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Enzyme Nomenclature
Information on EC 4.1.1.94 - ethylmalonyl-CoA decarboxylase
for references in articles please use BRENDA:EC4.1.1.94
Word Map on EC 4.1.1.94
- 4.1.1.94
- crotonyl-coa
-
aciduria
-
polyhydroxyalkanoates
-
intermediary
- butyryl-coa
- acetyl-coa
-
poly3-hydroxybutyrate-co-3-hydroxyhexanoate
-
hydratase
-
proofreading
- breast
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
4.1.1.94
-
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RECOMMENDED NAME
GeneOntology No.
ethylmalonyl-CoA decarboxylase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(S)-ethylmalonyl-CoA = butanoyl-CoA + CO2
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-
-
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SYSTEMATIC NAME
IUBMB Comments
(S)-ethylmalonyl-CoA carboxy-lyase (butanoyl-CoA-forming)
The enzyme, which exists in all vertebrates, decarboxylates ethylmalonyl-CoA, a potentially toxic compound that is formed in low amounts by the activity of EC 6.4.1.2 (acetyl-CoA carboxylase) and EC 6.4.1.3 (propanoyl-CoA carboxylase). It prefers the S isomer, and can decarboxylate (R)-methylmalonyl-CoA with lower efficiency. cf. EC 4.1.1.41 (methylmalonyl-CoA decarboxylase).
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
enzyme mutation may be involved in the development of certain forms of ethylmalonic aciduria
metabolism
-
ethylmalonyl-CoA decarboxylase may correct a side activity of acetyl-CoA carboxylase
physiological function
-
ethylmalonyl-CoA decarboxylase may correct a side activity of acetyl-CoA carboxylase
additional information
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ECHDC1-specific siRNAs decrease the ethylmalonyl-CoA decarboxylase activity in human cells and increase the formation of ethylmalonate, most particularly in cells incubated with butyrate
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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
(S)-ethylmalonyl-CoA
butanoyl-CoA + CO2
-
best substrate, it is likely that the enzyme catalyzes preferentially the decarboxylation of one of the two isomers
-
-
?
(S)-ethylmalonyl-CoA
butanoyl-CoA + CO2
-
best substrate, it is likely that the enzyme catalyzes preferentially the decarboxylation of one of the two isomers. Recombinant ethylmalonyl-CoA decarboxylase acts preferentially on (S)-ethylmalonyl-CoA
-
-
?
(S)-ethylmalonyl-CoA
butanoyl-CoA + CO2
-
best substrate, it is likely that the enzyme catalyzes preferentially the decarboxylation of one of the two isomers
-
-
?
additional information
?
-
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the enzyme shows no malonyl-CoA decarboxylase or enoyl-CoA hydratase activity
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-
-
additional information
?
-
-
the enzyme shows no malonyl-CoA decarboxylase or enoyl-CoA hydratase activity
-
-
-
additional information
?
-
-
the enzyme shows no malonyl-CoA decarboxylase or enoyl-CoA hydratase activity
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-
-
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
ECHDC1-specific siRNAs decrease the ethylmalonyl-CoA decarboxylase activity in human cells and increase the formation of ethylmalonate, most particularly in cells incubated with butyrate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00096
(S)-ethylmalonyl-CoA
-
pH 7.1, 30°C, recombinant enzyme in absence of ATP-Mg2-
0.0065
(S)-ethylmalonyl-CoA
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pH 7.1, 30°C, recombinant enzyme in presence of 5 mM ATP-Mg2-
0.0031
methylmalonyl-CoA
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pH 7.1, 30°C, recombinant enzyme in absence of ATP-Mg2-
0.0151
methylmalonyl-CoA
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pH 7.1, 30°C, recombinant enzyme in presence of 5 mM ATP-Mg2-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
9.5
(S)-ethylmalonyl-CoA
-
pH 7.1, 30°C, recombinant enzyme in absence of ATP-Mg2-
10
(S)-ethylmalonyl-CoA
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pH 7.1, 30°C, recombinant enzyme in presence of 5 mM ATP-Mg2-
1.61
methylmalonyl-CoA
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pH 7.1, 30°C, recombinant enzyme in absence of ATP-Mg2-
1.81
methylmalonyl-CoA
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pH 7.1, 30°C, recombinant enzyme in presence of 5 mM ATP-Mg2-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1500
(S)-ethylmalonyl-CoA
-
pH 7.1, 30°C, recombinant enzyme in presence of 5 mM ATP-Mg2-
9900
(S)-ethylmalonyl-CoA
-
pH 7.1, 30°C, recombinant enzyme in absence of ATP-Mg2-
110
methylmalonyl-CoA
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pH 7.1, 30°C, recombinant enzyme in presence of 5 mM ATP-Mg2-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.1
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
expression of siRNA in HEK-293T cells suppresses the enzyme with an about 3fold decrease in ECHDC1 mRNA levels
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LINKS TO OTHER DATABASES (specific for EC-Number 4.1.1.94)
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