Sandbox Reserved 496

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== '''Bifunctional Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase (CODH/ACS)''' ==
== '''Bifunctional Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase (CODH/ACS)''' ==
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<Structure load='1mjg' size='500' frame='true' align='right' caption='Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase' scene='Insert optional scene name here' />
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<Structure load='1mjg' size='400' frame='true' align='right' caption='Carbon monoxide dehydrogenase/acetyl-CoA synthase asymmetric unit containing two α2β2 tetramers.' scene='Insert optional scene name here' />
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==='''Structure'''===
==='''Structure'''===
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The CODH/ACS enzyme from M. thermoacetica is an α2β2 tetramer. The β subunit containing chains A, B, C, and D (residues ) carries out CODH activity, while the α subunit containing chains is responsible for ACS activity.
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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.
==='''Mechanism of Action'''===
==='''Mechanism of Action'''===

Revision as of 21:34, 1 May 2012

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This Sandbox is Reserved from 13/03/2012, through 01/06/2012 for use in the course "Proteins and Molecular Mechanisms" taught by Robert B. Rose at the North Carolina State University, Raleigh, NC USA. This reservation includes Sandbox Reserved 451 through Sandbox Reserved 500.
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Contents

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

Carbon monoxide dehydrogenase/acetyl-CoA synthase asymmetric unit containing two α2β2 tetramers.

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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.

Mechanism of Action


Possible Applications


References
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