Information on EC 4.1.1.41 - Methylmalonyl-CoA decarboxylase

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The expected taxonomic range for this enzyme is: Bacteria

EC NUMBER
COMMENTARY
4.1.1.41
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RECOMMENDED NAME
GeneOntology No.
Methylmalonyl-CoA decarboxylase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
(S)-methylmalonyl-CoA = propanoyl-CoA + CO2
show the reaction diagram
(S)-2-methyl-3-oxopropanoyl-CoA = propanoyl-CoA + CO2
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REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
decarboxylation
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-
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PATHWAY
KEGG Link
MetaCyc Link
conversion of succinate to propionate
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Propanoate metabolism
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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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Decarboxylase, methylmalonyl coenzyme A
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Methylmalonyl-CoA decarboxylase
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Methylmalonyl-CoA decarboxylase
Streptomyces avermitilis NRRL8165
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Methylmalonyl-coenzyme A decarboxylase
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Propionyl coenzyme A carboxylase
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Propionyl-CoA carboxylase
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Sodium pump methylmalonyl-CoA decarboxylase
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CAS REGISTRY NUMBER
COMMENTARY
37289-44-4
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ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Streptomyces avermitilis NRRL8165
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
Streptomyces avermitilis NRRL8165
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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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(S)-methylmalonyl-CoA
propanoyl-CoA + CO2
show the reaction diagram
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-
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(S)-methylmalonyl-CoA
propanoyl-CoA + CO2
show the reaction diagram
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(S)-methylmalonyl-CoA
propanoyl-CoA + CO2
show the reaction diagram
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-
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(S)-methylmalonyl-CoA
propanoyl-CoA + CO2
show the reaction diagram
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irreversible
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(S)-methylmalonyl-CoA
propanoyl-CoA + CO2
show the reaction diagram
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retention of the configuration during the decarboxylation reaction
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(S)-methylmalonyl-CoA
?
show the reaction diagram
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enzyme of the succinate pathway
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(S)-methylmalonyl-CoA
?
show the reaction diagram
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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
?
show the reaction diagram
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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
?
show the reaction diagram
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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
?
show the reaction diagram
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the enzyme is one of the sodium pumps, which are driven by decarboxylation energy, reconstitution of the sodium pump
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(S)-methylmalonyl-CoA
?
show the reaction diagram
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reconstitution of the sodium pump
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(S)-methylmalonyl-CoA
?
show the reaction diagram
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the enzyme is a sodium-transport decarboxylase
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(S)-methylmalonyl-CoA
?
show the reaction diagram
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proteoliposomes are reconstituted with the Na+-pump methylmalonyl-CoA decarboxylase from Veillonella alcalescens
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Malonyl-CoA
Acetyl-CoA + CO2
show the reaction diagram
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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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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(S)-methylmalonyl-CoA
?
show the reaction diagram
-
enzyme of the succinate pathway
-
-
-
(S)-methylmalonyl-CoA
?
show the reaction diagram
-
the Na+-transport enzyme converts the chemical energy of a decarboxylation reaction into an ion gradient
-
-
-
(S)-methylmalonyl-CoA
?
show the reaction diagram
-
the enzyme is responsible for the formation of the propionate moiety in the fermentation of lactate and the decarboxylation of succinate
-
-
-
(S)-methylmalonyl-CoA
?
show the reaction diagram
-
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
?
show the reaction diagram
-
the enzyme is one of the sodium pumps, which are driven by decarboxylation energy, reconstitution of the sodium pump
-
-
-
(S)-methylmalonyl-CoA
?
show the reaction diagram
-
reconstitution of the sodium pump
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(S)-methylmalonyl-CoA
?
show the reaction diagram
-
the enzyme is a sodium-transport decarboxylase
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-
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(S)-methylmalonyl-CoA
?
show the reaction diagram
-
proteoliposomes are reconstituted with the Na+-pump methylmalonyl-CoA decarboxylase from Veillonella alcalescens
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COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
biotin
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is contained in the gamma subunit
biotin
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1 mol covalently bound biotin per 125500 g protein, localized exclusivly in the gamma subunit
biotin
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prosthetic group
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Na+
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activates
Na+
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activates; Km: 1 mM at 0.1 mM (R,S)-methylmalonyl-CoA
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(S)-methylmalonyl-CoA
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substrate inhibition above 0.014 mM
glutaryl-CoA
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succinyl-CoA
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KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.002
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(S)-methylmalonyl-CoA
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0.007
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(S)-methylmalonyl-CoA
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at 20 mM NaCl
0.012
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(S)-methylmalonyl-CoA
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0.035
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malonyl-CoA
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at 20 mM NaCl
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
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additional information
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pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
Escherichia coli (strain K12)
Escherichia coli (strain K12)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
275000
300000
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sucrose density gradient centrifugation
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
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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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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
hexamer
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dimer of trimers, crystallographic data
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
unliganded form and in complex with an inert thioether analogue of methylmalonyl-CoA
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Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
PCCalpha is expressed at very low levels in the E15.5 embryonic liver
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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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