Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 4.1.1.9 - malonyl-CoA decarboxylase and Organism(s) Mus musculus and UniProt Accession Q99J39

for references in articles please use BRENDA:EC4.1.1.9
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.9 malonyl-CoA decarboxylase
IUBMB Comments
Specific for malonyl-CoA. The enzyme from Pseudomonas ovalis also catalyses the reaction of EC 2.8.3.3 malonate CoA-transferase.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Mus musculus
UNIPROT: Q99J39
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
hide
malonyl-CoA
=
acetyl-CoA
+
CO2
=
+
Synonyms
malonyl-coa decarboxylase, malonyl coa decarboxylase, mlycd, malonyl-coenzyme a decarboxylase, malonyl coenzyme a decarboxylase, malonyl-coa decarboxylase/acetyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malonyl CoA decarboxylase
-
Acyl-CoA: malonate CoA transferase/malonyl-CoA decarboxylase
-
-
-
-
Decarboxylase, malonyl coenzyme A
-
-
-
-
malonyl CoA decarboxylase
-
-
Malonyl coenzyme A decarboxylase
-
-
-
-
Malonyl-CoA decarboxylase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
malonyl-CoA carboxy-lyase (acetyl-CoA-forming)
Specific for malonyl-CoA. The enzyme from Pseudomonas ovalis also catalyses the reaction of EC 2.8.3.3 malonate CoA-transferase.
CAS REGISTRY NUMBER
COMMENTARY hide
9024-99-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Malonyl-CoA
Acetyl-CoA + CO2
show the reaction diagram
Malonyl-CoA
Acetyl-CoA + CO2
show the reaction diagram
additional information
?
-
-
MCD is an inhibitor of carnitine palmitoyl-CoA transferase-1
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Malonyl-CoA
Acetyl-CoA + CO2
show the reaction diagram
Malonyl-CoA
Acetyl-CoA + CO2
show the reaction diagram
-
malonyl-CoA degradation, transcriptional control of MCD by peroxisome proliferator-activated receptor alpha, involved in the regulation of fatty acid oxidation
-
?
additional information
?
-
-
MCD is an inhibitor of carnitine palmitoyl-CoA transferase-1
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CBM-3001106
-
methyl-5-(N-(4-(1,1,1,3,3,3-hexafluoro-2-hydroxypropan-2-yl) phenyl)morpholine-4-carboxamido)pentanoate
-
i.e. CBM-301106, specific inhibitor of the enzyme
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
neonatal
Manually annotated by BRENDA team
-
peritoneal
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
decreased fat oxidation in enzyme-deficient mice results in the accumulation of lipid intermediates in peripheral tissues, but this is not associated with a worsening of age-associated insulin resistance and, conversely, improves longevity. This improvement is associated with reduced oxidative stress and reduced acetylation of the antioxidant enzyme superoxide dismutase 2 in muscle but not the liver
physiological function
a two week induction of the enzyme in skeletal muscle does not alter body weight or ameliorate glucose intolerance, conversely it further impairs insulin signaling in the skeletal muscle of diet-induced obese mice. Furthermore, an acute induction of the enzyme leads to a suppression of fatty acid oxidative genes suggesting a redundant and metabolite driven regulation of gene expression
malfunction
-
pharmacological inhibition of malonyl-CoA decarboxylase reduces the inflammatory response associated with insulin resistance. Additionally, inhibition of MCD strongly diminishes lipopolysaccharide-induced activation of palmitate oxidation and prevents lipopolysaccharide-induced collapse of total cellular antioxidant capacity and prevents increases in the level of ceramide in cardiomyocytes and macrophages while also ameliorating LPS-initiated decreases in PPAR binding. Genetic inactivation of malonyl-CoA decarboxylase protects mice against high-fat diet-induced insulin resistance
physiological function
-
malonyl-CoA decarboxylase regulates fatty acid oxidation
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DCMC_MOUSE
492
0
54736
Swiss-Prot
Mitochondrion (Reliability: 2)
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
MCD is involved in regulating cardiac malonyl-CoA levels, inhibition of MCD can limit rates of fatty acid oxidation, leading to a secondary increase in glucose oxidation associated with an improvement in the functional recovery of the heart during ischaemia/reperfusion injury
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Campbell, F.M.; Kozak, R.; Wagner, A.; Altarejos, J.Y.; Dyck, J.R.B.; Belke, D.D.; Severson, D.L.; Kelly, D.P.; Lopaschuk, G.D.
A role for peroxisome proliferator-activated receptor alpha (PPARalpha) in the control of cardiac malonyl-CoA levels. Reduced fatty acid oxidation rates and increased glucose oxidation rates in the hearts of mice lacking PPARalpha are associated with higher concentrations of malonyl-CoA and reduced expression of malonyl-CoA decarboxylase
J. Biol. Chem.
277
4098-4103
2002
Mus musculus
Manually annotated by BRENDA team
Ussher, J.R.; Lopaschuk, G.D.
The malonyl CoA axis as a potential target for treating ischaemic heart disease
Cardiovasc. Res.
79
259-268
2008
Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Koves, T.R.; Ussher, J.R.; Noland, R.C.; Slentz, D.; Mosedale, M.; Ilkayeva, O.; Bain, J.; Stevens, R.; Dyck, J.R.; Newgard, C.B.; Lopaschuk, G.D.; Muoio, D.M.
Mitochondrial overload and incomplete fatty acid oxidation contribute to skeletal muscle insulin resistance
Cell Metab.
7
45-56
2008
Mus musculus
Manually annotated by BRENDA team
Lane, M.D.; Wolfgang, M.; Cha, S.; Dai, Y.
Regulation of food intake and energy expenditure by hypothalamic malonyl-CoA
Int. J. Obes.
32
S49-S54
2008
Mus musculus
-
Manually annotated by BRENDA team
Samokhvalov, V.; Ussher, J.R.; Fillmore, N.; Armstrong, I.K.; Keung, W.; Moroz, D.; Lopaschuk, D.G.; Seubert, J.; Lopaschuk, G.D.
Inhibition of malonyl-CoA decarboxylase reduces the inflammatory response associated with insulin resistance
Am. J. Physiol. Endocrinol. Metab.
303
E1459-E1468
2012
Mus musculus
Manually annotated by BRENDA team
Rodriguez, S.; Ellis, J.M.; Wolfgang, M.J.
Chemical-genetic induction of malonyl-CoA decarboxylase in skeletal muscle
BMC Biochem.
15
20
2014
Mus musculus (Q99J39), Mus musculus
Manually annotated by BRENDA team
Ussher, J.R.; Fillmore, N.; Keung, W.; Zhang, L.; Mori, J.; Sidhu, V.K.; Fukushima, A.; Gopal, K.; Lopaschuk, D.G.; Wagg, C.S.; Jaswal, J.S.; Dyck, J.R.; Lopaschuk, G.D.
Genetic and pharmacological inhibition of malonyl CoA decarboxylase does not exacerbate age-related insulin resistance in mice
Diabetes
65
1883-1891
2016
Mus musculus (Q99J39), Mus musculus
Manually annotated by BRENDA team