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Information on EC 2.3.1.169 - CO-methylating acetyl-CoA synthase and Organism(s) Methanosarcina thermophila and UniProt Accession P72021
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2.3.1.169 CO-methylating acetyl-CoA synthaseIUBMB Comments
Contains nickel, copper and iron-sulfur clusters. Involved, together with EC 1.2.7.4, carbon-monoxide dehydrogenase (ferredoxin), in the synthesis of acetyl-CoA from CO2 and H2.
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Word Map
- 2.3.1.169
- methanosarcina
- thermophila
- acetylthiocholine
-
methyl-coenzyme
-
methanogenesis
- butyrylthiocholine
-
busch
-
base-off
- propionylthiocholine
-
nickel-containing
-
moorella
- azinphos-methyl
- acetivorans
-
2-naphthyl
- thermoacetica
-
bioorganometallic
-
five-subunit
- methylcobalamin
-
acetate-grown
The taxonomic range for the selected organisms is: Methanosarcina thermophila
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
+
a [Co(I) corrinoid Fe-S protein]
=
+
+
a [methyl-Co(III) corrinoid Fe-S protein]
Synonyms
acsch, co dehydrogenase enzyme complex, carbon monoxide dehydrogenase/acetyl-coenzyme a synthase, carbon monoxide dehydrogenase/acetyl coenzyme a synthase, multienzyme carbon monoxide dehydrogenase complex, co-methylating acetyl-coa synthase, co dehydrogenase/acetyl coa synthase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetyl-CoA decarboxylase/synthase
-
-
-
-
Acetyl-CoA synthase
-
-
-
-
Acetyl-coenzyme A synthase
-
-
-
-
Carbon monoxide dehydrogenase
-
-
-
-
carbon monoxide dehydrogenase-corrinoid enzyme complex
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-
-
-
carbon monoxide dehydrogenase/acetyl-CoA synthase
-
-
-
-
CO dehydrogenase
-
-
-
-
CO dehydrogenase enzyme complex
-
-
-
-
CODH
-
-
-
-
CODH/ASC
-
-
-
-
multienzyme carbon monoxide dehydrogenase complex
-
-
-
-
multienzyme CO dehydrogenase/acetyl-CoA synthase complex
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-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + a [Co(I) corrinoid Fe-S protein] = CO + CoA + a [methyl-Co(III) corrinoid Fe-S protein]
acetyl-CoA + a [Co(I) corrinoid Fe-S protein] = CO + CoA + a [methyl-Co(III) corrinoid Fe-S protein]
the multienzyme complex contains at least two protein components: a CO-oxidizing Ni/Fe-S component and a Co/Fe-S component
-
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
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
demethylation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:corrinoid protein O-acetyltransferase
Contains nickel, copper and iron-sulfur clusters. Involved, together with EC 1.2.7.4, carbon-monoxide dehydrogenase (ferredoxin), in the synthesis of acetyl-CoA from CO2 and H2.
CAS REGISTRY NUMBER
COMMENTARY
176591-19-8
-
64972-88-9
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
CH3-CO-S-CoA + H+ + tetrahydromethanopterin
CH3-tetrahydromethanopterin + CO + HS-CoA
-
-
?
CO + H2O
CO2 + H+ + electron
the multienzyme complex catalyses the reversible oxidation of CO to CO2
-
r
acetyl-CoA + corrinoid protein
CoA + CO + methylcorrinoid protein
-
-
-
-
r
CH3I + CO + HS-CoA
CH3-CO-S-CoA + HI
-
the multienzyme complex catalyses the acetyl-CoA synthesis from CH3I, CO and CoA as well as to cleave acetyl-CoA into its methyl, carbonyl, and CoA components as the first step in the catabolism of acetyl-CoA to methane and CO2
-
-
?
additional information
?
-
the multienzyme complex catalyses the exchange between free CO and carbonyl group of acetyl-CoA, and the exchange between CoA and the CoA moiety of acetyl-CoA
-
-
?
additional information
?
-
-
the multienzyme complex catalyses the exchange between free CO and carbonyl group of acetyl-CoA, and the exchange between CoA and the CoA moiety of acetyl-CoA
-
-
?
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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + corrinoid protein
CoA + CO + methylcorrinoid protein
-
-
-
-
r
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe
Ni
a Ni/Fe-S cluster of multienzyme CO dehydrogenase/acetyl-CoA synthase complex is the active site of acetyl-CoA cleavage and synthesis
CO
-
a cobalt-containing Co/Fe-S component of multienzyme complex serves as a methyl carrier in the pathway of methane synthesis from acetate
Fe
Ni
-
the multienzyme complex contains at least two protein components: a CO-oxidizing Ni/Fe-S component and a cobalt-containing Co/Fe-S component
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
Fe
a Ni/Fe-S cluster of multienzyme CO dehydrogenase/acetyl-CoA synthase complex is the active site of acetyl-CoA cleavage and synthesis
Fe
-
the multienzyme complex contains at least two protein components: a CO-oxidizing Ni/Fe-S component and a cobalt-containing Co/Fe-S component
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.53
methylcorrinoid protein
-
pH 7.2, 25°C, recombinant ACSD beta
additional information
additional information
-
kinetics of recombinant ACSD beta for acetyl-CoA synthase activity, acetyltransferase activity, and acetyl-CoA/CO exchange activity, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0002
acetyl-CoA
-
pH 7.2, 25°C, recombinant ACSD beta, acetyl-CoA/CO exchange activity
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
physiological function
-
direct synthesis and cleavage of acetyl-CoA are carried out by the acetyl-CoA decarbonylase/synthase, ACDS, multienzyme complex in Archaea
additional information
-
open and closed conformations of ACS, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
alpha,beta,gamma,delta,epsilon, the enzyme complex is part of a five-subunit complex, the alpha and epsilon subunits are required for CO oxidation, the gamma end delta subunits constitute a corrinoid/iron-sulfur protein, the beta subunit harbors the Ni/Fe-S cluster, that is the active site of acetyl-CoA cleavage/synthesis, the interaction between the alpha,epsilon dimer and the beta subunit is necessary for breaking and forming the C-C bond of acetyl-CoA, SDS-PAGE
additional information
-
alpha,beta,gamma,delta,epsilon, the enzyme complex is part of a five-subunit complex, the alpha and epsilon subunits are required for CO oxidation, the gamma end delta subunits constitute a corrinoid/iron-sulfur protein, the beta subunit harbors the Ni/Fe-S cluster, that is the active site of acetyl-CoA cleavage/synthesis, the interaction between the alpha,epsilon dimer and the beta subunit is necessary for breaking and forming the C-C bond of acetyl-CoA, SDS-PAGE
additional information
-
open and closed conformations of ACS, overview
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jablonski, P.E.; Lu, W.P.; Ragsdale, S.W.; Ferry, J.G.
Characterization of the metal centers of the corrinoid/iron-sulfur component of the carbon monoxide dehydrogenase enzyme complex from Methanosarcina thermophila by EPR spectroscopy and spectroelectrochemistry
J. Biol. Chem.
268
325-329
1993
Methanosarcina thermophila
Murakami, E.; Ragsdale, S.W.
Evidence for intersubunit communication during acetyl-CoA cleavage by the multienzyme CO dehydrogenase/acetyl-CoA synthase complex from Methanosarcina thermophila. Evidence that the beta subunit catalyzes C-C and C-S bond cleavage
J. Biol. Chem.
275
4699-4707
2000
Methanosarcina thermophila (P72021), Methanosarcina thermophila, Methanosarcina thermophila TM1 (P72021)
Gencic, S.; Duin, E.C.; Grahame, D.A.
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
J. Biol. Chem.
285
15450-15463
2010
Carboxydothermus hydrogenoformans, Carboxydothermus hydrogenoformans DSM 6008, Methanosarcina thermophila, Methanosarcina thermophila TM-1
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