Information on EC 3.1.2.19 - ADP-dependent medium-chain-acyl-CoA hydrolase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.1.2.19
-
RECOMMENDED NAME
GeneOntology No.
ADP-dependent medium-chain-acyl-CoA hydrolase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
acyl-CoA + H2O = CoA + a carboxylate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of thioester
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ADP-dependent-medium-chain-acyl-CoA hydrolase
Requires ADP; inhibited by NADH. Maximum activity is shown with nonanoyl-CoA.
CAS REGISTRY NUMBER
COMMENTARY hide
63363-75-7
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Syrian hamster, adult female, acclimated to cold
-
-
Manually annotated by BRENDA team
adult female Sprague-Dawley rats
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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
acyl-CoA + H2O
CoA + a carboxylate
show the reaction diagram
-
-
-
?
malonyl-CoA + H2O
malonate + CoA
show the reaction diagram
-
very poor substrate
-
-
?
nonanoyl-CoA + H2O
CoA + nonanoate
show the reaction diagram
octanoyl-CoA + H2O
CoA + octanoate
show the reaction diagram
-
-
-
?
additional information
?
-
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
acyl-CoA + H2O
CoA + a carboxylate
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ADP
-
requirement
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ba2+
-
activation
Ca2+
-
activation
K+
-
activation, 0.2 M
Li+
-
activation
Mg2+
-
activation
additional information
-
no activation by Na+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
AMP
-
inhibitory at high concentration
ATP
-
inhibitory at high concentration
beta-NADH
additional information
-
no inhibition by alpha-NADH, NADPH, NAD+, EDTA or EGTA
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.013
ADP
-
pH 7.4, 25°C
0.3
Ca2+
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pH 7.4, 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.11
-
mitochondria
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
-
not in liver tissue
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
-
about, gel filtration
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
t1/2: 1 min, in buffer with Triton X-100 but without substrates, decrease of activity in intact mitochondria, ADP stabilizes: t1/2: 1 h, substrates protect
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
ADP stabilizes
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE