EC Number   |
General Information |
Reference |
|---|
    2.3.1.169 | evolution |
comparison of bifunctional CO dehydrogenase/acetyl-CoA synthase enzyme from anaerobic bacteria and of the acetyl-CoA decarbonylase/synthase (ACDS) multienzyme complex from Archaea, and of the role of the ACS N-terminal domain in promoting acetyl C-C bond fragmentation at the A cluster, overview |
-, 719862 |
| 2.3.1.169 | evolution |
phylogenomic study of monoxide dehydrogenase/acetyl-CoA synthase (CODH/ACS) in over 6400 archaeal and bacterial genomes. The CODH/ACS complex displays astounding conservation and vertical inheritance over geological times. Rare intradomain and interdomain transfer events might tie into important functional transitions, including the acquisition of CODH/ACS in some archaeal methanogens not known to fix carbon, the tinkering of the complex in a clade of model bacterial acetogens, or emergence of archaeal-bacterial hybrid complexes. Presence of a CODH/ACS complex with at least four subunits in the last universal common ancestor. Different scenarios on the possible role of ancestral CODH/ACS are discussed |
758239 |
| 2.3.1.169 | evolution |
phylogenomic study of monoxide dehydrogenase/acetyl-CoA synthase (CODH/ACS) in over 6400 archaeal and bacterial genomes. The CODH/ACS complex displays astounding conservation and vertical inheritance over geological times. Rare intradomain and interdomain transferevents might tie into important functional transitions, including the acquisition of CODH/ACS in some archaeal methanogens not known to fix carbon, the tinkering of the complex in a clade of model bacterial acetogens, or emergence of archaeal-bacterial hybrid complexes. Presence of a CODH/ACS complex with at least four subunits in the last universal common ancestor. Different scenarios on the possible role of ancestral CODH/ACS are discussed |
758239 |
| 2.3.1.169 | malfunction |
in the ACSChDLETAN truncation mutant, the Km value is decreased to about one-seventh of its value in the full-length protein, and the Vmax value is increased by a factor of around 4.4. Overall, the Vmax/Km ratio increases by around 30fold, indicating an apparent unmasking of the intrinsic catalytic efficiency for overall synthesis of acetyl-CoA. Changes in the kinetics of acetyl-CoA synthesis are possibly due to differences in CO accessibility to the A cluster in different forms of the enzyme |
-, 719862 |
| 2.3.1.169 | metabolism |
carbon monoxide dehydrogenase/acetyl-CoA synthase (CODH/ACS) is a five-subunit enzyme complex responsible for the carbonyl branch of the Wood-Ljungdahl (WL) pathway, considered one of the most ancient metabolisms for anaerobic carbon fixation |
758239 |
| 2.3.1.169 | metabolism |
expression of the Cdh1- and Cdh2-encoding genes is regulated differentially in response to growth phase and to changing substrate conditions. CdhA3 clearly affects expression of cdh1, suggesting that it functions in signal perception and transduction rather than in catabolism |
719744 |
| 2.3.1.169 | more |
bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase, the different active sites of this bifunctional enzyme complex are connected via a channel, 138 angstroms long, that provides a conduit for carbon monoxide generated at the C-cluster on one subunit to be incorporated into acetyl-CoA at the A-cluster on the other subunit. The enzyme catalyzes two different reactions. The C-cluster in the CODH subunit generates CO from CO2, while the A-cluster of the ACS subunit combines the CO with CoA and a methyl group to form acetyl-CoA |
644679 |
| 2.3.1.169 | more |
open and closed conformations of ACS, overview |
-, 719862 |
| 2.3.1.169 | physiological function |
acetyl-CoA synthase, ACS, a subunit of the bifunctional CO dehydrogenase/acetyl-CoA synthase, CODH/ACS, complex of Moorella thermoacetica requires reductive activation in order to catalyze acetyl-CoA synthesis and related partial reactions, including the CO/acetyl-CoA exchange reaction |
714240 |
| 2.3.1.169 | physiological function |
CODH/ACS is the only protein required to catalyze exchange of the carbonyl group of acetyl-CoA with free CO. CODH/ACS acts on both the acetyl C-C and C-S bonds in acetyl-CoA, and it identified CODH/ACS as the condensing enzyme that catalyzes the final steps in acetyl-CoA synthesis in acetogenic bacteria |
720372 |
