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show all sequences of 6.2.1.B11

Novel type of ADP-forming acetyl coenzyme A synthetase in hyperthermophilic archaea: heterologous expression and characterization of isoenzymes from the sulfate reducer Archaeoglobus fulgidus and the methanogen Methanococcus jannaschii

Musfeldt, M.; Schonheit, P.; J. Bacteriol. 184, 636-644 (2002)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
overexpressed in Escherichia coli
Methanocaldococcus jannaschii
overexpressed in Escherichia coli; overexpressed in Escherichia coli
Archaeoglobus fulgidus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.007
-
ADP
pH 8.0, 55°C
Archaeoglobus fulgidus
0.01
-
acetyl-CoA
pH 8.0, 55°C
Archaeoglobus fulgidus
0.015
-
ADP
pH 8.0, 55°C
Methanocaldococcus jannaschii
0.017
-
phenylacetyl-CoA
pH 8.0, 55°C
Archaeoglobus fulgidus
0.025
-
CoA
pH 8.0, 55°C
Archaeoglobus fulgidus
0.03
-
ATP
pH 8.0, 55°C
Archaeoglobus fulgidus
0.037
-
acetyl-CoA
pH 8.0, 55°C
Methanocaldococcus jannaschii
0.11
-
phenylacetate
pH 8.0, 55°C
Archaeoglobus fulgidus
0.11
-
phosphate
pH 8.0, 55°C
Archaeoglobus fulgidus
0.13
-
ATP
pH 8.0, 55°C
Archaeoglobus fulgidus
0.34
-
acetate
pH 8.0, 55°C
Archaeoglobus fulgidus
0.47
-
phosphate
pH 8.0, 55°C
Methanocaldococcus jannaschii
0.53
-
CoA
pH 8.0, 55°C
Archaeoglobus fulgidus
1.24
-
indole-3-acetate
pH 8.0, 55°C
Archaeoglobus fulgidus
2.5
-
phenylacetate
pH 8.0, 55°C
Archaeoglobus fulgidus
2.58
-
acetate
pH 8.0, 55°C
Archaeoglobus fulgidus
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Ca2+
enzyme activity requires divalent cations. Mg2+(100%), which is the most effective, can be partially replaced by Co2+ (51%), Mn2+ (38%), and to a lesser extent (less than 20%) by Fe2+, Zn2+, Ni2+, Ca2+, and Cu2+
Archaeoglobus fulgidus
Co2+
enzyme activity requires divalent cations. Mg2+(100%), which is the most effective, can be partially replaced by Co2+ (51%), Mn2+ (38%), and to a lesser extent (less than 20%) by Fe2+, Zn2+, Ni2+, Ca2+, and Cu2+
Archaeoglobus fulgidus
Cu2+
activity depends on divalent cations. Mg2+which is most effective, could partially be replaced by Mn2+, Zn2+, and Cu2+ (each 30 to 40%); enzyme activity requires divalent cations. Mg2+(100%), which is the most effective, can be partially replaced by Co2+ (51%), Mn2+ (38%), and to a lesser extent (less than 20%) by Fe2+, Zn2+, Ni2+, Ca2+, and Cu2+
Archaeoglobus fulgidus
Fe2+
enzyme activity requires divalent cations. Mg2+(100%), which is the most effective, can be partially replaced by Co2+ (51%), Mn2+ (38%), and to a lesser extent (less than 20%) by Fe2+, Zn2+, Ni2+, Ca2+, and Cu2+
Archaeoglobus fulgidus
Mg2+
activity depends on divalent cations. Mg2+which is most effective, could partially be replaced by Mn2+, Zn2+, and Cu2+ (each 30 to 40%); enzyme activity requires divalent cations. Mg2+(100%), which is the most effective, can be partially replaced by Co2+ (51%), Mn2+ (38%), and to a lesser extent (less than 20%) by Fe2+, Zn2+, Ni2+, Ca2+, and Cu2+
Archaeoglobus fulgidus
Mn2+
activity depends on divalent cations. Mg2+which is most effective, could partially be replaced by Mn2+, Zn2+, and Cu2+ (each 30 to 40%); enzyme activity requires divalent cations. Mg2+(100%), which is the most effective, can be partially replaced by Co2+ (51%), Mn2+ (38%), and to a lesser extent (less than 20%) by Fe2+, Zn2+, Ni2+, Ca2+, and Cu2+
Archaeoglobus fulgidus
Ni2+
enzyme activity requires divalent cations. Mg2+(100%), which is the most effective, can be partially replaced by Co2+ (51%), Mn2+ (38%), and to a lesser extent (less than 20%) by Fe2+, Zn2+, Ni2+, Ca2+, and Cu2+
Archaeoglobus fulgidus
Zn2+
activity depends on divalent cations. Mg2+which is most effective, could partially be replaced by Mn2+, Zn2+, and Cu2+ (each 30 to 40%)
Archaeoglobus fulgidus
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
7000
-
2 * 7000, SDS-PAGE
Archaeoglobus fulgidus
7400
-
2 * 7400, SDS-PAGE
Methanocaldococcus jannaschii
72000
-
2 * 72000, SDS-PAGE
Archaeoglobus fulgidus
78172
-
2 * 78172, calculated from sequence
Methanocaldococcus jannaschii
140000
-
gel filtration; gel filtration
Archaeoglobus fulgidus
160000
-
gel filtration
Methanocaldococcus jannaschii
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Archaeoglobus fulgidus
O28341
-
-
Archaeoglobus fulgidus
O29057
-
-
Methanocaldococcus jannaschii
Q58010
-
-
Methanocaldococcus jannaschii DSM 2661
Q58010
-
-
Purification (Commentary)
Commentary
Organism
recombinant enzyme
Methanocaldococcus jannaschii
recombinant enzyme; recombinant enzyme
Archaeoglobus fulgidus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ADP + phosphate + acetyl-CoA
the enzyme is specific for acetyl-CoA (100%) and butyryl-CoA (120%) but does not take phenylacetyl-CoA (0%). A significant rate of the reverse reaction direction, i.e., the ATP- and CoA-dependent conversion of acetate or butyrate to the corresponding CoA esters, can not be demonstrated
651712
Methanocaldococcus jannaschii
ATP + acetate + CoA
-
-
-
ir
ADP + phosphate + acetyl-CoA
the enzyme is specific for acetyl-CoA (100%) and butyryl-CoA (120%) but does not take phenylacetyl-CoA (0%). A significant rate of the reverse reaction direction, i.e., the ATP- and CoA-dependent conversion of acetate or butyrate to the corresponding CoA esters, can not be demonstrated
651712
Methanocaldococcus jannaschii DSM 2661
ATP + acetate + CoA
-
-
-
ir
ADP + phosphate + butyryl-CoA
the enzyme is specific for acetyl-CoA (100%) and butyryl-CoA (120%) but does not take phenylacetyl-CoA (0%)
651712
Methanocaldococcus jannaschii
ATP + butyrate + CoA
-
-
-
?
ADP + phosphate + butyryl-CoA
the enzyme is specific for acetyl-CoA (100%) and butyryl-CoA (120%) but does not take phenylacetyl-CoA (0%)
651712
Methanocaldococcus jannaschii DSM 2661
ATP + butyrate + CoA
-
-
-
?
ADP + phosphate + indole-3-acetyl-CoA
-
651712
Archaeoglobus fulgidus
ATP + indole-3-acetate + CoA
-
-
-
r
ADP + phosphate + phenylacetyl-CoA
-
651712
Archaeoglobus fulgidus
ATP + phenylacetate + CoA
-
-
-
r
ATP + acetate + CoA
activity is 13% compared to activity with phenylacetate. At 1 mM acetyl-CoA, the enzyme activity is less than 2% of the rate obtained with phenylacetyl-CoA
651712
Archaeoglobus fulgidus
ADP + phosphate + acetyl-CoA
-
-
-
?
ATP + acetate + CoA
GTP is as effective as ATP as a substrate
651712
Archaeoglobus fulgidus
ADP + phosphate + acetyl-CoA
-
-
-
r
ATP + butyrate + CoA
activity is 36% compared to activity with phenylacetate
651712
Archaeoglobus fulgidus
ADP + phosphate + butyryl-CoA
-
-
-
?
ATP + butyrate + CoA
activity is 84% compared to activity with acetate
651712
Archaeoglobus fulgidus
ADP + phosphate + butyryl-CoA
-
-
-
r
ATP + fumarate + CoA
activity is 10% compared to activity with acetate
651712
Archaeoglobus fulgidus
ADP + phosphate + fumaryl-CoA
-
-
-
?
ATP + fumarate + CoA
activity is 29% compared to activity with phenylacetate
651712
Archaeoglobus fulgidus
ADP + phosphate + fumaryl-CoA
-
-
-
?
ATP + indole-3-acetate + CoA
the enzyme shows the highest activity with the aryl acids, indoleacetate (100%) and phenylacetate (65%), as compared to acetate (10-13%)
651712
Archaeoglobus fulgidus
ADP + phosphate + indole-3-acetyl-CoA
-
-
-
r
ATP + indole-3-acetate + CoA
activity is 4% compared to activity with acetate
651712
Archaeoglobus fulgidus
ADP + phosphate + phenylacetyl-CoA
-
-
-
?
ATP + isobutyrate + CoA
activity is 31% compared to activity with phenylacetate
651712
Archaeoglobus fulgidus
ADP + phosphate + isobutyryl-CoA
-
-
-
?
ATP + isobutyrate + CoA
activity is 56% compared to activity with acetate
651712
Archaeoglobus fulgidus
ADP + phosphate + isobutyryl-CoA
-
-
-
?
ATP + isovalerate + CoA
activity is 10% compared to activity with acetate
651712
Archaeoglobus fulgidus
ADP + phosphate + isovaleryl-CoA
-
-
-
?
ATP + isovalerate + CoA
activity is 18% compared to activity with phenylacetate
651712
Archaeoglobus fulgidus
ADP + phosphate + isovaleryl-CoA
-
-
-
?
ATP + phenylacetate + CoA
activity is 10% compared to activity with acetate
651712
Archaeoglobus fulgidus
ADP + phosphate + phenylacetyl-CoA
-
-
-
?
ATP + phenylacetate + CoA
the enzyme shows the highest activity with the aryl acids, indoleacetate (100%) and phenylacetate (65%), as compared to acetate (10-13%). ATP (100%) is effectively replaced by GTP (70%)
651712
Archaeoglobus fulgidus
ADP + phosphate + phenylacetyl-CoA
-
-
-
r
ATP + propionate + CoA
activity is 42% compared to activity with phenylacetate
651712
Archaeoglobus fulgidus
ADP + phosphate + propionyl-CoA
-
-
-
?
ATP + propionate + CoA
propionate is as effective as acetate as substrate
651712
Archaeoglobus fulgidus
ADP + phosphate + propionyl-CoA
-
-
-
r
ATP + succinate + CoA
activity is 9% compared to activity with acetate
651712
Archaeoglobus fulgidus
ADP + phosphate + succinyl-CoA
-
-
-
?
GTP + acetate + CoA
GTP is as effective as ATP as a substrate
651712
Archaeoglobus fulgidus
GDP + phosphate + acetyl-CoA
-
-
-
r
GTP + indole-3-acetate + CoA
ATP (100%) is effectively replaced by GTP (70%)
651712
Archaeoglobus fulgidus
GDP + phosphate + indole-3-acetyl-CoA
-
-
-
?
GTP + phenylacetate + CoA
ATP (100%) is effectively replaced by GTP (70%)
651712
Archaeoglobus fulgidus
GDP + phosphate + phenylacetyl-CoA
-
-
-
?
Subunits
Subunits
Commentary
Organism
homodimer
2 * 7000, SDS-PAGE; 2 * 72000, SDS-PAGE
Archaeoglobus fulgidus
homodimer
2 * 7400, SDS-PAGE; 2 * 78172, calculated from sequence
Methanocaldococcus jannaschii
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
55
-
assay at
Methanocaldococcus jannaschii
77
-
-
Archaeoglobus fulgidus
Temperature Range [°C]
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
60
80
60°C: about 55% of maximal activity, 80°C: 80% of maximal activity
Archaeoglobus fulgidus
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
70
-
5 h, about 30% loss of activity
Archaeoglobus fulgidus
80
-
150 min, about 65% loss of activity
Archaeoglobus fulgidus
85
-
30 min, about 80% loss of activity. Almost complete loss of activity after 100 min
Archaeoglobus fulgidus
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
1.84
-
acetate
pH 8.0, 55°C
Archaeoglobus fulgidus
2.3
-
phenylacetyl-CoA
pH 8.0, 55°C
Archaeoglobus fulgidus
2.9
-
CoA
pH 8.0, 55°C
Archaeoglobus fulgidus
3
-
ATP
pH 8.0, 55°C
Archaeoglobus fulgidus
3
-
phenylacetate
pH 8.0, 55°C
Archaeoglobus fulgidus
3.45
-
indole-3-acetate
pH 8.0, 55°C
Archaeoglobus fulgidus
11.5
-
phenylacetate
pH 8.0, 55°C
Archaeoglobus fulgidus
58
-
phosphate
pH 8.0, 55°C
Archaeoglobus fulgidus
70
-
ADP
pH 8.0, 55°C
Archaeoglobus fulgidus
95
-
acetyl-CoA
pH 8.0, 55°C
Archaeoglobus fulgidus
110
-
CoA
pH 8.0, 55°C
Archaeoglobus fulgidus
138
-
acetate
pH 8.0, 55°C
Archaeoglobus fulgidus
150
-
ATP
pH 8.0, 55°C
Archaeoglobus fulgidus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
-
Archaeoglobus fulgidus
8
-
assay at
Archaeoglobus fulgidus
8
-
assay at
Methanocaldococcus jannaschii
pH Range
pH Minimum
pH Maximum
Commentary
Organism
6
8
about 50% of the maximal activity is found at pH 6 and 8
Archaeoglobus fulgidus
Cloned(Commentary) (protein specific)
Commentary
Organism
overexpressed in Escherichia coli
Archaeoglobus fulgidus
overexpressed in Escherichia coli
Methanocaldococcus jannaschii
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.007
-
ADP
pH 8.0, 55°C
Archaeoglobus fulgidus
0.01
-
acetyl-CoA
pH 8.0, 55°C
Archaeoglobus fulgidus
0.015
-
ADP
pH 8.0, 55°C
Methanocaldococcus jannaschii
0.017
-
phenylacetyl-CoA
pH 8.0, 55°C
Archaeoglobus fulgidus
0.025
-
CoA
pH 8.0, 55°C
Archaeoglobus fulgidus
0.03
-
ATP
pH 8.0, 55°C
Archaeoglobus fulgidus
0.037
-
acetyl-CoA
pH 8.0, 55°C
Methanocaldococcus jannaschii
0.11
-
phenylacetate
pH 8.0, 55°C
Archaeoglobus fulgidus
0.11
-
phosphate
pH 8.0, 55°C
Archaeoglobus fulgidus
0.13
-
ATP
pH 8.0, 55°C
Archaeoglobus fulgidus
0.34
-
acetate
pH 8.0, 55°C
Archaeoglobus fulgidus
0.47
-
phosphate
pH 8.0, 55°C
Methanocaldococcus jannaschii
0.53
-
CoA
pH 8.0, 55°C
Archaeoglobus fulgidus
1.24
-
indole-3-acetate
pH 8.0, 55°C
Archaeoglobus fulgidus
2.5
-
phenylacetate
pH 8.0, 55°C
Archaeoglobus fulgidus
2.58
-
acetate
pH 8.0, 55°C
Archaeoglobus fulgidus
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Ca2+
enzyme activity requires divalent cations. Mg2+(100%), which is the most effective, can be partially replaced by Co2+ (51%), Mn2+ (38%), and to a lesser extent (less than 20%) by Fe2+, Zn2+, Ni2+, Ca2+, and Cu2+
Archaeoglobus fulgidus
Co2+
enzyme activity requires divalent cations. Mg2+(100%), which is the most effective, can be partially replaced by Co2+ (51%), Mn2+ (38%), and to a lesser extent (less than 20%) by Fe2+, Zn2+, Ni2+, Ca2+, and Cu2+
Archaeoglobus fulgidus
Cu2+
activity depends on divalent cations. Mg2+which is most effective, could partially be replaced by Mn2+, Zn2+, and Cu2+ (each 30 to 40%)
Archaeoglobus fulgidus
Cu2+
enzyme activity requires divalent cations. Mg2+(100%), which is the most effective, can be partially replaced by Co2+ (51%), Mn2+ (38%), and to a lesser extent (less than 20%) by Fe2+, Zn2+, Ni2+, Ca2+, and Cu2+
Archaeoglobus fulgidus
Fe2+
enzyme activity requires divalent cations. Mg2+(100%), which is the most effective, can be partially replaced by Co2+ (51%), Mn2+ (38%), and to a lesser extent (less than 20%) by Fe2+, Zn2+, Ni2+, Ca2+, and Cu2+
Archaeoglobus fulgidus
Mg2+
activity depends on divalent cations. Mg2+which is most effective, could partially be replaced by Mn2+, Zn2+, and Cu2+ (each 30 to 40%)
Archaeoglobus fulgidus
Mg2+
enzyme activity requires divalent cations. Mg2+(100%), which is the most effective, can be partially replaced by Co2+ (51%), Mn2+ (38%), and to a lesser extent (less than 20%) by Fe2+, Zn2+, Ni2+, Ca2+, and Cu2+
Archaeoglobus fulgidus
Mn2+
activity depends on divalent cations. Mg2+which is most effective, could partially be replaced by Mn2+, Zn2+, and Cu2+ (each 30 to 40%)
Archaeoglobus fulgidus
Mn2+
enzyme activity requires divalent cations. Mg2+(100%), which is the most effective, can be partially replaced by Co2+ (51%), Mn2+ (38%), and to a lesser extent (less than 20%) by Fe2+, Zn2+, Ni2+, Ca2+, and Cu2+
Archaeoglobus fulgidus
Ni2+
enzyme activity requires divalent cations. Mg2+(100%), which is the most effective, can be partially replaced by Co2+ (51%), Mn2+ (38%), and to a lesser extent (less than 20%) by Fe2+, Zn2+, Ni2+, Ca2+, and Cu2+
Archaeoglobus fulgidus
Zn2+
activity depends on divalent cations. Mg2+which is most effective, could partially be replaced by Mn2+, Zn2+, and Cu2+ (each 30 to 40%)
Archaeoglobus fulgidus
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
7000
-
2 * 7000, SDS-PAGE
Archaeoglobus fulgidus
7400
-
2 * 7400, SDS-PAGE
Methanocaldococcus jannaschii
72000
-
2 * 72000, SDS-PAGE
Archaeoglobus fulgidus
78172
-
2 * 78172, calculated from sequence
Methanocaldococcus jannaschii
140000
-
gel filtration
Archaeoglobus fulgidus
160000
-
gel filtration
Methanocaldococcus jannaschii
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant enzyme
Archaeoglobus fulgidus
recombinant enzyme
Methanocaldococcus jannaschii
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ADP + phosphate + acetyl-CoA
the enzyme is specific for acetyl-CoA (100%) and butyryl-CoA (120%) but does not take phenylacetyl-CoA (0%). A significant rate of the reverse reaction direction, i.e., the ATP- and CoA-dependent conversion of acetate or butyrate to the corresponding CoA esters, can not be demonstrated
651712
Methanocaldococcus jannaschii
ATP + acetate + CoA
-
-
-
ir
ADP + phosphate + acetyl-CoA
the enzyme is specific for acetyl-CoA (100%) and butyryl-CoA (120%) but does not take phenylacetyl-CoA (0%). A significant rate of the reverse reaction direction, i.e., the ATP- and CoA-dependent conversion of acetate or butyrate to the corresponding CoA esters, can not be demonstrated
651712
Methanocaldococcus jannaschii DSM 2661
ATP + acetate + CoA
-
-
-
ir
ADP + phosphate + butyryl-CoA
the enzyme is specific for acetyl-CoA (100%) and butyryl-CoA (120%) but does not take phenylacetyl-CoA (0%)
651712
Methanocaldococcus jannaschii
ATP + butyrate + CoA
-
-
-
?
ADP + phosphate + butyryl-CoA
the enzyme is specific for acetyl-CoA (100%) and butyryl-CoA (120%) but does not take phenylacetyl-CoA (0%)
651712
Methanocaldococcus jannaschii DSM 2661
ATP + butyrate + CoA
-
-
-
?
ADP + phosphate + indole-3-acetyl-CoA
-
651712
Archaeoglobus fulgidus
ATP + indole-3-acetate + CoA
-
-
-
r
ADP + phosphate + phenylacetyl-CoA
-
651712
Archaeoglobus fulgidus
ATP + phenylacetate + CoA
-
-
-
r
ATP + acetate + CoA
activity is 13% compared to activity with phenylacetate. At 1 mM acetyl-CoA, the enzyme activity is less than 2% of the rate obtained with phenylacetyl-CoA
651712
Archaeoglobus fulgidus
ADP + phosphate + acetyl-CoA
-
-
-
?
ATP + acetate + CoA
GTP is as effective as ATP as a substrate
651712
Archaeoglobus fulgidus
ADP + phosphate + acetyl-CoA
-
-
-
r
ATP + butyrate + CoA
activity is 36% compared to activity with phenylacetate
651712
Archaeoglobus fulgidus
ADP + phosphate + butyryl-CoA
-
-
-
?
ATP + butyrate + CoA
activity is 84% compared to activity with acetate
651712
Archaeoglobus fulgidus
ADP + phosphate + butyryl-CoA
-
-
-
r
ATP + fumarate + CoA
activity is 10% compared to activity with acetate
651712
Archaeoglobus fulgidus
ADP + phosphate + fumaryl-CoA
-
-
-
?
ATP + fumarate + CoA
activity is 29% compared to activity with phenylacetate
651712
Archaeoglobus fulgidus
ADP + phosphate + fumaryl-CoA
-
-
-
?
ATP + indole-3-acetate + CoA
the enzyme shows the highest activity with the aryl acids, indoleacetate (100%) and phenylacetate (65%), as compared to acetate (10-13%)
651712
Archaeoglobus fulgidus
ADP + phosphate + indole-3-acetyl-CoA
-
-
-
r
ATP + indole-3-acetate + CoA
activity is 4% compared to activity with acetate
651712
Archaeoglobus fulgidus
ADP + phosphate + phenylacetyl-CoA
-
-
-
?
ATP + isobutyrate + CoA
activity is 31% compared to activity with phenylacetate
651712
Archaeoglobus fulgidus
ADP + phosphate + isobutyryl-CoA
-
-
-
?
ATP + isobutyrate + CoA
activity is 56% compared to activity with acetate
651712
Archaeoglobus fulgidus
ADP + phosphate + isobutyryl-CoA
-
-
-
?
ATP + isovalerate + CoA
activity is 10% compared to activity with acetate
651712
Archaeoglobus fulgidus
ADP + phosphate + isovaleryl-CoA
-
-
-
?
ATP + isovalerate + CoA
activity is 18% compared to activity with phenylacetate
651712
Archaeoglobus fulgidus
ADP + phosphate + isovaleryl-CoA
-
-
-
?
ATP + phenylacetate + CoA
activity is 10% compared to activity with acetate
651712
Archaeoglobus fulgidus
ADP + phosphate + phenylacetyl-CoA
-
-
-
?
ATP + phenylacetate + CoA
the enzyme shows the highest activity with the aryl acids, indoleacetate (100%) and phenylacetate (65%), as compared to acetate (10-13%). ATP (100%) is effectively replaced by GTP (70%)
651712
Archaeoglobus fulgidus
ADP + phosphate + phenylacetyl-CoA
-
-
-
r
ATP + propionate + CoA
activity is 42% compared to activity with phenylacetate
651712
Archaeoglobus fulgidus
ADP + phosphate + propionyl-CoA
-
-
-
?
ATP + propionate + CoA
propionate is as effective as acetate as substrate
651712
Archaeoglobus fulgidus
ADP + phosphate + propionyl-CoA
-
-
-
r
ATP + succinate + CoA
activity is 9% compared to activity with acetate
651712
Archaeoglobus fulgidus
ADP + phosphate + succinyl-CoA
-
-
-
?
GTP + acetate + CoA
GTP is as effective as ATP as a substrate
651712
Archaeoglobus fulgidus
GDP + phosphate + acetyl-CoA
-
-
-
r
GTP + indole-3-acetate + CoA
ATP (100%) is effectively replaced by GTP (70%)
651712
Archaeoglobus fulgidus
GDP + phosphate + indole-3-acetyl-CoA
-
-
-
?
GTP + phenylacetate + CoA
ATP (100%) is effectively replaced by GTP (70%)
651712
Archaeoglobus fulgidus
GDP + phosphate + phenylacetyl-CoA
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
homodimer
2 * 72000, SDS-PAGE
Archaeoglobus fulgidus
homodimer
2 * 7000, SDS-PAGE
Archaeoglobus fulgidus
homodimer
2 * 7400, SDS-PAGE; 2 * 78172, calculated from sequence
Methanocaldococcus jannaschii
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
55
-
assay at
Methanocaldococcus jannaschii
77
-
-
Archaeoglobus fulgidus
Temperature Range [°C] (protein specific)
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
60
80
60°C: about 55% of maximal activity, 80°C: 80% of maximal activity
Archaeoglobus fulgidus
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
70
-
5 h, about 30% loss of activity
Archaeoglobus fulgidus
80
-
150 min, about 65% loss of activity
Archaeoglobus fulgidus
85
-
30 min, about 80% loss of activity. Almost complete loss of activity after 100 min
Archaeoglobus fulgidus
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
1.84
-
acetate
pH 8.0, 55°C
Archaeoglobus fulgidus
2.3
-
phenylacetyl-CoA
pH 8.0, 55°C
Archaeoglobus fulgidus
2.9
-
CoA
pH 8.0, 55°C
Archaeoglobus fulgidus
3
-
ATP
pH 8.0, 55°C
Archaeoglobus fulgidus
3
-
phenylacetate
pH 8.0, 55°C
Archaeoglobus fulgidus
3.45
-
indole-3-acetate
pH 8.0, 55°C
Archaeoglobus fulgidus
11.5
-
phenylacetate
pH 8.0, 55°C
Archaeoglobus fulgidus
58
-
phosphate
pH 8.0, 55°C
Archaeoglobus fulgidus
70
-
ADP
pH 8.0, 55°C
Archaeoglobus fulgidus
95
-
acetyl-CoA
pH 8.0, 55°C
Archaeoglobus fulgidus
110
-
CoA
pH 8.0, 55°C
Archaeoglobus fulgidus
138
-
acetate
pH 8.0, 55°C
Archaeoglobus fulgidus
150
-
ATP
pH 8.0, 55°C
Archaeoglobus fulgidus
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
-
Archaeoglobus fulgidus
8
-
assay at
Archaeoglobus fulgidus
8
-
assay at
Methanocaldococcus jannaschii
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
6
8
about 50% of the maximal activity is found at pH 6 and 8
Archaeoglobus fulgidus
General Information
General Information
Commentary
Organism
physiological function
the enzyme is involved in acetate formation and energy conservation
Archaeoglobus fulgidus
physiological function
the enzyme is involved in acetate formation and energy conservation
Methanocaldococcus jannaschii
General Information (protein specific)
General Information
Commentary
Organism
physiological function
the enzyme is involved in acetate formation and energy conservation
Archaeoglobus fulgidus
physiological function
the enzyme is involved in acetate formation and energy conservation
Methanocaldococcus jannaschii
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.7
-
acetate
pH 8.0, 55°C
Archaeoglobus fulgidus
1.2
-
phenylacetate
pH 8.0, 55°C
Archaeoglobus fulgidus
2.7
-
indole-3-acetate
pH 8.0, 55°C
Archaeoglobus fulgidus
5.4
-
CoA
pH 8.0, 55°C
Archaeoglobus fulgidus
100
-
ATP
pH 8.0, 55°C
Archaeoglobus fulgidus
111
-
phenylacetate
pH 8.0, 55°C
Archaeoglobus fulgidus
140
-
phenylacetyl-CoA
pH 8.0, 55°C
Archaeoglobus fulgidus
400
-
acetate
pH 8.0, 55°C
Archaeoglobus fulgidus
520
-
phosphate
pH 8.0, 55°C
Archaeoglobus fulgidus
1120
-
ATP
pH 8.0, 55°C
Archaeoglobus fulgidus
4000
-
CoA
pH 8.0, 55°C
Archaeoglobus fulgidus
9200
-
acetyl-CoA
pH 8.0, 55°C
Archaeoglobus fulgidus
10000
-
ADP
pH 8.0, 55°C
Archaeoglobus fulgidus
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.7
-
acetate
pH 8.0, 55°C
Archaeoglobus fulgidus
1.2
-
phenylacetate
pH 8.0, 55°C
Archaeoglobus fulgidus
2.7
-
indole-3-acetate
pH 8.0, 55°C
Archaeoglobus fulgidus
5.4
-
CoA
pH 8.0, 55°C
Archaeoglobus fulgidus
100
-
ATP
pH 8.0, 55°C
Archaeoglobus fulgidus
111
-
phenylacetate
pH 8.0, 55°C
Archaeoglobus fulgidus
140
-
phenylacetyl-CoA
pH 8.0, 55°C
Archaeoglobus fulgidus
400
-
acetate
pH 8.0, 55°C
Archaeoglobus fulgidus
520
-
phosphate
pH 8.0, 55°C
Archaeoglobus fulgidus
1120
-
ATP
pH 8.0, 55°C
Archaeoglobus fulgidus
4000
-
CoA
pH 8.0, 55°C
Archaeoglobus fulgidus
9200
-
acetyl-CoA
pH 8.0, 55°C
Archaeoglobus fulgidus
10000
-
ADP
pH 8.0, 55°C
Archaeoglobus fulgidus
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
Weiße
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
Weiße
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