Information on EC 6.2.1.B11 - carboxylic acid-CoA ligase (NDP-forming)

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
6.2.1.B11
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
carboxylic acid-CoA ligase (NDP-forming)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
NTP + a carboxylate + CoA = NDP + phosphate + an acyl-CoA
show the reaction diagram
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
carboxylic acid:CoA ligase (NDP-forming)
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Q5JIA8: alpha-subunit, Q5JIA9: beta-subunit
Q5JIA8 and Q5JIA9
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
show the reaction diagram
ADP + phosphate + butyryl-CoA
ATP + butyrate + CoA
show the reaction diagram
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 + 2-(4-hydroxyphenyl)acetate + CoA
ADP + phosphate + 2-(4-hydroxyphenyl)acetyl-CoA
show the reaction diagram
Q5JIA8 and Q5JIA9
the enzyme accommodates a broad range of acids that correspond to those generated in the oxidative metabolism of Ala, Val, Leu, Ile, Met, Phe, and Cys
-
-
?
ATP + 2-(indol-3-yl)acetate + CoA
ADP + phosphate + 2-(indol-3-yl)acetyl-CoA
show the reaction diagram
Q5JIA8 and Q5JIA9
low activity. Low activity. The enzyme accommodates a broad range of acids that correspond to those generated in the oxidative metabolism of Ala, Val, Leu, Ile, Met, Phe, and Cys
-
-
?
ATP + 2-methylbutyrate + CoA
ADP + phosphate + 2-methylbutyryl-CoA
show the reaction diagram
Q5JIA8 and Q5JIA9
the enzyme accommodates a broad range of acids that correspond to those generated in the oxidative metabolism of Ala, Val, Leu, Ile, Met, Phe, and Cys
-
-
?
ATP + 3-methylthiopropionate + CoA
ADP + phosphate + 3-methylthiopropionyl-CoA
show the reaction diagram
Q5JIA8 and Q5JIA9
the enzyme accommodates a broad range of acids that correspond to those generated in the oxidative metabolism of Ala, Val, Leu, Ile, Met, Phe, and Cys
-
-
?
ATP + 4-aminobutyrate + CoA
ADP + phosphate + 4-aminobutyryl-CoA
show the reaction diagram
Q5JIA8 and Q5JIA9
low activity. The enzyme accommodates a broad range of acids that correspond to those generated in the oxidative metabolism of Ala, Val, Leu, Ile, Met, Phe, and Cys
-
-
?
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
show the reaction diagram
ATP + butyrate + CoA
ADP + phosphate + butyryl-CoA
show the reaction diagram
ATP + fumarate + CoA
ADP + phosphate + fumaryl-CoA
show the reaction diagram
ATP + glycolate + CoA
ADP + phosphate + glycolyl-CoA
show the reaction diagram
Q5JIA8 and Q5JIA9
low activity. The enzyme accommodates a broad range of acids that correspond to those generated in the oxidative metabolism of Ala, Val, Leu, Ile, Met, Phe, and Cys
-
-
?
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 + indole-3-acetate + CoA
ADP + phosphate + phenylacetyl-CoA
show the reaction diagram
activity is 4% compared to activity with acetate
-
-
?
ATP + isobutyrate + CoA
ADP + phosphate + isobutyryl-CoA
show the reaction diagram
ATP + isovalerate + CoA
ADP + phosphate + isovaleryl-CoA
show the reaction diagram
ATP + lactate + CoA
ADP + phosphate + lactoyl-CoA
show the reaction diagram
Q5JIA8 and Q5JIA9
low activity. The enzyme accommodates a broad range of acids that correspond to those generated in the oxidative metabolism of Ala, Val, Leu, Ile, Met, Phe, and Cys
-
-
?
ATP + phenylacetate + CoA
ADP + phosphate + phenylacetyl-CoA
show the reaction diagram
ATP + propionate + CoA
ADP + phosphate + propionyl-CoA
show the reaction diagram
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
activity is 9% compared to activity with acetate
-
-
?
ATP + thioglycolate + CoA
ADP + phosphate + thioglycolyl-CoA
show the reaction diagram
Q5JIA8 and Q5JIA9
the enzyme accommodates a broad range of acids that correspond to those generated in the oxidative metabolism of Ala, Val, Leu, Ile, Met, Phe, and Cys
-
-
?
GTP + acetate + CoA
GDP + phosphate + acetyl-CoA
show the reaction diagram
GTP is as effective as ATP as a substrate
-
-
r
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%)
-
-
?
additional information
?
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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+
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+
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+
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+
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+
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+
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 - 2.58
acetate
0.01 - 0.037
acetyl-CoA
0.007 - 0.015
ADP
0.03 - 0.13
ATP
0.0056 - 0.53
CoA
1.24
indole-3-acetate
pH 8.0, 55°C
0.11 - 2.5
phenylacetate
0.017
phenylacetyl-CoA
pH 8.0, 55°C
0.11 - 0.47
phosphate
additional information
acetate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.84 - 138
acetate
95
acetyl-CoA
Archaeoglobus fulgidus
O28341, O29057
pH 8.0, 55°C
70
ADP
Archaeoglobus fulgidus
O28341, O29057
pH 8.0, 55°C
3 - 150
ATP
2.9 - 110
CoA
3.45
indole-3-acetate
Archaeoglobus fulgidus
O28341, O29057
pH 8.0, 55°C
3 - 11.5
phenylacetate
2.3
phenylacetyl-CoA
Archaeoglobus fulgidus
O28341, O29057
pH 8.0, 55°C
58
phosphate
Archaeoglobus fulgidus
O28341, O29057
pH 8.0, 55°C
additional information
acetate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.7 - 400
acetate
47
9200
acetyl-CoA
Archaeoglobus fulgidus
O28341, O29057
pH 8.0, 55°C
29
10000
ADP
Archaeoglobus fulgidus
O28341, O29057
pH 8.0, 55°C
13
100 - 1120
ATP
4
5.4 - 9490
CoA
18
2.7
indole-3-acetate
Archaeoglobus fulgidus
O28341, O29057
pH 8.0, 55°C
3639
1.2 - 111
phenylacetate
776
140
phenylacetyl-CoA
Archaeoglobus fulgidus
O28341, O29057
pH 8.0, 55°C
1147
520
phosphate
Archaeoglobus fulgidus
O28341, O29057
pH 8.0, 55°C
16
additional information
acetate
47
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
Q5JIA8 and Q5JIA9
assay at
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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7000
2 * 7000, SDS-PAGE
7400
2 * 7400, SDS-PAGE
27148
Q5JIA8 and Q5JIA9
2 * 51861 (TK0944) + 2 * 27148 (TK0943), calculated from sequence
51861
Q5JIA8 and Q5JIA9
2 * 51861 (TK0944) + 2 * 27148 (TK0943), calculated from sequence
72000
2 * 72000, SDS-PAGE
78172
2 * 78172, calculated from sequence
140000
gel filtration; gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
tetramer
Q5JIA8 and Q5JIA9
2 * 51861 (TK0944) + 2 * 27148 (TK0943), calculated from sequence
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
arrangement of the acyl-CoA synthetase subunits alpha and beta within an alpha2beta2-heterotetrameric complex significantly differs from other members of the superfamily. To transmit an activated phosphoryl moiety from the acetyl-CoA binding site (within the alpha subunit) to the NDP-binding site (within the beta subunit), a distance of 51 A has to be bridged. This transmission requires a larger rearrangement within the protein complex involving a 21-aa-long phosphohistidine-containing segment of the alpha subunit. Spatial restraints of the interaction of this segment with the beta subunit explain the necessity for a second highly conserved His residue within the beta subunit
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70
5 h, about 30% loss of activity
85
30 min, about 80% loss of activity. Almost complete loss of activity after 100 min
90
Q5JIA8 and Q5JIA9
half-life of the TK2127/TK0943 protein: 170 min
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme; recombinant enzyme
recombinant TK0944/TK0943 protein
Q5JIA8 and Q5JIA9
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
coexpression of TK0944 and TK0943 in Escherichia coli
Q5JIA8 and Q5JIA9
overexpressed in Escherichia coli
overexpressed in Escherichia coli; overexpressed in Escherichia coli