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Enzyme Nomenclature
Information on EC 4.1.1.41 - (S)-methylmalonyl-CoA decarboxylase
for references in articles please use BRENDA:EC4.1.1.41
Word Map on EC 4.1.1.41
- 4.1.1.41
- propionyl-coa
- veillonella
- parvula
- modestum
- propionigenium
-
biotin-containing
- alcalescens
- carboxyltransferase
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avidin-sepharose
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
4.1.1.41
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RECOMMENDED NAME
GeneOntology No.
(S)-methylmalonyl-CoA decarboxylase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(S)-methylmalonyl-CoA = propanoyl-CoA + CO2
(S)-2-methyl-3-oxopropanoyl-CoA = propanoyl-CoA + CO2
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
(S)-methylmalonyl-CoA carboxy-lyase (propanoyl-CoA-forming)
The enzyme from Veillonella alcalescens is a biotinyl-protein, requires Na+ and acts as a sodium pump.
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CAS REGISTRY NUMBER
COMMENTARY
37289-44-4
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
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genes involved in precursor biosyntheses for avermectin or other antibiotics, such as methylmalonyl-CoA decarboxylase, are upregulated by 2.4fold in aveI mutant at day 10, which may potentially lead to increased supply of precursors into the antibiotics
physiological function
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the propionyl-CoA carboxylase pathway does not increase the production of FK506, a polyketide macrolide with immunosuppressant activity, in Streptomyces clavuligerus CKD1119
physiological function
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14-year-old Asian-American male with propionic acidaemia shows propionyl-CoA carboxylase deficiency with mutations in PCCB: IVS7+2 T-G (c.763+2 T-G) and p.R410Q (c.1229 G-A), and residual enzyme activity which likely explains the patient's mild phenotype with isolated cardiomyopathy without any documented episodes of metabolic acidosis or evidence of any neurocognitive deficits
physiological function
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propionic acidemia, a rare autosomal recessive disorder, is caused by deficiency in propionyl-CoA carboxylase, and is categorized into two forms: an early (neonatal) onset form, in which clinical symptoms are presented within the first 90 days of life, and a late onset form. Deficiency in propionyl-CoA carboxylase leads to accumulation of toxic substances in the body, that results in severe metabolic decompensation
physiological function
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the propionyl-CoA carboxylase pathway does not increase the production of FK506, a polyketide macrolide with immunosuppressant activity, in Streptomyces clavuligerus CKD1119
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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
additional information
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Na+-independent carboxyltransferase activity: catalyzes the isotopic exchange between methylmalonyl-CoA and [1-14C]propionyl-CoA or between malonyl-CoA and [1-14C]acetyl-CoA, catalyzes the carboxyl transfer reaction from methylmalonyl-CoA to acetyl-CoA yielding propionyl-CoA and malonyl-CoA and vice versa
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(S)-methylmalonyl-CoA
?
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the enzyme catalyzes the only energy-conserving step during succinate fermentation. The decarboxylation of (S)-methylmalonyl-CoA is coupled to the vectorial transport of Na+ across the cytoplasmic membrane, thereby creating a sodium ion motive force that is used for ATP synthesis
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(S)-methylmalonyl-CoA
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the Na+-transport enzyme converts the chemical energy of a decarboxylation reaction into an ion gradient
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(S)-methylmalonyl-CoA
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the enzyme is responsible for the formation of the propionate moiety in the fermentation of lactate and the decarboxylation of succinate
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(S)-methylmalonyl-CoA
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the enzyme is one of the sodium pumps, which are driven by decarboxylation energy
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(S)-methylmalonyl-CoA
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the enzyme is a sodium-transport decarboxylase
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(S)-methylmalonyl-CoA
?
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proteoliposomes are reconstituted with the Na+-pump methylmalonyl-CoA decarboxylase from Veillonella alcalescens
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(S)-methylmalonyl-CoA
propanoyl-CoA + CO2
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(S)-methylmalonyl-CoA
propanoyl-CoA + CO2
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retention of the configuration during the decarboxylation reaction
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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)-methylmalonyl-CoA
?
-
the enzyme catalyzes the only energy-conserving step during succinate fermentation. The decarboxylation of (S)-methylmalonyl-CoA is coupled to the vectorial transport of Na+ across the cytoplasmic membrane, thereby creating a sodium ion motive force that is used for ATP synthesis
-
-
-
(S)-methylmalonyl-CoA
?
-
the Na+-transport enzyme converts the chemical energy of a decarboxylation reaction into an ion gradient
-
-
-
(S)-methylmalonyl-CoA
?
-
the enzyme is responsible for the formation of the propionate moiety in the fermentation of lactate and the decarboxylation of succinate
-
-
-
(S)-methylmalonyl-CoA
?
-
the enzyme is one of the sodium pumps, which are driven by decarboxylation energy
-
-
-
(S)-methylmalonyl-CoA
?
-
the enzyme is a sodium-transport decarboxylase
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-
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(S)-methylmalonyl-CoA
?
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proteoliposomes are reconstituted with the Na+-pump methylmalonyl-CoA decarboxylase from Veillonella alcalescens
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
biotin
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1 mol covalently bound biotin per 125500 g protein, localized exclusivly in the gamma subunit
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Na+
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
13100
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x * 56100, alpha, carboxyltransferase, + x * 41200, beta, carboxybiotin-carrier-protein decarboxylase, + x * 13100, gamma, biotin carrier protein, + x * 14200, delta, essential for the assembly of the complex, calculation of the MW from nucleotide sequence
14000
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x * 60000, alpha, + x * 33000, beta, + x * 18500, gamma, + x * 14000, delta, SDS-PAGE
14200
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x * 56100, alpha, carboxyltransferase, + x * 41200, beta, carboxybiotin-carrier-protein decarboxylase, + x * 13100, gamma, biotin carrier protein, + x * 14200, delta, essential for the assembly of the complex, calculation of the MW from nucleotide sequence
18500
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x * 60000, alpha, + x * 33000, beta, + x * 18500, gamma, + x * 14000, delta, SDS-PAGE
33000
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x * 60000, alpha, + x * 33000, beta, + x * 18500, gamma, + x * 14000, delta, SDS-PAGE
41200
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x * 56100, alpha, carboxyltransferase, + x * 41200, beta, carboxybiotin-carrier-protein decarboxylase, + x * 13100, gamma, biotin carrier protein, + x * 14200, delta, essential for the assembly of the complex, calculation of the MW from nucleotide sequence
56100
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x * 56100, alpha, carboxyltransferase, + x * 41200, beta, carboxybiotin-carrier-protein decarboxylase, + x * 13100, gamma, biotin carrier protein, + x * 14200, delta, essential for the assembly of the complex, calculation of the MW from nucleotide sequence
60000
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x * 60000, alpha, + x * 33000, beta, + x * 18500, gamma, + x * 14000, delta, SDS-PAGE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
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x * 56000 + x * 35000 + x * 17500 + x * 17000, SDS-PAGE; x * 56100, alpha, carboxyltransferase, + x * 41200, beta, carboxybiotin-carrier-protein decarboxylase, + x * 13100, gamma, biotin carrier protein, + x * 14200, delta, essential for the assembly of the complex, calculation of the MW from nucleotide sequence
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x * 60000, alpha, + x * 33000, beta, + x * 18500, gamma, + x * 14000, delta, SDS-PAGE
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the following functions are assigned to the different polypeptide chains: alpha /carboxyltransferase, beta /carboxybiotin-carrier-protein decarboxylase, gamma /biotin carrier protein
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
unliganded form and in complex with an inert thioether analogue of methylmalonyl-CoA
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
highest expression levels of PCCalpha in adult central nervous system in neocortex and hippocampal formation, thalamic and hypothalamic nuclei, midbrain nuclei such as the red nucleus and substantia nigra, as well as pons, medulla and the Purkinje and granular layers of cerebellum. PCCalpha is expressed in neurons of basal ganglia. High expression levels of PCCalpha in the whole embryonic central nervous system, both at E15.5 and E18.5, with the highest expression in the periventricular zones of telencephalon, midbrain and rhombencephalon. Choroid plexus also expresses high levels. Expression in embryonic liver increases towards E18.5. Outside the central nervous system, brown adipose tissue shows a very high expression level
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