakura, Taku; Zendo, Takeshi; Sonomoto, Kenji; Shimizu-Kadota, Mariko; Yoshikawa, Hirofumi.
Affiliation
  • Nabeta K; Department of Bioscience, Tokyo University of Agriculture, 1-1-1 Sakuragaoka, Setagaya-ku, Tokyo 156-8502, Japan.
  • Watanabe S; Department of Bioscience, Tokyo University of Agriculture, 1-1-1 Sakuragaoka, Setagaya-ku, Tokyo 156-8502, Japan.
  • Chibazakura T; Department of Bioscience, Tokyo University of Agriculture, 1-1-1 Sakuragaoka, Setagaya-ku, Tokyo 156-8502, Japan.
  • Zendo T; Laboratory of Microbial Technology, Division of Systems Bioengineering, Department of Bioscience and Biotechnology, Faculty of Agriculture, Graduate School, Kyushu University, 744 Motooka, Nishi-ku, Fukuoka 819-0395, Japan.
  • Sonomoto K; Laboratory of Microbial Technology, Division of Systems Bioengineering, Department of Bioscience and Biotechnology, Faculty of Agriculture, Graduate School, Kyushu University, 744 Motooka, Nishi-ku, Fukuoka 819-0395, Japan.
  • Shimizu-Kadota M; Department of Environmental Systems Sciences, Musashino University, 3-3-3 Ariake, Koto-ku, Tokyo 135-8181, Japan.
  • Yoshikawa H; Department of Bioscience, Tokyo University of Agriculture, 1-1-1 Sakuragaoka, Setagaya-ku, Tokyo 156-8502, Japan.
Biosci Microbiota Food Health ; 38(3): 111-114, 2019.
Article de En | MEDLINE | ID: mdl-31384523
ABSTRACT
Phosphoketolase (PK) is responsible for heterolactic fermentation; however, the PK gene of Enterococcus mundtii QU 25, xfpA, is transcribed constitutively, even under homolactic fermentation conditions. In order to deduce the regulatory mechanisms of PK activity in QU 25, XfpA levels in QU 25 cells under hetero- and homolactic fermentation conditions were tested using western blotting. The results showed that the XfpA protein expression was similar under both conditions and that the expression products formed complexes, most likely homodimers, indicating that the regulation of PK activity is downstream of translation.
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Texte intégral: 1 Collection: 01-internacional Base de données: MEDLINE Langue: En Journal: Biosci Microbiota Food Health Année: 2019 Type de document: Article Pays d'affiliation: Japon

Texte intégral: 1 Collection: 01-internacional Base de données: MEDLINE Langue: En Journal: Biosci Microbiota Food Health Année: 2019 Type de document: Article Pays d'affiliation: Japon