6.2.1.B11: carboxylic acid-CoA ligase (NDP-forming)
This is an abbreviated version!
For detailed information about carboxylic acid-CoA ligase (NDP-forming), go to the full flat file.
Word Map on EC 6.2.1.B11
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6.2.1.B11
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archaeon
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pyrococcus
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hyperthermophilic
-
acetyl-coa
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furiosus
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acetyl-coenzyme
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heterotetramer
- 6.2.1.B11
- archaeon
- pyrococcus
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hyperthermophilic
- acetyl-coa
- furiosus
-
acetyl-coenzyme
- heterotetramer
Reaction
Synonyms
ACD, acetyl CoA synthetase (ADP forming), acetyl coenzyme A synthetase (ADP forming), Acetyl-CoA synthetase (ADP-forming), ACSIIITk, acyl-CoA synthetase (NDP forming), ADP-forming acetyl coenzyme A synthetase, AF1211, AF1938, ckcACD1, EhACD, Kcr_0198, MJ0590, More, NDP-forming acyl-CoA synthetase, TK0944/TK0943 protein
ECTree
6.2.1.B11 carboxylic acid-CoA ligase (NDP-forming)Advanced search results
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results (Substrates Products
Substrates Products on EC 6.2.1.B11 - carboxylic acid-CoA ligase (NDP-forming)
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ADP + phosphate + indole-3-acetyl-CoA
ATP + indole-3-acetate + CoA
-
-
-
r
ADP + phosphate + phenylacetyl-CoA
ATP + phenylacetate + CoA
-
-
-
r
ATP + 2-(4-hydroxyphenyl)acetate + CoA
ADP + phosphate + 2-(4-hydroxyphenyl)acetyl-CoA
Q5JIA8; 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
Q5JIA8; 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
Q5JIA8; 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
Q5JIA8; 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
Q5JIA8; 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 + glycolate + CoA
ADP + phosphate + glycolyl-CoA
Q5JIA8; 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 + lactate + CoA
ADP + phosphate + lactoyl-CoA
Q5JIA8; 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 + succinate + CoA
ADP + phosphate + succinyl-CoA
activity is 9% compared to activity with acetate
-
-
?
ATP + thioglycolate + CoA
ADP + phosphate + thioglycolyl-CoA
Q5JIA8; 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 + indole-3-acetate + CoA
GDP + phosphate + indole-3-acetyl-CoA
ATP (100%) is effectively replaced by GTP (70%)
-
-
?
GTP + phenylacetate + CoA
GDP + phosphate + phenylacetyl-CoA
ATP (100%) is effectively replaced by GTP (70%)
-
-
?
ITP + acetate + CoA
IDP + phosphate + acetyl-CoA
ITP gives 15% of the activity with ATP
-
-
r
ADP + phosphate + acetyl-CoA
ATP + acetate + 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
-
-
ir
ADP + phosphate + acetyl-CoA
ATP + acetate + 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
-
-
ir
ADP + phosphate + butyryl-CoA
ATP + butyrate + CoA
the enzyme is specific for acetyl-CoA (100%) and butyryl-CoA (120%) but does not take phenylacetyl-CoA (0%)
-
-
?
ADP + phosphate + butyryl-CoA
ATP + butyrate + CoA
the enzyme is specific for acetyl-CoA (100%) and butyryl-CoA (120%) but does not take phenylacetyl-CoA (0%)
-
-
?
ATP + acetate + CoA
ADP + phosphate + acetyl-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
-
-
?
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
GTP is as effective as ATP as a substrate
-
-
r
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
-
-
-
r
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
Q5JIA8; 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 + butyrate + CoA
ADP + phosphate + butyryl-CoA
activity is 36% compared to activity with phenylacetate
-
-
?
ATP + butyrate + CoA
ADP + phosphate + butyryl-CoA
activity is 84% compared to activity with acetate
-
-
r
ATP + fumarate + CoA
ADP + phosphate + fumaryl-CoA
activity is 10% compared to activity with acetate
-
-
?
ATP + fumarate + CoA
ADP + phosphate + fumaryl-CoA
activity is 29% compared to activity with phenylacetate
-
-
?
ATP + indole-3-acetate + CoA
ADP + phosphate + indole-3-acetyl-CoA
activity is 4% compared to activity with acetate
-
-
?
ATP + indole-3-acetate + CoA
ADP + phosphate + indole-3-acetyl-CoA
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
activity is 31% compared to activity with phenylacetate
-
-
?
ATP + isobutyrate + CoA
ADP + phosphate + isobutyryl-CoA
activity is 56% compared to activity with acetate
-
-
?
ATP + isobutyrate + CoA
ADP + phosphate + isobutyryl-CoA
Q5JIA8; 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 + isovalerate + CoA
ADP + phosphate + isovaleryl-CoA
activity is 10% compared to activity with acetate
-
-
?
ATP + isovalerate + CoA
ADP + phosphate + isovaleryl-CoA
activity is 18% compared to activity with phenylacetate
-
-
?
ATP + isovalerate + CoA
ADP + phosphate + isovaleryl-CoA
Q5JIA8; 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 + phenylacetate + CoA
ADP + phosphate + phenylacetyl-CoA
activity is 10% compared to activity with acetate
-
-
?
ATP + phenylacetate + CoA
ADP + phosphate + phenylacetyl-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%)
-
-
r
ATP + phenylacetate + CoA
ADP + phosphate + phenylacetyl-CoA
Q5JIA8; 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 + propionate + CoA
ADP + phosphate + propionyl-CoA
activity is 42% compared to activity with phenylacetate
-
-
?
ATP + propionate + CoA
ADP + phosphate + propionyl-CoA
propionate is as effective as acetate as substrate
-
-
r
GTP + acetate + CoA
GDP + phosphate + acetyl-CoA
GTP is as effective as ATP as a substrate
-
-
r
GTP + acetate + CoA
GDP + phosphate + acetyl-CoA
GTP gives 57% of the activity with ATP
-
-
r
additional information
?
-
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, binding mode of the Ac moiety within acetyl-CoA, and binding mode of Ado nucleotides within site II located in the beta subunit
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
Q5JIA8; Q5JIA9
activity with 2-(imidazol-4-yl)acetate is less than 5% of the activity with acetate
-
-
?
additional information
?
-
-
activity with 2-(imidazol-4-yl)acetate is less than 5% of the activity with acetate
-
-
?
