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Bifunctional Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase (CODH/ACS)

Introduction

Structure

The CODH/ACS enzyme from M. thermoacetica is an α2β2 tetramer. Each β subunit (residues 2 to 674) carries out CODH activity, while each α subunit(residues 2 to 729) is responsible for ACS activity. The β subunit has 57% helical and 9% β-sheet character with 31 helices and 15 β-strands. The α subunit is comprised of three domains, two with α+β folds and a third with a helical region at the NH2-terminus of a Rossmann fold which is similar to a portion of the β subunit structure ^[1]. Overall, the α subunit has 50% helical and 14% β-sheet character with 36 helices and 22 β-strands.

Mechanism of Action

Possible Applications

References

1. ↑ Doukov TI, Iverson TM, Seravalli J, Ragsdale SW, Drennan CL. A Ni-Fe-Cu center in a bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase. Science. 2002 Oct 18;298(5593):567-72. PMID:12386327 doi:10.1126/science.1075843