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Literature summary extracted from

  • Mullins, E.A.; Kappock, T.J.
    Crystal structures of Acetobacter aceti succinyl-coenzyme A (CoA):acetate CoA-transferase reveal specificity determinants and illustrate the mechanism used by class I CoA-transferases (2012), Biochemistry, 51, 8422-8434.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.8.3.8 expressed in Escherichia coli C41(DE3) cells Acetobacter aceti
2.8.3.18 expression in Escherichia coli Acetobacter aceti
2.8.3.18 gene aarC, sequence comparisons and phylogenetic analysis, expression of C-terminally His6-tagged wild-type and mutant enzymes Acetobacter aceti

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.8.3.8 hanging drop vapor diffusion method, using 1.7-2.0 M ammonium sulfate, 0.2 M sodium chloride, 0.1 M sodium cacodylate (pH 6.5), and 25 mM 2-mercaptoethanol Acetobacter aceti
2.8.3.18 crystal structures of a C-terminally His6-tagged form of several wild-type and mutant complexes, including freeze-trapped acetylglutamyl anhydride and glutamyl-CoA thioester adducts. The latter shows the acetate product bound to an auxiliary site that is required for efficient carboxylate substrate recognition. Mutant E294A crystallizes in a closed complex containing dethiaacetyl-CoA, which adopts an unusual curled conformation. A model of the acetyl-CoA Michaelis complex reveals that the nucleophilic glutamate is held at a near-ideal angle for attack as the thioester oxygen is forced into an oxyanion hole composed of Gly388 NH and CoA N2'' CoA is nearly immobile along its entire length during all stages of the enzyme reaction Acetobacter aceti
2.8.3.18 native and C-terminally His6-tagged wild-type enzymes in complexes including freeze-trapped acetylglutamyl anhydride and glutamyl-CoA thioester adducts, hanging drop vapor diffusion method, mixing of 0.002 ml of protein solution containing 5.6 mg/ml AarC in 45 mM potassium phosphate, pH 8.0, 90 mM potassium chloride, and 2 mM CoA or 6.0 mg/ml His6-tagged AarC in 45 mM Tris-HCl, pH 8.0, 90 mM potassium chloride, and 2 mM CoA, with 0.002 ml of reservoir solution containing 0.8-1.0 M sodium citrate, 0.1 M imidazole, pH 8.2, and 25 mM 2-mercaptoethanol for orthorhombic crystals or 1.7-2.0 M ammonium sulfate, 0.2 M sodium chloride, 0.1 M sodium cacodylate, pH 6.5, and 25 mM 2-mercaptoethanol for hexagonal crystals, room temperature of about 22°C, X-ray diffraction structure determination and analysis Acetobacter aceti

Protein Variants

EC Number Protein Variants Comment Organism
2.8.3.8 E294A the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme Acetobacter aceti
2.8.3.8 E435A insoluble mutant Acetobacter aceti
2.8.3.8 E435D the mutant shows almost wild type activity Acetobacter aceti
2.8.3.8 E435Q insoluble mutant Acetobacter aceti
2.8.3.8 R228E the mutant has a specific defect in its ability to bind both carboxylate substrates succinyl-CoA and acetyl-CoA and does not use 4-aminobutyrate as substrate Acetobacter aceti
2.8.3.8 S71A the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme Acetobacter aceti
2.8.3.18 E294A complete loss of activity Acetobacter aceti
2.8.3.18 E294A site-directed mutagenesis, the mutant specific catalytic activity is 10000fold reduced compared to the wild-type enzyme, ligand bound crystal structure modeling Acetobacter aceti
2.8.3.18 E435A mutant protein is completely insoluble Acetobacter aceti
2.8.3.18 E435A site-directed mutagenesis, the mutant is completely insoluble, ligand bound crystal structure determination and analysis, the mutant crystallizes in a closed complex containing dethiaacetyl-CoA, which adopts an unusual curled conformation Acetobacter aceti
2.8.3.18 E435D activity similar to wild-type Acetobacter aceti
2.8.3.18 E435D site-directed mutagenesis, the mutant catalytic properties are nearly equivalent to those of the His6-tagged wild-type enzyme, ligand bound crystal structure modeling Acetobacter aceti
2.8.3.18 E435Q mutant protein is completely insoluble Acetobacter aceti
2.8.3.18 E435Q site-directed mutagenesis, the mutant is completely insoluble, ligand bound crystal structure modeling Acetobacter aceti
2.8.3.18 N347A large decrease in catalytic activity Acetobacter aceti
2.8.3.18 N347A site-directed mutagenesis, the mutant shows impaired catalytic activity, but the apparent affinities for all four substrates are largely unaffected, ligand bound crystal structure modeling Acetobacter aceti
2.8.3.18 R228E large decrease in catalytic activity Acetobacter aceti
2.8.3.18 R228E site-directed mutagenesis, the mutant has a specific defect in its ability to bind both carboxylate substrates, ligand bound crystal structure modeling Acetobacter aceti
2.8.3.18 S71A large decrease in catalytic activity Acetobacter aceti
2.8.3.18 S71A site-directed mutagenesis, the mutant shows impaired catalytic activity associated with lower kcat values, ligand bound crystal structure modeling Acetobacter aceti

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.8.3.8 acetate
-
 Acetobacter aceti
2.8.3.18 acetate
-
 Acetobacter aceti
2.8.3.18 citrate weak competitive inhibition against succinate Acetobacter aceti
2.8.3.18 succinate weak competitive inhibition Acetobacter aceti

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.8.3.8 110
-
 acetate wild type enzyme, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C Acetobacter aceti
2.8.3.18 additional information
-
 additional information steady-state kinetic analysis using a Michaelis-Menten model, a substrate inhibition model, or a competitive inhibition model, overview. Arg228 has an important kinetic role in carboxylate substrate binding Acetobacter aceti

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.8.3.18 succinyl-CoA + acetate Acetobacter aceti via an acetylglutamyl anhydride intermediate and glutamyl-CoA thioester adduct acetyl-CoA + succinate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.8.3.8 Acetobacter aceti B3EY95
-
-
2.8.3.18 Acetobacter aceti B3EY95
-
-
2.8.3.18 Acetobacter aceti B3EY95 gene aarC
-
2.8.3.18 Acetobacter aceti 1023 B3EY95 gene aarC
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.8.3.8 ammonium sulfate precipitation, dye-affinity chromatography, ion-exchange column chromatography, and gel filtration Acetobacter aceti

Reaction

EC Number Reaction Comment Organism Reaction ID
2.8.3.18 succinyl-CoA + acetate = acetyl-CoA + succinate the general half-reaction for class I CoA-transferases shows two tetrahedral oxyanion intermediates, which differ by whether CoA becomes attached to the external carbonyl, provided by the acyl-CoA/carboxylate substrate, or the internal carbonyl, provided by the essential active-site glutamate. Following exchange of the carboxylate product, the second half-reaction proceeds in the reverse order of the first half-reaction. In the first half-reaction, the binary enzyme·acyl-CoA complex is converted into a CoA thiolate complex that also contains an acylglutamyl anhydride adduct. Ping-pong kinetic mechanism. Val270 has a dual influence on carboxylate substrate selectivity, as a gate and as a clamp, Arg228 has an important kinetic role in carboxylate substrate binding. The auxiliary site nonselectively binds carboxylates at the threshold of the catalytic pocket, while selectivity is enforced by the conserved gating residue Val270 and the interior of the catalytic pocke Acetobacter aceti
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.8.3.8 acetate + succinyl-CoA 5.1% activity compared to succinate Acetobacter aceti succinate + acetyl-CoA
-
 r
2.8.3.8 acetate + succinyl-CoA 5.1% activity compared to succinate Acetobacter aceti 1023 succinate + acetyl-CoA
-
 r
2.8.3.8 additional information less than 1% activity with acetoacetate, propionate, D-malate, fumarate, L-malate, formate, oxaloacetate, DL-methylsuccinate, and glutarate. No activity is detected with dethiaacetyl-CoA, glycolate, glyoxylate, oxalate, trifluoroacetate, DL-lactate, L-lactate, malonate, pyruvate, maleate, butyrate, D-tartrate, L-tartrate, alpha-ketoglutarate, citrate, or DL-isocitrate Acetobacter aceti ?
-
 ?
2.8.3.8 additional information less than 1% activity with acetoacetate, propionate, D-malate, fumarate, L-malate, formate, oxaloacetate, DL-methylsuccinate, and glutarate. No activity is detected with dethiaacetyl-CoA, glycolate, glyoxylate, oxalate, trifluoroacetate, DL-lactate, L-lactate, malonate, pyruvate, maleate, butyrate, D-tartrate, L-tartrate, alpha-ketoglutarate, citrate, or DL-isocitrate Acetobacter aceti 1023 ?
-
 ?
2.8.3.8 succinate + acetyl-CoA 100% activity Acetobacter aceti acetate + succinyl-CoA
-
 r
2.8.3.8 succinate + acetyl-CoA 100% activity Acetobacter aceti 1023 acetate + succinyl-CoA
-
 r
2.8.3.18 acetyl-CoA + acetoacetate 0.35% of the activity with succinate Acetobacter aceti acetoacetyl-CoA + acetate
-
 r
2.8.3.18 acetyl-CoA + D-malate 0.28% of the activity with succinate Acetobacter aceti D-malyl-CoA + acetate
-
 r
2.8.3.18 acetyl-CoA + fumarate 0.20% of the activity with succinate Acetobacter aceti fumaryl-CoA + acetate
-
 r
2.8.3.18 acetyl-CoA + propionate 0.34% of the activity with succinate Acetobacter aceti propionyl-CoA + acetate
-
 r
2.8.3.18 acetyl-CoA + succinate
-
 Acetobacter aceti succinyl-CoA + acetate
-
 r
2.8.3.18 additional information no activity with glycolate, glyoxylate, oxalate, trifluoroacetate, DL-lactate, L-lactate, malonate, pyruvate, maleate, butyrate, D-tartrate, L-tartrate, 2-oxooglutarate, citrate, or DL-isocitrate Acetobacter aceti ?
-
 ?
2.8.3.18 additional information substrate specificity, overview. Acetoacetate, propionate, D-malate, fumarate, L-malate, formate, oxaloacetate, DL-methylsuccinate, glutarate are alternate substrates, no activity with glycolate, glyoxylate, oxalate, trifluoroacetate, DL-lactate, L-lactate, malonate, pyruvate, maleate, butyrate, D-tartrate, L-tartrate, 2-oxooglutarate, citrate, or DL-isocitrate Acetobacter aceti ?
-
 ?
2.8.3.18 additional information no activity with glycolate, glyoxylate, oxalate, trifluoroacetate, DL-lactate, L-lactate, malonate, pyruvate, maleate, butyrate, D-tartrate, L-tartrate, 2-oxooglutarate, citrate, or DL-isocitrate Acetobacter aceti 1023 ?
-
 ?
2.8.3.18 additional information substrate specificity, overview. Acetoacetate, propionate, D-malate, fumarate, L-malate, formate, oxaloacetate, DL-methylsuccinate, glutarate are alternate substrates, no activity with glycolate, glyoxylate, oxalate, trifluoroacetate, DL-lactate, L-lactate, malonate, pyruvate, maleate, butyrate, D-tartrate, L-tartrate, 2-oxooglutarate, citrate, or DL-isocitrate Acetobacter aceti 1023 ?
-
 ?
2.8.3.18 succinyl-CoA + acetate 5.1% of the activity with succinate + acetyl-CoA Acetobacter aceti acetyl-CoA + succinate
-
 r
2.8.3.18 succinyl-CoA + acetate via an acetylglutamyl anhydride intermediate and glutamyl-CoA thioester adduct Acetobacter aceti acetyl-CoA + succinate
-
 ?
2.8.3.18 succinyl-CoA + acetoacetate
-
 Acetobacter aceti acetoacetyl-CoA + succinate
-
 ?
2.8.3.18 succinyl-CoA + D-malate
-
 Acetobacter aceti D-malyl-CoA + succinate
-
 ?
2.8.3.18 succinyl-CoA + DL-methylsuccinate
-
 Acetobacter aceti DL-methylsuccinyl-CoA + succinate
-
 ?
2.8.3.18 succinyl-CoA + formate
-
 Acetobacter aceti formyl-CoA + succinate
-
 ?
2.8.3.18 succinyl-CoA + fumarate
-
 Acetobacter aceti fumaryl-CoA + succinate
-
 ?
2.8.3.18 succinyl-CoA + glutarate
-
 Acetobacter aceti glutaryl-CoA + succinate
-
 ?
2.8.3.18 succinyl-CoA + L-malate
-
 Acetobacter aceti L-malyl-CoA + succinate
-
 ?
2.8.3.18 succinyl-CoA + oxaloacetate
-
 Acetobacter aceti oxaloacetyl-CoA + succinate
-
 ?
2.8.3.18 succinyl-CoA + propionate
-
 Acetobacter aceti propionyl-CoA + succinate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.8.3.8 AarC
-
 Acetobacter aceti
2.8.3.8 SCACT
-
 Acetobacter aceti
2.8.3.8 succinyl-CoA:acetate CoA-transferase
-
 Acetobacter aceti
2.8.3.8 succinyl-coenzyme A:acetate CoA-transferase
-
 Acetobacter aceti
2.8.3.18 AarC
-
 Acetobacter aceti
2.8.3.18 acetic acid resistance factor
-
 Acetobacter aceti
2.8.3.18 SCACT
-
 Acetobacter aceti
2.8.3.18 SCOT
-
 Acetobacter aceti
2.8.3.18 succinyl-CoA:3-oxoacid CoA-transferase
-
 Acetobacter aceti
2.8.3.18 succinyl-CoA:acetate CoA-transferase
-
 Acetobacter aceti
2.8.3.18 succinyl-coenzyme A:acetate CoA-transferase
-
 Acetobacter aceti

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.8.3.18 30
-
 assay at Acetobacter aceti

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.8.3.8 290
-
 acetate wild type enzyme, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C Acetobacter aceti

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.8.3.18 8
-
 assay at Acetobacter aceti

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
2.8.3.18 3.8
-
 unstable below Acetobacter aceti
2.8.3.18 3.8 6.8
-
 Acetobacter aceti

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.8.3.8 1600
-
 acetate wild type enzyme, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C Acetobacter aceti
2.8.3.18 150
-
 succinate pH 8.0, 30°C Acetobacter aceti
2.8.3.18 150
-
 citrate pH 8.0, temperature not specified in the publication Acetobacter aceti
2.8.3.18 1600
-
 acetate pH 8.0, temperature not specified in the publication Acetobacter aceti

General Information

EC Number General Information Comment Organism
2.8.3.8 metabolism succinyl-CoA:acetate CoA-transferase is an acetic acid resistance factor (AarC) with a role in a variant citric acid cycle Acetobacter aceti
2.8.3.8 physiological function the enzyme is an acetic acid resistance factor that is required for acetate resistance Acetobacter aceti
2.8.3.18 evolution the enzyme belongs to the class I-CoA-transferases, which, typified by mitochondrial succinyl-CoA:3-oxoacid CoA-transferase, form multiple covalent adducts involving an essential glutamate residue. Arg228 is found in only AarC and several closely allied SCACT group sequences, EC 6.2.1 Acetobacter aceti
2.8.3.18 additional information the nucleophilic glutamate is held at a near-ideal angle for attack as the thioester oxygen is forced into an oxyanion hole composed of Gly388 NH and CoA N2''. CoA is nearly immobile along its entire length during all stages of the enzyme reaction. Spatial and sequence conservation of key residues indicates that this mechanism is general among class I CoA-transferases, structural model for the AarC mechanism, overview. An auxiliary carboxylate binding site, located just outside the AarC catalytic pocket, contributes to the efficient recognition and conversion of the physiological carboxylate substrates. Protein conformational dynamics, overview. Arg228 has an important kinetic role in carboxylate substrate binding. Regulation of carboxylate access to the active-site glutamate, overview Acetobacter aceti
2.8.3.18 physiological function the enzyme is an acetic acid resistance factor AarC that is required for acetate resistance by vinegar factory strain Acetobacter aceti 1023. The enzyme acts in a variant citric acid cycle that overoxidizes acetic acid to CO2, which then diffuses into the acidic culture medium Acetobacter aceti

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.8.3.8 0.029
-
 acetate mutant enzyme S71A, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C Acetobacter aceti
2.8.3.8 0.03
-
 succinate mutant enzyme S71A, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C Acetobacter aceti
2.8.3.8 0.074
-
 succinyl-CoA mutant enzyme S71A, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C Acetobacter aceti
2.8.3.8 0.13
-
 succinyl-CoA mutant enzyme R228E, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C Acetobacter aceti
2.8.3.8 0.16
-
 acetate mutant enzyme N347A, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C Acetobacter aceti
2.8.3.8 0.3
-
 succinate mutant enzyme R228E, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C Acetobacter aceti
2.8.3.8 0.39
-
 succinyl-CoA mutant enzyme N347A, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C Acetobacter aceti
2.8.3.8 0.6
-
 acetate mutant enzyme R228E, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C Acetobacter aceti
2.8.3.8 0.7
-
 acetyl-CoA mutant enzyme N347A, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C Acetobacter aceti
2.8.3.8 0.7
-
 acetyl-CoA mutant enzyme S71A, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C Acetobacter aceti
2.8.3.8 2.3
-
 acetyl-CoA mutant enzyme R228E, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C Acetobacter aceti
2.8.3.8 2.7
-
 succinate mutant enzyme N347A, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C Acetobacter aceti
2.8.3.8 3
-
 acetate mutant enzyme E435D, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C Acetobacter aceti
2.8.3.8 3.4
-
 acetyl-CoA wild type enzyme, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C Acetobacter aceti
2.8.3.8 9
-
 succinyl-CoA mutant enzyme E435D, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C Acetobacter aceti
2.8.3.8 9
-
 succinyl-CoA wild type enzyme, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C Acetobacter aceti
2.8.3.8 52
-
 acetyl-CoA mutant enzyme E435D, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C Acetobacter aceti
2.8.3.8 73
-
 succinate mutant enzyme E435D, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C Acetobacter aceti
2.8.3.8 79
-
 succinate wild type enzyme, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C Acetobacter aceti
2.8.3.8 2600
-
 acetate wild type enzyme, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C Acetobacter aceti
2.8.3.18 0.000074
-
 succinyl-CoA pH 8.0, 30°C, mutant S71A Acetobacter aceti
2.8.3.18 0.00013
-
 succinyl-CoA pH 8.0, 30°C, mutant R228E Acetobacter aceti
2.8.3.18 0.00039
-
 succinyl-CoA pH 8.0, 30°C, mutant N347A Acetobacter aceti
2.8.3.18 0.0007
-
 acetyl-CoA pH 8.0, 30°C, mutant N347A Acetobacter aceti
2.8.3.18 0.0007
-
 acetyl-CoA pH 8.0, 30°C, mutant S71A Acetobacter aceti
2.8.3.18 0.0023
-
 acetyl-CoA pH 8.0, 30°C, mutant R228E Acetobacter aceti
2.8.3.18 0.0034
-
 acetyl-CoA pH 8.0, 30°C, His6-tagged wild-type enzyme Acetobacter aceti
2.8.3.18 0.005
-
 acetyl-CoA pH 8.0, 30°C, mutant E435D Acetobacter aceti
2.8.3.18 0.009
-
 succinyl-CoA pH 8.0, 30°C, His6-tagged wild-type enzyme and mutant E435D Acetobacter aceti
2.8.3.18 0.029
-
 acetate mutant S71A, pH 8.0, temperature not specified in the publication Acetobacter aceti
2.8.3.18 0.029
-
 acetate pH 8.0, 30°C, mutant S71A Acetobacter aceti
2.8.3.18 0.03
-
 succinate mutant S71A, pH 8.0, temperature not specified in the publication Acetobacter aceti
2.8.3.18 0.03
-
 succinate pH 8.0, 30°C, mutant S71A Acetobacter aceti
2.8.3.18 0.074
-
 succinyl-CoA mutant S71A, pH 8.0, temperature not specified in the publication Acetobacter aceti
2.8.3.18 0.13
-
 succinyl-CoA mutant R228E, pH 8.0, temperature not specified in the publication Acetobacter aceti
2.8.3.18 0.16
-
 acetate mutant N347A, pH 8.0, temperature not specified in the publication Acetobacter aceti
2.8.3.18 0.16
-
 acetate pH 8.0, 30°C, mutant N347A Acetobacter aceti
2.8.3.18 0.3
-
 succinate mutant R228E, pH 8.0, temperature not specified in the publication Acetobacter aceti
2.8.3.18 0.3
-
 succinate pH 8.0, 30°C, mutant R228E Acetobacter aceti
2.8.3.18 0.39
-
 succinyl-CoA mutant N347A, pH 8.0, temperature not specified in the publication Acetobacter aceti
2.8.3.18 0.6
-
 acetate mutant R228E, pH 8.0, temperature not specified in the publication Acetobacter aceti
2.8.3.18 0.6
-
 acetate pH 8.0, 30°C, mutant R228E Acetobacter aceti
2.8.3.18 0.7
-
 acetyl-CoA mutant N347A, pH 8.0, temperature not specified in the publication Acetobacter aceti
2.8.3.18 0.7
-
 acetyl-CoA mutant S71A, pH 8.0, temperature not specified in the publication Acetobacter aceti
2.8.3.18 2.7
-
 succinate mutant N347A, pH 8.0, temperature not specified in the publication Acetobacter aceti
2.8.3.18 2.7
-
 succinate pH 8.0, 30°C, mutant N347A Acetobacter aceti
2.8.3.18 3
-
 acetate mutant E435D, pH 8.0, temperature not specified in the publication Acetobacter aceti
2.8.3.18 3
-
 acetate pH 8.0, 30°C, mutant E435D Acetobacter aceti
2.8.3.18 3.4
-
 acetyl-CoA wild-type, pH 8.0, temperature not specified in the publication Acetobacter aceti
2.8.3.18 4
-
 acetate wild-type, pH 8.0, temperature not specified in the publication Acetobacter aceti
2.8.3.18 4
-
 acetate pH 8.0, 30°C, His6-tagged wild-type enzyme Acetobacter aceti
2.8.3.18 5.2
-
 acetyl-CoA mutant E435D, pH 8.0, temperature not specified in the publication Acetobacter aceti
2.8.3.18 9
-
 succinyl-CoA wild-type, pH 8.0, temperature not specified in the publication Acetobacter aceti
2.8.3.18 9
-
 succinyl-CoA mutant E435D, pH 8.0, temperature not specified in the publication Acetobacter aceti
2.8.3.18 73
-
 succinate mutant E435D, pH 8.0, temperature not specified in the publication Acetobacter aceti
2.8.3.18 73
-
 succinate pH 8.0, 30°C, mutant E435D Acetobacter aceti
2.8.3.18 79
-
 succinate wild-type, pH 8.0, temperature not specified in the publication Acetobacter aceti
2.8.3.18 79
-
 succinate pH 8.0, 30°C, His6-tagged wild-type enzyme Acetobacter aceti