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

doi:10.1038/nchembio.589

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

Department of Chemistry & Nanoscience

Research output: Contribution to journal › Article › peer-review

22 Scopus citations

Abstract

The interaction between fermentation-respiration switch (FrsA) protein and glucose-specific enzyme IIA^Glc 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-IIA^Glc revealed residues required for catalysis as well as the structural basis for the activation by d-IIA^Glc.

Original language	English
Pages (from-to)	434-436
Number of pages	3
Journal	Nature Chemical Biology
Volume	7
Issue number	7
DOIs	https://doi.org/10.1038/nchembio.589
State	Published - 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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title = "FrsA functions as a cofactor-independent decarboxylase to control metabolic flux",

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.",

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

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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AU - Lee, Kyung Jo

AU - Jeong, Chang Sook

AU - An, Young Jun

AU - Lee, Hyun Jung

AU - Park, Soon Jung

AU - Seok, Yeong Jae

AU - Kim, Pil

AU - Lee, Jung Hyun

AU - Lee, Kyu Ho

AU - Cha, Sun Shin

N1 - 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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AB - 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.

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JO - Nature Chemical Biology

JF - Nature Chemical Biology

IS - 7

ER -

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

Abstract

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