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Literature summary for 2.3.1.169 extracted from
- Tight coupling of partial reactions in the cc from Methanosarcina thermophila: acetyl C-C bond fragmentation at the a cluster promoted by protein conformational changes (2010), J. Biol. Chem., 285, 15450-15463.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression of ACSD beta in Escherichia coli strain NM522 | Methanosarcina thermophila |
| gene ascB, expression of full-length protein, designated ACSCh732 amino acids, and as a form lacking the 317-amino acid N-terminal domain, designated ACSChDELTAN, 415 amino acids, in Escherichia coli strain NM522 | Carboxydothermus hydrogenoformans |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | kinetics of recombinant ACSCh732 and ACSChDELTAN for acetyl-CoA synthase activity, acetyltransferase activity, and acetyl-CoA/CO exchange activity, overview | Carboxydothermus hydrogenoformans | |
| additional information | - |
additional information | kinetics of recombinant ACSD beta for acetyl-CoA synthase activity, acetyltransferase activity, and acetyl-CoA/CO exchange activity, overview | Methanosarcina thermophila | |
| 0.066 | - |
methylcorrinoid protein | pH 7.2, 25°C, recombinant ACSChDELTAN | Carboxydothermus hydrogenoformans |  |
| 0.087 | - |
CO | pH 7.2, 25°C, recombinant ACSD beta | Methanosarcina thermophila | |
| 0.36 | - |
CO | pH 7.2, 25°C, recombinant ACSChDELTAN | Carboxydothermus hydrogenoformans | |
| 0.46 | - |
methylcorrinoid protein | pH 7.2, 25°C, recombinant ACSCh732 | Carboxydothermus hydrogenoformans | |
| 0.53 | - |
methylcorrinoid protein | pH 7.2, 25°C, recombinant ACSD beta | Methanosarcina thermophila | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Fe2+ | a [Fe4S4] cluster | Methanosarcina thermophila | |
| Fe2+ | Fe/S-containing active site metal center, the A cluster | Carboxydothermus hydrogenoformans | |
| Ni2+ | nickel-containing active site metal center, the A cluster, a binuclear Ni-Ni center bridged by a cysteine thiolate to an [Fe4S4] cluster. Ni2+-CO equatorial coordination environment in closed buried hydrophobic and open solvent-exposed states | Methanosarcina thermophila | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| acetyl-CoA + corrinoid protein | Methanosarcina thermophila | - |
CoA + CO + methylcorrinoid protein | - |
r | |
| acetyl-CoA + corrinoid protein | Carboxydothermus hydrogenoformans | - |
CoA + CO + methylcorrinoid protein | - |
r | |
| acetyl-CoA + corrinoid protein | Carboxydothermus hydrogenoformans DSM 6008 | - |
CoA + CO + methylcorrinoid protein | - |
r | |
| acetyl-CoA + corrinoid protein | Methanosarcina thermophila TM-1 | - |
CoA + CO + methylcorrinoid protein | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Carboxydothermus hydrogenoformans | - |
gene acsB | - |
| Carboxydothermus hydrogenoformans DSM 6008 | - |
gene acsB | - |
| Methanosarcina thermophila | - |
- |
- |
| Methanosarcina thermophila TM-1 | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant ACSCh732 and ACSChDELTAN from Escherichia coli strain NM522 by anion exchange and hydroxyapatite chromatography, followed by another and different step of anion exchange chromatography and by hydrophobic interaction chromatography to 94-95% purity forACSCh and around 98% purity for ACSChDELTAN | Carboxydothermus hydrogenoformans |
| recombinant ACSD beta from Escherichia coli strain NM522 by anion exchange chromatography, followed by hydrophobic interaction chromatography and another and different step of ion exchange of anion exchange chromatography to around 98% purity for ACDS beta | Methanosarcina thermophila |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| acetyl-CoA + a [Co(I) corrinoid Fe-S protein] = CO + CoA + a [methyl-Co(III) corrinoid Fe-S protein] | chemical steps and conformational changes in the mechanism of acetyl-CoA synthase, overview | Methanosarcina thermophila | |
| acetyl-CoA + a [Co(I) corrinoid Fe-S protein] = CO + CoA + a [methyl-Co(III) corrinoid Fe-S protein] | chemical steps and conformational changes in the mechanism of acetyl-CoA synthase, overview | Carboxydothermus hydrogenoformans |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| acetyl-CoA + corrinoid protein | - |
Methanosarcina thermophila | CoA + CO + methylcorrinoid protein | - |
r | |
| acetyl-CoA + corrinoid protein | - |
Carboxydothermus hydrogenoformans | CoA + CO + methylcorrinoid protein | - |
r | |
| acetyl-CoA + corrinoid protein | - |
Carboxydothermus hydrogenoformans DSM 6008 | CoA + CO + methylcorrinoid protein | - |
r | |
| acetyl-CoA + corrinoid protein | - |
Methanosarcina thermophila TM-1 | CoA + CO + methylcorrinoid protein | - |
r | |
| additional information | an Fe/S-containing active site metal center, the A cluster, catalyzes acetyl CC bond formation/breakdown. Carbonyl group exchange of acetyl-CoA with CO is a hallmark of CODH/ACS, coupling analysis of the recombinant A cluster protein of acetyl-CoA synthase of Carboxydothermus hydrogenoformans, ACSCh, and truncated ACSCh lacking its 317-amino acid N-terminal domain, overview | Carboxydothermus hydrogenoformans | ? | - |
? | |
| additional information | an nickel-containing active site metal center, the A cluster, catalyzes acetyl C-C bond formation/breakdown. Carbonyl group exchange of acetyl-CoA with CO is weakly active in ACDS, and exchange with CO2 is up to 350 times faster, indicating tight coupling of CO release at the A cluster to CO oxidation to CO2 at the C cluster in CO dehydrogenase, coupling analysis of the recombinant A cluster protein of ACDS. Direct role of the ACS N-terminal domain in promoting acetyl C-C bond fragmentation. Protein conformational changes, related to open/closed states have direct effects on the coordination geometry and stability of the A cluster Ni2+-acetyl intermediate, controlling Ni2-acetyl fragmentation and Ni2(CO)(CH3) condensation. Involvement of subunit-subunit interactions in ACDS, versus interdomain contacts in ACS, ensures that CO is not released from the ACDS beta-subunit in the absence of appropriate interactions with the alpha2epsilon2 CO dehydrogenase component, ACDS complex partial reactions in the overall synthesis and cleavage of acetyl-CoA, overview | Methanosarcina thermophila | ? | - |
? | |
| additional information | an Fe/S-containing active site metal center, the A cluster, catalyzes acetyl CC bond formation/breakdown. Carbonyl group exchange of acetyl-CoA with CO is a hallmark of CODH/ACS, coupling analysis of the recombinant A cluster protein of acetyl-CoA synthase of Carboxydothermus hydrogenoformans, ACSCh, and truncated ACSCh lacking its 317-amino acid N-terminal domain, overview | Carboxydothermus hydrogenoformans DSM 6008 | ? | - |
? | |
| additional information | an nickel-containing active site metal center, the A cluster, catalyzes acetyl C-C bond formation/breakdown. Carbonyl group exchange of acetyl-CoA with CO is weakly active in ACDS, and exchange with CO2 is up to 350 times faster, indicating tight coupling of CO release at the A cluster to CO oxidation to CO2 at the C cluster in CO dehydrogenase, coupling analysis of the recombinant A cluster protein of ACDS. Direct role of the ACS N-terminal domain in promoting acetyl C-C bond fragmentation. Protein conformational changes, related to open/closed states have direct effects on the coordination geometry and stability of the A cluster Ni2+-acetyl intermediate, controlling Ni2-acetyl fragmentation and Ni2(CO)(CH3) condensation. Involvement of subunit-subunit interactions in ACDS, versus interdomain contacts in ACS, ensures that CO is not released from the ACDS beta-subunit in the absence of appropriate interactions with the alpha2epsilon2 CO dehydrogenase component, ACDS complex partial reactions in the overall synthesis and cleavage of acetyl-CoA, overview | Methanosarcina thermophila TM-1 | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | open and closed conformations of ACS, overview | Methanosarcina thermophila |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ACDS multienzyme complex | - |
Methanosarcina thermophila |
| acetyl-CoA decarbonylase/synthase multienzyme complex | - |
Methanosarcina thermophila |
| CO dehydrogenase/acetyl-CoA synthase | - |
Carboxydothermus hydrogenoformans |
| CODH/ACS | - |
Carboxydothermus hydrogenoformans |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Methanosarcina thermophila |
| 25 | - |
assay at | Carboxydothermus hydrogenoformans |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.00012 | - |
acetyl-CoA | pH 7.2, 25°C, recombinant ACSChDELTAN, acetyl-CoA/CO exchange activity | Carboxydothermus hydrogenoformans | |
| 0.0002 | - |
acetyl-CoA | pH 7.2, 25°C, recombinant ACSD beta, acetyl-CoA/CO exchange activity | Methanosarcina thermophila | |
| 0.142 | - |
acetyl-CoA | pH 7.2, 25°C, recombinant ACSCh732, acetyl-CoA/CO exchange activity | Carboxydothermus hydrogenoformans | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6.7 | - |
acetyltransferase assay at | Carboxydothermus hydrogenoformans |
| 6.7 | 7.2 | assay at | Methanosarcina thermophila |
| 7.2 | - |
acetyl-CoA synthase assay at | Carboxydothermus hydrogenoformans |
General Information
| General Information | Comment | Organism |
|---|---|---|
| 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 | Methanosarcina thermophila |
| 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 | Carboxydothermus hydrogenoformans |
| 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 | Carboxydothermus hydrogenoformans |
| additional information | open and closed conformations of ACS, overview | Methanosarcina thermophila |
| physiological function | direct synthesis and cleavage of acetyl-CoA are carried out by the acetyl-CoA decarbonylase/synthase, ACDS, multienzyme complex in Archaea | Methanosarcina thermophila |
| physiological function | direct synthesis and cleavage of acetyl-CoA are carried out by the bifunctional CO dehydrogenase/acetyl-CoA synthase enzyme in anaerobic bacteria | Carboxydothermus hydrogenoformans |
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Release 2023.1 (January 2023)
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