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Pyruvate Formate-Lyase Enables Efficient Growth of Escherichia coli on Acetate and Formate.
Zelcbuch, Lior; Lindner, Steffen N; Zegman, Yonatan; Vainberg Slutskin, Ilya; Antonovsky, Niv; Gleizer, Shmuel; Milo, Ron; Bar-Even, Arren.
Afiliação
  • Zelcbuch L; Department of Plant and Environmental Sciences, Weizmann Institute of Science , Rehovot 76100, Israel.
  • Lindner SN; Max Planck Institute of Molecular Plant Physiology , Am Mühlenberg 1, 14476 Potsdam-Golm, Germany.
  • Zegman Y; Department of Plant and Environmental Sciences, Weizmann Institute of Science , Rehovot 76100, Israel.
  • Vainberg Slutskin I; Department of Plant and Environmental Sciences, Weizmann Institute of Science , Rehovot 76100, Israel.
  • Antonovsky N; Department of Plant and Environmental Sciences, Weizmann Institute of Science , Rehovot 76100, Israel.
  • Gleizer S; Department of Plant and Environmental Sciences, Weizmann Institute of Science , Rehovot 76100, Israel.
  • Milo R; Department of Plant and Environmental Sciences, Weizmann Institute of Science , Rehovot 76100, Israel.
  • Bar-Even A; Max Planck Institute of Molecular Plant Physiology , Am Mühlenberg 1, 14476 Potsdam-Golm, Germany.
Biochemistry ; 55(17): 2423-6, 2016 05 03.
Article em En | MEDLINE | ID: mdl-27093333
ABSTRACT
Pyruvate formate-lyase (PFL) is a ubiquitous enzyme that supports increased ATP yield during sugar fermentation. While the PFL reaction is known to be reversible in vitro, the ability of PFL to support microbial growth by condensing acetyl-CoA and formate in vivo has never been directly tested. Here, we employ Escherichia coli mutant strains that cannot assimilate acetate via the glyoxylate shunt and use carbon labeling experiments to unequivocally demonstrate PFL-dependent co-assimilation of acetate and formate. Moreover, PFL-dependent growth is faster than growth on acetate using the glyoxylate shunt. Hence, growth via the reverse activity of PFL could have substantial ecological and biotechnological significance.
Assuntos

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Acetilcoenzima A / Acetiltransferases / Proteínas de Escherichia coli / Escherichia coli / Formiatos / Acetatos Idioma: En Ano de publicação: 2016 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Acetilcoenzima A / Acetiltransferases / Proteínas de Escherichia coli / Escherichia coli / Formiatos / Acetatos Idioma: En Ano de publicação: 2016 Tipo de documento: Article