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Information on EC 7.2.4.3 - (S)-methylmalonyl-CoA decarboxylase (sodium-transporting)
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EC Tree
7.2.4.3 (S)-methylmalonyl-CoA decarboxylase (sodium-transporting)IUBMB Comments
This bacterial enzyme couples the decarboxylation of (S)-methylmalonyl-CoA to propanoyl-CoA to the vectorial transport of Na+ across the cytoplasmic membrane, thereby creating a sodium ion motive force that is used for ATP synthesis. It is a membrane-associated biotin protein and is strictly dependent on sodium ions for activity.
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Word Map
- 7.2.4.3
- propionyl-coa
- veillonella
- parvula
- modestum
- propionigenium
- alcalescens
-
biotin-containing
-
extratemporal
- carboxyltransferase
-
avidin-sepharose
The enzyme appears in viruses and cellular organisms
Synonyms
methylmalonyl-coa decarboxylase, propionyl coenzyme a carboxylase, sodium pump methylmalonyl-coa decarboxylase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Decarboxylase, methylmalonyl coenzyme A
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-
-
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EC 4.1.1.41
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-
formerly
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Methylmalonyl-CoA decarboxylase
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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Methylmalonyl-CoA decarboxylase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(S)-methylmalonyl-CoA + Na+[side 1] + H+[side 2] = propanoyl-CoA + CO2 + Na+[side 2]
(S)-2-methyl-3-oxopropanoyl-CoA = propanoyl-CoA + CO2
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
(S)-methylmalonyl-CoA carboxy-lyase (propanoyl-CoA-forming, sodium-transporting)
This bacterial enzyme couples the decarboxylation of (S)-methylmalonyl-CoA to propanoyl-CoA to the vectorial transport of Na+ across the cytoplasmic membrane, thereby creating a sodium ion motive force that is used for ATP synthesis. It is a membrane-associated biotin protein and is strictly dependent on sodium ions for activity.
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CAS REGISTRY NUMBER
COMMENTARY
37289-44-4
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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
?
-
-
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 + Na+[side 1] + H+[side 2]
propanoyl-CoA + CO2 + Na+[side 2]
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-
-
-
?
(S)-methylmalonyl-CoA + Na+[side 1] + H+[side 2]
propanoyl-CoA + CO2 + Na+[side 2]
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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 + Na+[side 1] + H+[side 2]
propanoyl-CoA + CO2 + Na+[side 2]
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-
-
?
(S)-methylmalonyl-CoA + Na+[side 1] + H+[side 2]
propanoyl-CoA + CO2 + Na+[side 2]
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-
-
-
?
(S)-methylmalonyl-CoA + Na+[side 1] + H+[side 2]
propanoyl-CoA + CO2 + Na+[side 2]
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irreversible
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-
?
(S)-methylmalonyl-CoA + Na+[side 1] + H+[side 2]
propanoyl-CoA + CO2 + Na+[side 2]
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retention of the configuration during the decarboxylation reaction
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?
(S)-methylmalonyl-CoA + Na+[side 1] + H+[side 2]
propanoyl-CoA + CO2 + Na+[side 2]
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enzyme of the succinate pathway
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-
?
(S)-methylmalonyl-CoA + Na+[side 1] + H+[side 2]
propanoyl-CoA + CO2 + Na+[side 2]
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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 + Na+[side 1] + H+[side 2]
propanoyl-CoA + CO2 + Na+[side 2]
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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 + Na+[side 1] + H+[side 2]
propanoyl-CoA + CO2 + Na+[side 2]
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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 + Na+[side 1] + H+[side 2]
propanoyl-CoA + CO2 + Na+[side 2]
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reconstitution of the sodium pump
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-
?
(S)-methylmalonyl-CoA + Na+[side 1] + H+[side 2]
propanoyl-CoA + CO2 + Na+[side 2]
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the enzyme is a sodium-transport decarboxylase
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-
?
(S)-methylmalonyl-CoA + Na+[side 1] + H+[side 2]
propanoyl-CoA + CO2 + Na+[side 2]
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proteoliposomes are reconstituted with the Na+-pump methylmalonyl-CoA decarboxylase from Veillonella alcalescens
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-
?
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NATURAL SUBSTRATE
NATURAL 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
(S)-methylmalonyl-CoA + Na+[side 1] + H+[side 2]
propanoyl-CoA + CO2 + Na+[side 2]
-
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 + Na+[side 1] + H+[side 2]
propanoyl-CoA + CO2 + Na+[side 2]
-
enzyme of the succinate pathway
-
-
?
(S)-methylmalonyl-CoA + Na+[side 1] + H+[side 2]
propanoyl-CoA + CO2 + Na+[side 2]
-
the Na+-transport enzyme converts the chemical energy of a decarboxylation reaction into an ion gradient
-
-
?
(S)-methylmalonyl-CoA + Na+[side 1] + H+[side 2]
propanoyl-CoA + CO2 + Na+[side 2]
-
the enzyme is responsible for the formation of the propionate moiety in the fermentation of lactate and the decarboxylation of succinate
-
-
?
(S)-methylmalonyl-CoA + Na+[side 1] + H+[side 2]
propanoyl-CoA + CO2 + Na+[side 2]
-
the enzyme is one of the sodium pumps, which are driven by decarboxylation energy
-
-
?
(S)-methylmalonyl-CoA + Na+[side 1] + H+[side 2]
propanoyl-CoA + CO2 + Na+[side 2]
-
reconstitution of the sodium pump
-
-
?
(S)-methylmalonyl-CoA + Na+[side 1] + H+[side 2]
propanoyl-CoA + CO2 + Na+[side 2]
-
the enzyme is a sodium-transport decarboxylase
-
-
?
(S)-methylmalonyl-CoA + Na+[side 1] + H+[side 2]
propanoyl-CoA + CO2 + Na+[side 2]
-
proteoliposomes are reconstituted with the Na+-pump methylmalonyl-CoA decarboxylase from Veillonella alcalescens
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-
?
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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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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
(s)-methylmalonyl-coa decarboxylase (sodium-transporting) deficiency
Dysautonomia in an infant with secondary hyperammonemia due to propionyl coenzyme A carboxylase deficiency.
(s)-methylmalonyl-coa decarboxylase (sodium-transporting) deficiency
Heterozygote expression in propionyl coenzyme A carboxylase deficiency. Differences between major complementation groups.
(s)-methylmalonyl-coa decarboxylase (sodium-transporting) deficiency
Propionyl coenzyme A carboxylase deficiency presenting as non-ketotic hyperglycinaemia.
Cysticercosis
Neuropathological spectrum of drug resistant epilepsy: 15-years-experience from a tertiary care centre.
Epilepsies, Partial
Brain somatic mutations in SLC35A2 cause intractable epilepsy with aberrant N-glycosylation.
Epilepsy
Cognitive functioning after epilepsy surgery in children with mild malformation of cortical development and focal cortical dysplasia.
Epilepsy
Long-term seizure outcome after epilepsy surgery in patients with mild malformation of cortical development and focal cortical dysplasia.
Genetic Diseases, Inborn
Neuropathology of propionic acidemia: a report of two patients with basal ganglia lesions.
Malformations of Cortical Development
Focal cortical dysplasias: surgical outcome in 67 patients in relation to histological subtypes and dual pathology.
Multiple Carboxylase Deficiency
Multiple carboxylase deficiency: clinical and biochemical improvement following neonatal biotin treatment.
peptidyl-glutamate 4-carboxylase deficiency
Dysautonomia in an infant with secondary hyperammonemia due to propionyl coenzyme A carboxylase deficiency.
peptidyl-glutamate 4-carboxylase deficiency
Heterozygote expression in propionyl coenzyme A carboxylase deficiency. Differences between major complementation groups.
peptidyl-glutamate 4-carboxylase deficiency
Multiple carboxylase deficiency: clinical and biochemical improvement following neonatal biotin treatment.
peptidyl-glutamate 4-carboxylase deficiency
Propionyl coenzyme A carboxylase deficiency presenting as non-ketotic hyperglycinaemia.
Primary Dysautonomias
Dysautonomia in an infant with secondary hyperammonemia due to propionyl coenzyme A carboxylase deficiency.
Propionic Acidemia
Determination of methylmalonyl coenzyme A by ultra high-performance liquid chromatography tandem mass spectrometry for measuring propionyl coenzyme A carboxylase activity in patients with propionic acidemia.
Propionic Acidemia
Import of TAT-Conjugated Propionyl Coenzyme A Carboxylase Using Models of Propionic Acidemia.
Propionic Acidemia
Neuropathology of propionic acidemia: a report of two patients with basal ganglia lesions.
Seizures
Cognitive functioning after epilepsy surgery in children with mild malformation of cortical development and focal cortical dysplasia.
Seizures
Epilepsy surgery for pediatric patients with mild malformation of cortical development.
Seizures
Focal cortical dysplasias: surgical outcome in 67 patients in relation to histological subtypes and dual pathology.
Seizures
Long-term seizure outcome after epilepsy surgery in patients with mild malformation of cortical development and focal cortical dysplasia.
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
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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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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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
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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Show AA Sequence and Transmembrane Helices (410 entries)
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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
-
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
-
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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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
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
?
-
x * 60000, alpha, + x * 33000, beta, + x * 18500, gamma, + x * 14000, delta, SDS-PAGE
?
-
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hoffmann, A.; Dimroth, P.
Stereochemistry of the methylmalonyl-CoA decarboxylation reaction
FEBS Lett.
220
121-125
1987
Veillonella parvula
brenda
Hilpert, W.; Dimroth, P.
Sodium pump methylmalonyl-CoA decarboxylase from Veillonella alcalescens
Methods Enzymol.
125
540-546
1986
Veillonella parvula
-
brenda
Hilpert, W.; Dimroth, P.
Reconstitution of Na+ transport from purified merthylmalonyl-CoA decarboxylase and phospholipid vesicles
Eur. J. Biochem.
138
579-583
1984
Veillonella parvula
brenda
Hilpert, W.; Dimroth, P.
Purification and characterization of a new sodium-transport decarboxylase
Eur. J. Biochem.
132
579-587
1983
Veillonella parvula
brenda
Galivan, J.H.; Allen, S.H.G.
Methylmalonyl-CoA decarboxylase: partial purification and enzymatic properties
Arch. Biochem. Biophys.
126
838-847
1968
Veillonella parvula
brenda
Galivan, J.H.; Allen, S.H.G.
Methylmalonyl coenzyme A decarboxylase. Its role in succinate decarboxylation by Micrococcus lactilyticus
J. Biol. Chem.
243
1253-1261
1968
Veillonella parvula
brenda
Hilpert, W.; Dimroth, P.
Conversion of the chemical energy of methylmalonyl-CoA decarboxylation into a Na+ gradient
Nature
296
584-585
1982
Veillonella parvula
brenda
Rohde, M.; Dkena, P.; Mayer, F.; Dimroth, P.
Morphological properties of proteoliposomes reconstituted with Na+ pump methylmalonyl-CoA decarboxylase from Veillonella alcalescens
FEBS Lett.
195
280-284
1986
Veillonella parvula
-
brenda
Hoffmann, A.; Hilpert, W.; Dimroth, P.
The carboxyltransferase activity of the sodium-ion-translocating methylmalonyl-CoA decarboxylase of Veillonella alcalescens
Eur. J. Biochem.
179
645-650
1989
Veillonella parvula
brenda
Bott, M.; Pfister, K.; Burda, P.; Kalbermatter, O.; Woehlke, G.; Dimroth, P.
Methylmalonyl-CoA decarboxylase from Propionibacterium modestum. Cloning and sequencing of the structural genes and purification of the enzyme complex
Eur. J. Biochem.
250
590-599
1997
Propionigenium modestum
brenda
Benning, M.M.; Haller, T.; Gerlt, J.A.; Holden, H.M.
New reactions in the crotonase superfamily: structure of methylmalonyl CoA decarboxylase from Escherichia coli
Biochemistry
39
4630-4639
2000
Escherichia coli
brenda
Chen, L.; Chen, J.; Jiang, Y.; Zhang, W.; Jiang, W.; Lu, Y.
Transcriptomics analyses reveal global roles of the regulator AveI in Streptomyces avermitilis
FEMS Microbiol. Lett.
298
199-207
2009
Campylobacter sp. BCW_6873
brenda
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EXTERNAL LINKS (specific for EC-Number 7.2.4.3)
Transporter Classification Database (TCDB): 3.B.1.1.2
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