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Information on EC 4.1.1.94 - ethylmalonyl-CoA decarboxylase and Organism(s) Mus musculus and UniProt Accession Q9D9V3

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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.94 ethylmalonyl-CoA decarboxylase
IUBMB Comments
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)-ethylmalonyl-CoA with lower efficiency. cf. EC 7.2.4.1, (S)-methylmalonyl-CoA decarboxylase (sodium-transporting).
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This record set is specific for:
Mus musculus
UNIPROT: Q9D9V3
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The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
Synonyms
echdc1, ethylmalonyl-coa decarboxylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ECHDC1
-
-
ethylmalonyl-CoA decarboxylase
-
-
PATHWAY SOURCE
PATHWAYS
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)-ethylmalonyl-CoA with lower efficiency. cf. EC 7.2.4.1, (S)-methylmalonyl-CoA decarboxylase (sodium-transporting).
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(S)-ethylmalonyl-CoA
butanoyl-CoA + CO2
show the reaction diagram
-
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
-
-
?
methylmalonyl-CoA
propanoyl-CoA + CO2
show the reaction diagram
-
lower activity
-
-
?
additional information
?
-
-
the enzyme shows no malonyl-CoA decarboxylase or enoyl-CoA hydratase activity
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
MgATP2-
-
inhibits the enzyme slightly
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00096 - 0.0065
(S)-ethylmalonyl-CoA
0.0031 - 0.0151
methylmalonyl-CoA
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
9.5 - 10
(S)-ethylmalonyl-CoA
1.61 - 1.81
methylmalonyl-CoA
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1500 - 9900
(S)-ethylmalonyl-CoA
110 - 510
methylmalonyl-CoA
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8800
-
purified recombinant ECHDC1, pH 7.1, 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.1
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ECHD1_MOUSE
322
0
35467
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
34000
-
x * 34000, recombinant ECHDC1, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 34000, recombinant ECHDC1, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
improved artificial pathway for the biosynthesis of poly((R)-3-hydroxybutyrate-co-(R)-3-hydroxyhexanoate) with high 3-hydroxyhexanoate composition from fructose in Ralstonia eutropha. Introduction of EchDC1, encoding codon-optimized ethylmalonyl-CoA decarboxylase increases poly((R)-3-hydroxybutyrate-co-(R)-3-hydroxyhexanoate) biosynthesis, probably by converting ethylmalonyl-CoA generated by the reductive carboxylase activity of crotonyl-CoA carboxylase/reductase back into butyryl-CoA
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme by metal affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
ECHDC1 from mouse brain cDNA, expression as N-terminally His-tagged enzyme
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Linster, C.L.; Noel, G.; Stroobant, V.; Vertommen, D.; Vincent, M.F.; Bommer, G.T.; Veiga-da-Cunha, M.; Van Schaftingen, E.
Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite proofreading
J. Biol. Chem.
286
42992-43003
2011
Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Insomphun, C.; Xie, H.; Mifune, J.; Kawashima, Y.; Orita, I.; Nakamura, S.; Fukui, T.
Improved artificial pathway for biosynthesis of poly(3-hydroxybutyrate-co-3-hydroxyhexanoate) with high C6-monomer composition from fructose in Ralstonia eutropha
Metab. Eng.
27
38-45
2015
Mus musculus (Q9D9V3), Mus musculus
Manually annotated by BRENDA team