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Acetyl-CoA decarbonylase/synthase complex from Archaeoglobus fulgidus

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Abstract

The acetyl-CoA decarbonylase/synthase (ACDS) multienzyme complex catalyzes the reversible cleavage and synthesis of acetyl-CoA in methanogens. This report of the enzyme complex in Archaeoglobus fulgidus demonstrates the existence of a functional ACDS complex in an organism that is not a methanogen. The A. fulgidus enzyme complex contained five subunits of 89, 72, 50, 49.5, and 18.5 kDa, and it catalyzed the overall synthesis of acetyl-CoA according to the following reaction:

w CO2 + 2 Fdred(Fe2+) + 2 H+ + CH3– H4SPt + CoA ⇌ acetyl-CoA + H4SPt + 2 Fdox(Fe3+) + H2O

where Fd is ferredoxin, and CH3–H4SPt and H4SPt denote N 5-methyl-tetrahydrosarcinapterin and tetrahydrosarcinapterin, respectively.

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Received: 27 October 1997 / Accepted: 29 January 1998

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Dai, YR., Reed, D., Millstein, J. et al. Acetyl-CoA decarbonylase/synthase complex from Archaeoglobus fulgidus. Arch Microbiol 169, 525–529 (1998). https://doi.org/10.1007/s002030050606

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  • DOI: https://doi.org/10.1007/s002030050606

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