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Peer-Reviewed Publication
Biochimie2024;21912-20.April 1, 2024Journal Article

Dynamic lid domain of Chloroflexus aurantiacus Malonyl-CoA reductase controls the reaction.

Burak V Kabasakal1, Charles A R Cotton2, James W Murray3
1Department of Life Sciences, Imperial College, Exhibition Road, London, SW7 2AZ, UK; Turkish Accelerator and Radiation Laboratory, Gölbaşı, 06830, Ankara, Turkiye.
2Department of Life Sciences, Imperial College, Exhibition Road, London, SW7 2AZ, UK; Cambrium GmbH, Max-Urich-Strasse 3, 13355, Berlin, Germany.
3Department of Life Sciences, Imperial College, Exhibition Road, London, SW7 2AZ, UK. Electronic address: j.w.murray@imperial.ac.uk.
PubMed DOI

Abstract

Malonyl-Coenzyme A Reductase (MCR) in Chloroflexus aurantiacus, a characteristic enzyme of the 3-hydroxypropionate (3-HP) cycle, catalyses the reduction of malonyl-CoA to 3-HP. MCR is a bi-functional enzyme; in the first step, malonyl-CoA is reduced to the free intermediate malonate semialdehyde by the C-terminal region of MCR, and this is further reduced to 3-HP by the N-terminal region of MCR. H…

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