Protein Variants | Comment | Organism |
---|---|---|
C509A | site-directe mutagenesis, mutant C509A shows a significantly diminished methyl transfer activity compared to the wild-type enzyme | Moorella thermoacetica |
C509H | site-directed mutagenesis, mutant C509H can accept a methyl group from CH3-Co3+FeSP at over 70% extent. The near-wild-type-level of methyl group transfer activity for C509H indicates that the di-nickel site is assembled well in this mutant, and strongly suggests that an imidazole group can bridge the di-nickel site to the cubane of the A-cluster. Histidine that replaces the bridging cysteine 509 might function as a bridge, with one nitrogen of the imidazole ring coordinating to a cubane Fe and the other nitrogen coordinating to Nip | Moorella thermoacetica |
C509S | site-directed mutagenesis, mutant C509S, in which the cysteinate bridge C509 might be replaced by a serine oxide, exhibits no detectable methyl transfer activity. Oxygen is a harder donor than sulfide, and the electronic coupling between the cubane and the di-nickel site may differ relative to sulfide. Absence of methyl transfer activity in C509S indicates that an O bridge is not sufficient for this communication | Moorella thermoacetica |
C509V | site-directed mutagenesis, mutant C509V exhibits no detectable methyl group transfer activity due to it lacking a bridging coordinating atom, Val is more bulky and has greater steric hindrance | Moorella thermoacetica |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | the A-cluster of acetyl-coenzyme A synthase consists of an [Fe4S4] cubane bridged to a [NipNid] centre via C509 cysteinate. The bridging cysteinate, which can be substituted by histidine imidazole, mediates communication between the [Fe4S4] cubane and the [NipNid] centre during the synthesis of acetyl-CoA | Moorella thermoacetica | |
Ni2+ | the A-cluster of acetyl-coenzyme A synthase consists of an [Fe4S4] cubane bridged to a [NipNid] centre via C509 cysteinate. The bridging cysteinate, which can be substituted by histidine imidazole, mediates communication between the [Fe4S4] cubane and the [NipNid] centre during the synthesis of acetyl-CoA | Moorella thermoacetica |
Organism | UniProt | Comment | Textmining |
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Moorella thermoacetica | - |
- |
- |
Subunits | Comment | Organism |
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More | the A-cluster of acetyl-coenzyme A synthase consists of an [Fe4S4] cubane bridged to a [NipNid] centre via C509 cysteinate. The bridging cysteinate, which can be substituted by histidine imidazole, mediates communication between the [Fe4S4] cubane and the [NipNid] centre during the synthesis of acetyl-CoA. The ACS/CODH from Moorella thermoacetica is an alpha2beta2 tetramer containing seven metal clusters connected by a molecular tunnel network, overview | Moorella thermoacetica |
Synonyms | Comment | Organism |
---|---|---|
Acetyl-coenzyme A synthase | - |
Moorella thermoacetica |
ACS | - |
Moorella thermoacetica |
General Information | Comment | Organism |
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evolution | the metalloprotein acetyl-coenzyme A synthase/carbon monoxide dehydrogenase, ACS/CODH, is a bifunctional metalloenzyme found in anaerobic archaea and bacteria that grow hemoautotrophically on CO or CO2, and is significant for biological carbon fixation and understanding the origin of life | Moorella thermoacetica |