Information on EC 6.2.1.23 - dicarboxylate-CoA ligase

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The expected taxonomic range for this enzyme is: Rattus norvegicus

EC NUMBER
COMMENTARY hide
6.2.1.23
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RECOMMENDED NAME
GeneOntology No.
dicarboxylate-CoA ligase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + an alpha,omega-dicarboxylate + CoA = AMP + diphosphate + an omega-carboxyacyl-CoA
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acid-thiol ligation
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SYSTEMATIC NAME
IUBMB Comments
omega-dicarboxylate:CoA ligase (AMP-forming)
Acts on dicarboxylic acids of chain length C5 to C16; the best substrate is dodecanedioic acid.
CAS REGISTRY NUMBER
COMMENTARY hide
99332-77-1
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + decanedioic acid + CoA
AMP + diphosphate + decanedioyl-CoA
show the reaction diagram
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ATP + dodec-2-enedioic acid + CoA
AMP + diphosphate + dodec-2-enedioyl-CoA
show the reaction diagram
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i.e. traumatic acid, at 40% of the activity relative to dodecanedioic acid
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ATP + dodecanedioic acid + CoA
AMP + diphosphate + dodecanedioyl-CoA
show the reaction diagram
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highest activity with dodecandioic acid , ATP cannot be replaced by GTP
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ATP + heptanedioic acid + CoA
AMP + diphosphate + heptanedioyl-CoA
show the reaction diagram
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ATP + hexadecanedioic acid + CoA
AMP + diphosphate + hexadecanedioyl-CoA
show the reaction diagram
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ATP + hexanedioic acid + CoA
AMP + diphosphate + hexanedioyl-CoA
show the reaction diagram
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ATP + octanedioic acid + CoA
AMP + diphosphate + octanedioyl-CoA
show the reaction diagram
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ATP + pentanedioic acid + CoA
AMP + diphosphate + pentanedioyl-CoA
show the reaction diagram
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ATP + tetradecanedioic acid + CoA
AMP + diphosphate + tetradecanedioyl-CoA
show the reaction diagram
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additional information
?
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the dicarboxylyl-CoA synthetase appears to catalyze an essential step in the degradation of dicarboxylic acids
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
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the dicarboxylyl-CoA synthetase appears to catalyze an essential step in the degradation of dicarboxylic acids
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
AMP
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product inhibition
diphosphate
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product inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.55
ATP
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2.5
dodecanedioic acid
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
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dodecanedioic acid
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4 - 8.5
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pH 7.4: 40% of maximal activity, pH 8.5: 70% of maximal activity with dodecanedioic acid
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
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no activity detected in kidney, jejunum, heart, lung, skeletal muscle, smooth muscle, cerebrum, brain stem
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
freezing and thawing of liver homogenates strongly diminishes its activity within several h
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preincubation of fresh liver homogenate in the absence of substrate and cofactors leads to a loss of 75% of its activity within 30 min
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