2.3.1.169: CO-methylating acetyl-CoA synthase

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For detailed information about CO-methylating acetyl-CoA synthase, go to the full flat file.

Reaction

Synonyms

ACDS multienzyme complex, acetyl-CoA decarbonylase/synthase multienzyme complex, acetyl-CoA decarboxylase/synthase, Acetyl-CoA synthase, Acetyl-coenzyme A synthase, acetyl-coenzyme A synthase/carbon monoxide dehydrogenase, ACS/CODH, ACSCh, Carbon monoxide dehydrogenase, carbon monoxide dehydrogenase-corrinoid enzyme complex, carbon monoxide dehydrogenase/acetyl coenzyme A synthase, carbon monoxide dehydrogenase/acetyl-CoA synthase, carbon monoxide dehydrogenase/acetyl-coenzyme A synthase, CDH1, Cdh2, CO dehydrogenase, CO dehydrogenase enzyme complex, CO dehydrogenase/acetyl CoA synthase, CO dehydrogenase/acetyl coenzyme A synthase, CO dehydrogenase/acetyl-CoA synthase, CODH, CODH/ACS, CODH/ASC, KSU1_D0226, KSU1_D0227, monoxide dehydrogenase/acetyl-CoA synthase, multienzyme carbon monoxide dehydrogenase complex, multienzyme CO dehydrogenase/acetyl-CoA synthase complex

ECTree

     2 Transferases

         2.3 Acyltransferases

             2.3.1 Transferring groups other than aminoacyl groups

                2.3.1.169 CO-methylating acetyl-CoA synthase

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Results	in table
5	Activating Compound
2659	AA Sequence
2	CAS Registry Number
8	Cloned(Commentary)
3	Cofactor
6	Crystallization (Commentary)
1	Expression
23	General Information
2	General Stability
21	Inhibitors
1	kcat/KM [mM/s]
2	Ki Value [mM]
11	KM Value [mM]
1	Localization
62	Metals/Ions
11	Molecular Weight [Da]
17	Natural Substrates/ Products (Substrates)
60	Organism
7	Pathway
48	PDB ID
13	pH Optimum
11	Protein Variants
7	Purification (Commentary)
32	Reaction
1	Reaction Type
47	Reference
1	Renatured (Commentary)
1	Source Tissue
7	Specific Activity [micromol/min/mg]
66	Substrates and Products (Substrate)
13	Subunits
42	Synonyms
1	Systematic Name
7	Temperature Optimum [°C]
1	Temperature Range [°C]
2	Temperature Stability [°C]
5	Turnover Number [1/s]

Crystallization

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Crystallization on EC 2.3.1.169 - CO-methylating acetyl-CoA synthase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

density functional theory and polarized continuum model study. The optimized geometries show a large structural variability of the A-cluster depending on the oxidation state and the ligand attached to the proximal nickel atom. The calculated pKa values and redox potentials are in favor of the two-electron reduction mechanism coupled to a proton transfer

Carboxydothermus hydrogenoformans

P83789

736683

49 kDa fragment containing residues 311-729 of the intact enzym. In the fragment, domains A2 and A3 have significantlymoved to each other, corresponding to a rotation around a hinge region located close to the C-terminus of the long interdomain helix

Moorella thermoacetica

P27988

696354

a 2.5 A resolution structure of xenon-pressurized CODH/ACS, examination of the nature of gaseous cavities within the enzyme. The cavity calculation program CAVENV accurately predicts the channels connecting the C- and A-clusters, with 17 of 19 xenon binding sites within the predicted regions. The enzyme has a channel for a small substrate, a channel plug, a flexible acetyl-CoA synthase subunit that can open to interact with a large substrate, and an interdomain cavity to putatively bind a medium-sized substrate

Moorella thermoacetica

-

685228

crystal structure of recombinant ACS lacking the N-terminal domain that interacts with carbon monoxide dehydrogenase shows a large reorganization of the remaining two globular domains, producing a narrow cleft of suitable size, shape, and nature to bind CoA. Sequence comparisons with homologous archaeal enzymes that naturally lack the N-terminal domain show that many amino acids lining this cleft are conserved. Besides the typical [4Fe-4S] center, the A-cluster contains only one proximal metal ion that is most likely Cu or Zn. Incorporation of a functional Ni2Fe4S4 A-cluster would require only minor structural rearrangements

Moorella thermoacetica

P27988

696354

sitting drop vapor diffusion at room temperature in a Coy anaerobic chamber, 0.005 ml of protein solution containing 40-60 mg/ml CODH/ACS in 50 mM Tris, pH 7.6, are mixed with 0.0075 ml of reservoir solution containing 8% polyethylene glycol MME 5000, 20% glycerol, 200 mM calcium acetate, 100 mM PIPES, pH 6.5, and 2 mM dithioerythritol, X-ray diffraction structure determination and analysis at 2.2 A resolution, multiwavelength anomalous dispersion techniques, molecular replacement

Moorella thermoacetica

P27989

644679

structures of the 310 kDa bifunctional CODH/acetyl-CoA synthase complex bound both with a substrate H2O/OH- molecule and with a cyanide inhibitor. Both in native crystals and identical crystals soaked in a solution containing potassium cyanide, the substrateH2O/OH- molecule exhibits binding to the unique Fe site of the C-cluster. Cyanide binding is also observed in a bent conformation to Ni of the C-cluster, adjacent the substrate H2O/OH-molecule. The bridging sulfide is not present in either structure. Findings do not support a fifth, bridging sulfide playing a catalytic role in the enzyme mechanism

Moorella thermoacetica

-

696351