BRENDA - Enzyme Database
show all sequences of 6.2.1.B11

Biochemical and kinetic characterization of the recombinant ADP-forming acetyl coenzyme A synthetase from the amitochondriate protozoan Entamoeba histolytica

Jones, C.P.; Ingram-Smith, C.; Eukaryot. Cell 13, 1530-1537 (2014)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain Rosetta2(DE3)pLysS
Entamoeba histolytica
Inhibitors
Inhibitors
Commentary
Organism
Structure
acetyl phosphate
-
Entamoeba histolytica
AMP
slight inhibition
Entamoeba histolytica
ATP
ATP inhibits the acetate-forming direction of the reaction, with 50% inhibitory concentration of 0.81 mM, which is in the range of its physiological concentration. Diphosphate displays mixed inhibition versus each of the three substrates, acetyl-CoA, ADP, and phosphate. No inhibition by lactate and pyruvate
Entamoeba histolytica
cAMP
-
Entamoeba histolytica
D-fructose 1,6-bisphosphate
-
Entamoeba histolytica
D-fructose 6-phosphate
-
Entamoeba histolytica
D-glucose 6-phosphate
-
Entamoeba histolytica
diphosphate
diphosphate inhibits the acetate-forming direction of the reaction, with 50% inhibitory concentration of 0.75 mM, which is in the range of its physiological concentration. ATP displays mixed inhibition versus each of the three substrates, acetyl-CoA, ADP, and phosphate
Entamoeba histolytica
glyoxylate
inhibits the activity in the acetate-forming direction
Entamoeba histolytica
NAD+
-
Entamoeba histolytica
NADH
-
Entamoeba histolytica
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
Michaelis-Menten steady-state kinetic analysis, pseudo-first-order reaction kinetic determinations are performed in both directions of the reaction
Entamoeba histolytica
0.032
-
propionyl-CoA
pH 7.3, 37C, propionate-forming direction, with propionyl-CoA
Entamoeba histolytica
0.04
-
acetyl-CoA
pH 7.3, 37C, acetate-forming direction
Entamoeba histolytica
0.2
-
CoA
pH 7.3, 37C, acetyl-CoA-forming direction, with acetate
Entamoeba histolytica
0.71
-
ADP
pH 7.3, 37C, propionate-forming direction, with propionyl-CoA
Entamoeba histolytica
1.5
-
phosphate
pH 7.3, 37C, propionate-forming direction, with propionyl-CoA
Entamoeba histolytica
1.6
-
ADP
pH 7.3, 37C, acetate-forming direction, with acetyl-CoA
Entamoeba histolytica
1.6
-
CoA
pH 7.3, 37C, propionyl-CoA-forming direction, with propionate
Entamoeba histolytica
1.8
-
phosphate
pH 7.3, 37C, acetate-forming direction, with acetyl-CoA
Entamoeba histolytica
1.9
-
GDP
pH 7.3, 37C, acetate-forming direction, with acetyl-CoA
Entamoeba histolytica
7.2
-
ATP
pH 7.3, 37C, propionyl-CoA-forming direction, with propionate
Entamoeba histolytica
10
-
GTP
pH 7.3, 37C, acetyl-CoA-forming direction, with acetate
Entamoeba histolytica
12
-
ATP
pH 7.3, 37C, acetyl-CoA-forming direction, with acetate
Entamoeba histolytica
14
-
acetate
pH 7.3, 37C, acetyl-CoA-forming direction
Entamoeba histolytica
29
-
propionate
pH 7.3, 37C, propionyl-CoA-forming direction, with propionate
Entamoeba histolytica
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Ca2+
can slightly substitute for Mg2+
Entamoeba histolytica
Co2+
can partially substitute for Mg2+
Entamoeba histolytica
Cu2+
can slightly substitute for Mg2+
Entamoeba histolytica
Mg2+
required for activity, best divalent cation
Entamoeba histolytica
Mn2+
can substitute for Mg2+
Entamoeba histolytica
Ni2+
can slightly substitute for Mg2+
Entamoeba histolytica
Zn2+
can slightly substitute for Mg2+
Entamoeba histolytica
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
150000
-
recombinant His6-tagged enzyme, gel filtration
Entamoeba histolytica
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ATP + acetate + CoA
Entamoeba histolytica
-
ADP + phosphate + acetyl-CoA
-
-
r
GTP + acetate + CoA
Entamoeba histolytica
-
GDP + phosphate + acetyl-CoA
-
-
r
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Entamoeba histolytica
Q9NAT4
-
-
Purification (Commentary)
Commentary
Organism
recombinant His6-tagged enzyme from Escherichia coli strain Rosetta2(DE3)pLysS by nickel affinity chromatography
Entamoeba histolytica
Source Tissue
Source Tissue
Commentary
Organism
Textmining
trophozoite
-
Entamoeba histolytica
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ADP + phosphate + acetyl-CoA
-
744820
Entamoeba histolytica
ATP + acetate + CoA
-
-
-
r
ADP + phosphate + propionyl-CoA
-
744820
Entamoeba histolytica
ATP + propionate + CoA
-
-
-
r
ATP + acetate + CoA
-
744820
Entamoeba histolytica
ADP + phosphate + acetyl-CoA
-
-
-
r
ATP + propionate + CoA
-
744820
Entamoeba histolytica
ADP + phosphate + propionyl-CoA
-
-
-
r
GDP + phosphate + acetyl-CoA
-
744820
Entamoeba histolytica
GTP + acetate + CoA
-
-
-
r
GTP + acetate + CoA
-
744820
Entamoeba histolytica
GDP + phosphate + acetyl-CoA
-
-
-
r
GTP + acetate + CoA
GTP gives 57% of the activity with ATP
744820
Entamoeba histolytica
GDP + phosphate + acetyl-CoA
-
-
-
r
ITP + acetate + CoA
ITP gives 15% of the activity with ATP
744820
Entamoeba histolytica
IDP + phosphate + acetyl-CoA
-
-
-
r
additional information
the enzyme can utilize both ADP/ATP and GDP/GTP in the respective directions of the reaction. Less than 4% of maximal activity is observed with isobutyrate, valerate, isovalerate, hexanoate, heptanoate, octanoate, succinate, or phenylacetate as the acyl substrate. Activity observed with ATP (representing 100% activity) is nearly double that with GTP (57%) and substantially higher than the activities observed with ITP (15%), CTP (4.1%), or UTP (1.6%), no activity is observed with TTP or diphosphate. Enzymatic activity in the acetate-forming direction is determined by measuring the release of CoA with a sulfhydryl group (CoASH) from acyl-CoA by using Ellman's thiol reagent (DTNB). Production of NTB2- by CoASH cleavage of DTNB is measured spectrophotometrically at 412 nm. Activity in the acetate-forming direction is confirmed using the hexokinase/glucose-6-phosphate dehydrogenase-coupled assay. This assay couples ATP formation to the reduction of NADP+ to NADPH, which is measured spectrophotometrically at 340 nm
744820
Entamoeba histolytica
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
homodimer
2 * 78999, recombinant His6-tagged enzyme, sequence calculation and SDS-PAGE
Entamoeba histolytica
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
37
-
acetate-forming assay at
Entamoeba histolytica
55
-
acetyl-CoA-forming direction
Entamoeba histolytica
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
18
-
phosphate
pH 7.3, 37C, acetate-forming direction, with propionyl-CoA
Entamoeba histolytica
21
-
propionyl-CoA
pH 7.3, 37C, acetate-forming direction, with propionyl-CoA
Entamoeba histolytica
24
-
ADP
pH 7.3, 37C, acetate-forming direction, with propionyl-CoA
Entamoeba histolytica
110
-
acetyl-CoA
pH 7.3, 37C, acetate-forming direction
Entamoeba histolytica
120
-
phosphate
pH 7.3, 37C, acetate-forming direction, with acetyl-CoA
Entamoeba histolytica
140
-
ADP
pH 7.3, 37C, acetate-forming direction, with acetyl-CoA
Entamoeba histolytica
170
-
GDP
pH 7.3, 37C, acetate-forming direction, with acetyl-CoA
Entamoeba histolytica
180
-
GTP
pH 7.3, 37C, acetyl-CoA-forming direction, with acetate
Entamoeba histolytica
190
-
propionate
pH 7.3, 37C, propionyl-CoA-forming direction, with propionate
Entamoeba histolytica
220
-
CoA
pH 7.3, 37C, acetyl-CoA-forming direction, with acetate
Entamoeba histolytica
240
-
acetate
pH 7.3, 37C, acetyl-CoA-forming direction
Entamoeba histolytica
240
-
ATP
pH 7.3, 37C, propionyl-CoA-forming direction, with propionate
Entamoeba histolytica
260
-
CoA
pH 7.3, 37C, propionyl-CoA-forming direction, with propionate
Entamoeba histolytica
320
-
ATP
pH 7.3, 37C, acetyl-CoA-forming direction, with acetate
Entamoeba histolytica
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.3
-
assay at
Entamoeba histolytica
Cofactor
Cofactor
Commentary
Organism
Structure
ADP
-
Entamoeba histolytica
ATP
-
Entamoeba histolytica
GDP
-
Entamoeba histolytica
GTP
-
Entamoeba histolytica
IC50 Value
IC50 Value
IC50 Value Maximum
Commentary
Organism
Inhibitor
Structure
0.81
-
pH 7.3, 37C, acetate-forming direction
Entamoeba histolytica
ATP
0.83
-
pH 7.3, 37C, acetate-forming direction
Entamoeba histolytica
diphosphate
Cloned(Commentary) (protein specific)
Commentary
Organism
recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain Rosetta2(DE3)pLysS
Entamoeba histolytica
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
ADP
-
Entamoeba histolytica
ATP
-
Entamoeba histolytica
GDP
-
Entamoeba histolytica
GTP
-
Entamoeba histolytica
IC50 Value (protein specific)
IC50 Value
IC50 Value Maximum
Commentary
Organism
Inhibitor
Structure
0.81
-
pH 7.3, 37C, acetate-forming direction
Entamoeba histolytica
ATP
0.83
-
pH 7.3, 37C, acetate-forming direction
Entamoeba histolytica
diphosphate
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
acetyl phosphate
-
Entamoeba histolytica
AMP
slight inhibition
Entamoeba histolytica
ATP
ATP inhibits the acetate-forming direction of the reaction, with 50% inhibitory concentration of 0.81 mM, which is in the range of its physiological concentration. Diphosphate displays mixed inhibition versus each of the three substrates, acetyl-CoA, ADP, and phosphate. No inhibition by lactate and pyruvate
Entamoeba histolytica
cAMP
-
Entamoeba histolytica
D-fructose 1,6-bisphosphate
-
Entamoeba histolytica
D-fructose 6-phosphate
-
Entamoeba histolytica
D-glucose 6-phosphate
-
Entamoeba histolytica
diphosphate
diphosphate inhibits the acetate-forming direction of the reaction, with 50% inhibitory concentration of 0.75 mM, which is in the range of its physiological concentration. ATP displays mixed inhibition versus each of the three substrates, acetyl-CoA, ADP, and phosphate
Entamoeba histolytica
glyoxylate
inhibits the activity in the acetate-forming direction
Entamoeba histolytica
NAD+
-
Entamoeba histolytica
NADH
-
Entamoeba histolytica
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
Michaelis-Menten steady-state kinetic analysis, pseudo-first-order reaction kinetic determinations are performed in both directions of the reaction
Entamoeba histolytica
0.032
-
propionyl-CoA
pH 7.3, 37C, propionate-forming direction, with propionyl-CoA
Entamoeba histolytica
0.04
-
acetyl-CoA
pH 7.3, 37C, acetate-forming direction
Entamoeba histolytica
0.2
-
CoA
pH 7.3, 37C, acetyl-CoA-forming direction, with acetate
Entamoeba histolytica
0.71
-
ADP
pH 7.3, 37C, propionate-forming direction, with propionyl-CoA
Entamoeba histolytica
1.5
-
phosphate
pH 7.3, 37C, propionate-forming direction, with propionyl-CoA
Entamoeba histolytica
1.6
-
ADP
pH 7.3, 37C, acetate-forming direction, with acetyl-CoA
Entamoeba histolytica
1.6
-
CoA
pH 7.3, 37C, propionyl-CoA-forming direction, with propionate
Entamoeba histolytica
1.8
-
phosphate
pH 7.3, 37C, acetate-forming direction, with acetyl-CoA
Entamoeba histolytica
1.9
-
GDP
pH 7.3, 37C, acetate-forming direction, with acetyl-CoA
Entamoeba histolytica
7.2
-
ATP
pH 7.3, 37C, propionyl-CoA-forming direction, with propionate
Entamoeba histolytica
10
-
GTP
pH 7.3, 37C, acetyl-CoA-forming direction, with acetate
Entamoeba histolytica
12
-
ATP
pH 7.3, 37C, acetyl-CoA-forming direction, with acetate
Entamoeba histolytica
14
-
acetate
pH 7.3, 37C, acetyl-CoA-forming direction
Entamoeba histolytica
29
-
propionate
pH 7.3, 37C, propionyl-CoA-forming direction, with propionate
Entamoeba histolytica
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Ca2+
can slightly substitute for Mg2+
Entamoeba histolytica
Co2+
can partially substitute for Mg2+
Entamoeba histolytica
Cu2+
can slightly substitute for Mg2+
Entamoeba histolytica
Mg2+
required for activity, best divalent cation
Entamoeba histolytica
Mn2+
can substitute for Mg2+
Entamoeba histolytica
Ni2+
can slightly substitute for Mg2+
Entamoeba histolytica
Zn2+
can slightly substitute for Mg2+
Entamoeba histolytica
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
150000
-
recombinant His6-tagged enzyme, gel filtration
Entamoeba histolytica
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ATP + acetate + CoA
Entamoeba histolytica
-
ADP + phosphate + acetyl-CoA
-
-
r
GTP + acetate + CoA
Entamoeba histolytica
-
GDP + phosphate + acetyl-CoA
-
-
r
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His6-tagged enzyme from Escherichia coli strain Rosetta2(DE3)pLysS by nickel affinity chromatography
Entamoeba histolytica
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
trophozoite
-
Entamoeba histolytica
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ADP + phosphate + acetyl-CoA
-
744820
Entamoeba histolytica
ATP + acetate + CoA
-
-
-
r
ADP + phosphate + propionyl-CoA
-
744820
Entamoeba histolytica
ATP + propionate + CoA
-
-
-
r
ATP + acetate + CoA
-
744820
Entamoeba histolytica
ADP + phosphate + acetyl-CoA
-
-
-
r
ATP + propionate + CoA
-
744820
Entamoeba histolytica
ADP + phosphate + propionyl-CoA
-
-
-
r
GDP + phosphate + acetyl-CoA
-
744820
Entamoeba histolytica
GTP + acetate + CoA
-
-
-
r
GTP + acetate + CoA
-
744820
Entamoeba histolytica
GDP + phosphate + acetyl-CoA
-
-
-
r
GTP + acetate + CoA
GTP gives 57% of the activity with ATP
744820
Entamoeba histolytica
GDP + phosphate + acetyl-CoA
-
-
-
r
ITP + acetate + CoA
ITP gives 15% of the activity with ATP
744820
Entamoeba histolytica
IDP + phosphate + acetyl-CoA
-
-
-
r
additional information
the enzyme can utilize both ADP/ATP and GDP/GTP in the respective directions of the reaction. Less than 4% of maximal activity is observed with isobutyrate, valerate, isovalerate, hexanoate, heptanoate, octanoate, succinate, or phenylacetate as the acyl substrate. Activity observed with ATP (representing 100% activity) is nearly double that with GTP (57%) and substantially higher than the activities observed with ITP (15%), CTP (4.1%), or UTP (1.6%), no activity is observed with TTP or diphosphate. Enzymatic activity in the acetate-forming direction is determined by measuring the release of CoA with a sulfhydryl group (CoASH) from acyl-CoA by using Ellman's thiol reagent (DTNB). Production of NTB2- by CoASH cleavage of DTNB is measured spectrophotometrically at 412 nm. Activity in the acetate-forming direction is confirmed using the hexokinase/glucose-6-phosphate dehydrogenase-coupled assay. This assay couples ATP formation to the reduction of NADP+ to NADPH, which is measured spectrophotometrically at 340 nm
744820
Entamoeba histolytica
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
homodimer
2 * 78999, recombinant His6-tagged enzyme, sequence calculation and SDS-PAGE
Entamoeba histolytica
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
37
-
acetate-forming assay at
Entamoeba histolytica
55
-
acetyl-CoA-forming direction
Entamoeba histolytica
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
18
-
phosphate
pH 7.3, 37C, acetate-forming direction, with propionyl-CoA
Entamoeba histolytica
21
-
propionyl-CoA
pH 7.3, 37C, acetate-forming direction, with propionyl-CoA
Entamoeba histolytica
24
-
ADP
pH 7.3, 37C, acetate-forming direction, with propionyl-CoA
Entamoeba histolytica
110
-
acetyl-CoA
pH 7.3, 37C, acetate-forming direction
Entamoeba histolytica
120
-
phosphate
pH 7.3, 37C, acetate-forming direction, with acetyl-CoA
Entamoeba histolytica
140
-
ADP
pH 7.3, 37C, acetate-forming direction, with acetyl-CoA
Entamoeba histolytica
170
-
GDP
pH 7.3, 37C, acetate-forming direction, with acetyl-CoA
Entamoeba histolytica
180
-
GTP
pH 7.3, 37C, acetyl-CoA-forming direction, with acetate
Entamoeba histolytica
190
-
propionate
pH 7.3, 37C, propionyl-CoA-forming direction, with propionate
Entamoeba histolytica
220
-
CoA
pH 7.3, 37C, acetyl-CoA-forming direction, with acetate
Entamoeba histolytica
240
-
acetate
pH 7.3, 37C, acetyl-CoA-forming direction
Entamoeba histolytica
240
-
ATP
pH 7.3, 37C, propionyl-CoA-forming direction, with propionate
Entamoeba histolytica
260
-
CoA
pH 7.3, 37C, propionyl-CoA-forming direction, with propionate
Entamoeba histolytica
320
-
ATP
pH 7.3, 37C, acetyl-CoA-forming direction, with acetate
Entamoeba histolytica
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.3
-
assay at
Entamoeba histolytica
General Information
General Information
Commentary
Organism
physiological function
enzyme ACD is regulated through inhibition by ATP and diphosphate in the acetate-forming direction
Entamoeba histolytica
General Information (protein specific)
General Information
Commentary
Organism
physiological function
enzyme ACD is regulated through inhibition by ATP and diphosphate in the acetate-forming direction
Entamoeba histolytica
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
6.3
-
propionate
pH 7.3, 37C, propionyl-CoA-forming direction, with propionate
Entamoeba histolytica
12
-
phosphate
pH 7.3, 37C, acetate-forming direction, with propionyl-CoA
Entamoeba histolytica
16
-
acetate
pH 7.3, 37C, acetyl-CoA-forming direction
Entamoeba histolytica
18
-
GTP
pH 7.3, 37C, acetyl-CoA-forming direction, with acetate
Entamoeba histolytica
27
-
ATP
pH 7.3, 37C, acetyl-CoA-forming direction, with acetate
Entamoeba histolytica
33
-
ATP
pH 7.3, 37C, propionyl-CoA-forming direction, with propionate
Entamoeba histolytica
34
-
ADP
pH 7.3, 37C, acetate-forming direction, with propionyl-CoA
Entamoeba histolytica
65
-
phosphate
pH 7.3, 37C, acetate-forming direction, with acetyl-CoA
Entamoeba histolytica
89
-
ADP
pH 7.3, 37C, acetate-forming direction, with acetyl-CoA
Entamoeba histolytica
90
-
GDP
pH 7.3, 37C, acetate-forming direction, with acetyl-CoA
Entamoeba histolytica
160
-
CoA
pH 7.3, 37C, propionyl-CoA-forming direction, with propionate
Entamoeba histolytica
650
-
propionyl-CoA
pH 7.3, 37C, acetate-forming direction, with propionyl-CoA
Entamoeba histolytica
1100
-
CoA
pH 7.3, 37C, acetyl-CoA-forming direction, with acetate
Entamoeba histolytica
2600
-
acetyl-CoA
pH 7.3, 37C, acetate-forming direction
Entamoeba histolytica
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
6.3
-
propionate
pH 7.3, 37C, propionyl-CoA-forming direction, with propionate
Entamoeba histolytica
12
-
phosphate
pH 7.3, 37C, acetate-forming direction, with propionyl-CoA
Entamoeba histolytica
16
-
acetate
pH 7.3, 37C, acetyl-CoA-forming direction
Entamoeba histolytica
18
-
GTP
pH 7.3, 37C, acetyl-CoA-forming direction, with acetate
Entamoeba histolytica
27
-
ATP
pH 7.3, 37C, acetyl-CoA-forming direction, with acetate
Entamoeba histolytica
33
-
ATP
pH 7.3, 37C, propionyl-CoA-forming direction, with propionate
Entamoeba histolytica
34
-
ADP
pH 7.3, 37C, acetate-forming direction, with propionyl-CoA
Entamoeba histolytica
65
-
phosphate
pH 7.3, 37C, acetate-forming direction, with acetyl-CoA
Entamoeba histolytica
89
-
ADP
pH 7.3, 37C, acetate-forming direction, with acetyl-CoA
Entamoeba histolytica
90
-
GDP
pH 7.3, 37C, acetate-forming direction, with acetyl-CoA
Entamoeba histolytica
160
-
CoA
pH 7.3, 37C, propionyl-CoA-forming direction, with propionate
Entamoeba histolytica
650
-
propionyl-CoA
pH 7.3, 37C, acetate-forming direction, with propionyl-CoA
Entamoeba histolytica
1100
-
CoA
pH 7.3, 37C, acetyl-CoA-forming direction, with acetate
Entamoeba histolytica
2600
-
acetyl-CoA
pH 7.3, 37C, acetate-forming direction
Entamoeba histolytica
Other publictions for EC 6.2.1.B11
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
735197
Weie
Structure of NDP-forming Acety ...
Candidatus Korarchaeum cryptofilum, Candidatus Korarchaeum cryptofilum OPF8
Proc. Natl. Acad. Sci. USA
113
E519-E528
2016
-
-
-
1
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
746318
Weie
Structure of NDP-forming acet ...
Candidatus Korarchaeum cryptofilum
Proc. Natl. Acad. Sci. USA
113
E519-E528
2016
-
-
-
1
-
-
-
-
-
2
-
1
-
1
-
1
-
-
-
-
-
-
2
2
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
2
-
1
-
-
1
-
-
-
-
-
2
2
-
-
-
-
-
-
-
-
-
2
2
-
-
-
725295
Awano
Characterization of two member ...
Thermococcus kodakarensis
J. Bacteriol.
196
140-147
2014
-
-
1
-
-
-
-
6
-
-
2
-
-
6
-
-
1
-
-
-
-
-
13
1
1
-
2
6
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
6
-
-
2
-
-
-
-
1
-
-
-
-
13
1
1
-
2
6
1
-
-
-
-
-
-
-
6
6
744820
Jones
Biochemical and kinetic chara ...
Entamoeba histolytica
Eukaryot. Cell
13
1530-1537
2014
-
-
1
-
-
-
11
15
-
7
1
2
-
2
-
-
1
-
-
1
-
-
9
1
2
-
-
14
1
-
-
4
-
-
2
-
-
1
4
-
-
-
2
11
-
15
-
7
1
2
-
-
-
1
-
1
-
-
9
1
2
-
-
14
1
-
-
-
-
1
1
-
14
14
651712
Musfeldt
Novel type of ADP-forming acet ...
Archaeoglobus fulgidus, Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661
J. Bacteriol.
184
636-644
2002
-
-
2
-
-
-
-
16
-
8
6
-
-
13
-
-
2
-
-
-
-
-
26
2
2
1
3
13
3
1
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
16
-
11
7
-
-
-
-
3
-
-
-
-
26
3
2
1
3
13
3
1
-
-
-
2
2
-
13
13