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Information on EC 6.2.1.B11 - carboxylic acid-CoA ligase (NDP-forming) and Organism(s) Archaeoglobus fulgidus and UniProt Accession O29057

for references in articles please use BRENDA:EC6.2.1.B11
preliminary BRENDA-supplied EC number
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EC Tree
     6 Ligases
         6.2 Forming carbon-sulfur bonds
             6.2.1 Acid-thiol ligases
                6.2.1.B11 carboxylic acid-CoA ligase (NDP-forming)
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This record set is specific for:
Archaeoglobus fulgidus
UNIPROT: O29057 not found.
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The taxonomic range for the selected organisms is: Archaeoglobus fulgidus
The expected taxonomic range for this enzyme is: Archaea, Eukaryota
Synonyms
af1938, mj0590, af1211, ndp-forming acyl-coa synthetase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetyl CoA synthetase (ADP forming)
-
acetyl coenzyme A synthetase (ADP forming)
-
ADP-forming acetyl coenzyme A synthetase
-
acetyl CoA synthetase (ADP forming)
-
acetyl coenzyme A synthetase (ADP forming)
-
ADP-forming acetyl coenzyme A synthetase
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
carboxylic acid:CoA ligase (NDP-forming)
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
show the reaction diagram
GTP is as effective as ATP as a substrate
-
-
r
ATP + butyrate + CoA
ADP + phosphate + butyryl-CoA
show the reaction diagram
activity is 84% compared to activity with acetate
-
-
r
ATP + fumarate + CoA
ADP + phosphate + fumaryl-CoA
show the reaction diagram
activity is 10% compared to activity with acetate
-
-
?
ATP + indole-3-acetate + CoA
ADP + phosphate + indole-3-acetyl-CoA
show the reaction diagram
activity is 4% compared to activity with acetate
-
-
?
ATP + isobutyrate + CoA
ADP + phosphate + isobutyryl-CoA
show the reaction diagram
activity is 56% compared to activity with acetate
-
-
?
ATP + isovalerate + CoA
ADP + phosphate + isovaleryl-CoA
show the reaction diagram
activity is 10% compared to activity with acetate
-
-
?
ATP + phenylacetate + CoA
ADP + phosphate + phenylacetyl-CoA
show the reaction diagram
activity is 10% compared to activity with acetate
-
-
?
ATP + propionate + CoA
ADP + phosphate + propionyl-CoA
show the reaction diagram
propionate is as effective as acetate as substrate
-
-
r
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
activity is 9% compared to activity with acetate
-
-
?
GTP + acetate + CoA
GDP + phosphate + acetyl-CoA
show the reaction diagram
GTP is as effective as ATP as a substrate
-
-
r
ADP + phosphate + indole-3-acetyl-CoA
ATP + indole-3-acetate + CoA
show the reaction diagram
-
-
-
r
ADP + phosphate + phenylacetyl-CoA
ATP + phenylacetate + CoA
show the reaction diagram
-
-
-
r
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
show the reaction diagram
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
-
-
?
ATP + butyrate + CoA
ADP + phosphate + butyryl-CoA
show the reaction diagram
activity is 36% compared to activity with phenylacetate
-
-
?
ATP + fumarate + CoA
ADP + phosphate + fumaryl-CoA
show the reaction diagram
activity is 29% compared to activity with phenylacetate
-
-
?
ATP + indole-3-acetate + CoA
ADP + phosphate + indole-3-acetyl-CoA
show the reaction diagram
the enzyme shows the highest activity with the aryl acids, indoleacetate (100%) and phenylacetate (65%), as compared to acetate (10-13%)
-
-
r
ATP + isobutyrate + CoA
ADP + phosphate + isobutyryl-CoA
show the reaction diagram
activity is 31% compared to activity with phenylacetate
-
-
?
ATP + isovalerate + CoA
ADP + phosphate + isovaleryl-CoA
show the reaction diagram
activity is 18% compared to activity with phenylacetate
-
-
?
ATP + phenylacetate + CoA
ADP + phosphate + phenylacetyl-CoA
show the reaction diagram
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%)
-
-
r
ATP + propionate + CoA
ADP + phosphate + propionyl-CoA
show the reaction diagram
activity is 42% compared to activity with phenylacetate
-
-
?
GTP + indole-3-acetate + CoA
GDP + phosphate + indole-3-acetyl-CoA
show the reaction diagram
ATP (100%) is effectively replaced by GTP (70%)
-
-
?
GTP + phenylacetate + CoA
GDP + phosphate + phenylacetyl-CoA
show the reaction diagram
ATP (100%) is effectively replaced by GTP (70%)
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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+
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+
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+
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+
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+
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+
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+
Cu2+
activity depends on divalent cations. Mg2+which is most effective, could partially be replaced by Mn2+, Zn2+, and Cu2+ (each 30 to 40%)
Mg2+
activity depends on divalent cations. Mg2+which is most effective, could partially be replaced by Mn2+, Zn2+, and Cu2+ (each 30 to 40%)
Mn2+
activity depends on divalent cations. Mg2+which is most effective, could partially be replaced by Mn2+, Zn2+, and Cu2+ (each 30 to 40%)
Zn2+
activity depends on divalent cations. Mg2+which is most effective, could partially be replaced by Mn2+, Zn2+, and Cu2+ (each 30 to 40%)
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.34
acetate
pH 8.0, 55°C
0.01
acetyl-CoA
pH 8.0, 55°C
0.007
ADP
pH 8.0, 55°C
0.13
ATP
pH 8.0, 55°C
0.025
CoA
pH 8.0, 55°C
0.11
phenylacetate
pH 8.0, 55°C
0.11
phosphate
pH 8.0, 55°C
2.58
acetate
pH 8.0, 55°C
0.03
ATP
pH 8.0, 55°C
0.53
CoA
pH 8.0, 55°C
1.24
indole-3-acetate
pH 8.0, 55°C
2.5
phenylacetate
pH 8.0, 55°C
0.017
phenylacetyl-CoA
pH 8.0, 55°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
138
acetate
pH 8.0, 55°C
95
acetyl-CoA
pH 8.0, 55°C
150
ATP
pH 8.0, 55°C
110
CoA
pH 8.0, 55°C
11.5
phenylacetate
pH 8.0, 55°C
58
phosphate
pH 8.0, 55°C
1.84
acetate
pH 8.0, 55°C
2.9
CoA
pH 8.0, 55°C
3.45
indole-3-acetate
pH 8.0, 55°C
3
phenylacetate
pH 8.0, 55°C
2.3
phenylacetyl-CoA
pH 8.0, 55°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
400
acetate
pH 8.0, 55°C
9200
acetyl-CoA
pH 8.0, 55°C
10000
ADP
pH 8.0, 55°C
1120
ATP
pH 8.0, 55°C
4000
CoA
pH 8.0, 55°C
111
phenylacetate
pH 8.0, 55°C
520
phosphate
pH 8.0, 55°C
0.7
acetate
pH 8.0, 55°C
100
ATP
pH 8.0, 55°C
5.4
CoA
pH 8.0, 55°C
2.7
indole-3-acetate
pH 8.0, 55°C
1.2
phenylacetate
pH 8.0, 55°C
140
phenylacetyl-CoA
pH 8.0, 55°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8
about 50% of the maximal activity is found at pH 6 and 8
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60 - 80
60°C: about 55% of maximal activity, 80°C: 80% of maximal activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the enzyme is involved in acetate formation and energy conservation
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
140000
gel filtration
7000
2 * 7000, SDS-PAGE
140000
gel filtration
72000
2 * 72000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
2 * 7000, SDS-PAGE
homodimer
2 * 72000, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70
5 h, about 30% loss of activity
80
150 min, about 65% loss of activity
85
30 min, about 80% loss of activity. Almost complete loss of activity after 100 min
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpressed in Escherichia coli
overexpressed in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Musfeldt, M.; Schonheit, P.
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
J. Bacteriol.
184
636-644
2002
Archaeoglobus fulgidus (O28341), Archaeoglobus fulgidus (O29057), Archaeoglobus fulgidus, Methanocaldococcus jannaschii (Q58010), Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661 (Q58010)
Manually annotated by BRENDA team