FrsA functions as a cofactor-independent decarboxylase to control metabolic flux

Kyung Jo Lee, Chang Sook Jeong, Young Jun An, Hyun Jung Lee, Soon Jung Park, Yeong Jae Seok, Pil Kim, Jung Hyun Lee, Kyu Ho Lee, Sun Shin Cha

Research output: Contribution to journalArticlepeer-review

21 Scopus citations

Abstract

The interaction between fermentation-respiration switch (FrsA) protein and glucose-specific enzyme IIAGlc increases glucose fermentation under oxygen-limited conditions. We show that FrsA converts pyruvate to acetaldehyde and carbon dioxide in a cofactor-independent manner and that its pyruvate decarboxylation activity is enhanced by the dephosphorylated form of IIA Glc (d-IIA Glc). Crystal structures of FrsA and its complex with d-IIAGlc revealed residues required for catalysis as well as the structural basis for the activation by d-IIAGlc.

Original languageEnglish
Pages (from-to)434-436
Number of pages3
JournalNature Chemical Biology
Volume7
Issue number7
DOIs
StatePublished - Jun 2011

Bibliographical note

Funding Information:
We are grateful to Y.J. Lee, H.S. Lee, S.J. Chung and J.K. Lee for comments on the manuscript. This work was supported by the Marine and Extreme Genome Research Center program of Ministry of Land, Transport and Maritime Affairs, the Midcareer Researcher Program through National Research Foundation grant funded by the Ministry of Education, Science and Technology (20090092822), a KORDI inhouse program (PE98513) and the Development of Biohydrogen Production Technology Using Hyperthermophilic Archaea program of Ministry of Land, Transport and Maritime Affairs.

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