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Information on EC 2.1.3.1 - methylmalonyl-CoA carboxytransferase and Organism(s) Propionibacterium freudenreichii and UniProt Accession Q70AC7

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IUBMB Comments
A biotinyl-protein, containing cobalt and zinc. The enzyme, described from the bacterium Propionibacterium shermanii, is unique among the biotin-dependent enzymes in that it catalyses carboxyl transfer between two organic molecules, utilizing two separate carboxyltransferase domains. The enzyme is a very large complex, consisting of a hexameric central core of 12S subunits surrounded by six 5S subunit dimers, each connected to the central core by twelve 1.3S biotin carrier subunits.
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Propionibacterium freudenreichii
UNIPROT: Q70AC7
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The taxonomic range for the selected organisms is: Propionibacterium freudenreichii
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
transcarboxylase, dtsr1, methylmalonyl-coa carboxyltransferase, 5s subunit of transcarboxylase, methylmalonyl coa-oxalacetate transcarboxylase, carboxyltransferase subunit of acetyl-coa carboxylase, methylmalonyl-coa carboxytransferase, methylmalonyl-coa transcarboxylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carboxyltransferase, methylmalonyl coenzyme A
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methyl malonyl CoA carboxyl transferase
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methylmalonyl CoA carboxyltransferase
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methylmalonyl coenzyme A carboxyltransferase
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methylmalonyl-CoA carboxyltransferase
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methylmalonyl-CoA transcarboxylase
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oxalacetic transcarboxylase
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transcarboxylase
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carboxyl group transfer
PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
(S)-methylmalonyl-CoA:pyruvate carboxytransferase
A biotinyl-protein, containing cobalt and zinc. The enzyme, described from the bacterium Propionibacterium shermanii, is unique among the biotin-dependent enzymes in that it catalyses carboxyl transfer between two organic molecules, utilizing two separate carboxyltransferase domains. The enzyme is a very large complex, consisting of a hexameric central core of 12S subunits surrounded by six 5S subunit dimers, each connected to the central core by twelve 1.3S biotin carrier subunits.
CAS REGISTRY NUMBER
COMMENTARY hide
9029-86-1
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(S)-methylmalonyl-CoA + pyruvate
propanoyl-CoA + oxaloacetate
show the reaction diagram
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
(S)-methylmalonyl-CoA + pyruvate
propanoyl-CoA + oxaloacetate
show the reaction diagram
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.9
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determined by 2D gel electrophoresis, 1.3S subunit
5.12
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determined by 2D gel electrophoresis, 5S subunit
5.15
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determined by 2D gel electrophoresis, 12S subunit
5.18
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calculated pI-value, 1.3S subunit
5.26
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calculated pI-value, 12S subunit
5.27
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calculated pI-value, 5S subunit
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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the enzyme is one of three biotin-dependent carboxylases in the dicarboxylic acid pathway controlling the carbon fluxin the Wood-Werkman cycle, metabolic flux analysis
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
12000
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determined by 2D gel electrophoresis, 1.3S subunit
12370
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calculated molecular mass, 1.3S subunit
55620
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calculated molecular mass, 5S subunit
56400
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calculated molecular mass, 12S subunit
63000
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determined by 2D gel electrophoresis, 5S subunit
67000
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determined by 2D gel electrophoresis, 12S subunit
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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metabolic engineering of Propionibacteriumfreudenreichii subsp. shermanii DSM 4902 for enhanced propionic acid fermentation by overexpression of pyruvate carboxylase, methylmalonyl-CoA decarboxylase, and methylmalonyl-CoA carboxyltransferase, three biotin-dependent carboxylases in the dicarboxylic acid pathway controlling the carbon fluxin the Wood–Werkman cycle, from Propionibacterium acidipropionici ATCC 4875 in Propionibacterium shermani. The co-fermentation kinetics show that with more glycerol as carbon source, both the wild-type and Ps(pKPYC4) produce more propionic acid and succinic acid, but acetic acid formation is not as significantly affected, neither is the Gly/Glu ratio, metabolic flux analysis, detailed overview
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
radioactive labeling of Propionibacterium freudenreichii proteins is performed, analysis of the proteins by two-dimensional gel electrophoresis follows
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene mmc, co-overexpression of pyruvate carboxylase, methylmalonyl-CoA decarboxylase, and methylmalonyl-CoA carboxyltransferase from Propionibacterium acidipropionici ATCC 4875 in Propionibacterium shermanii, the MMC activity increases by 107%
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
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use of enzyme as a molecular marker for specific detection of Propionibacterium freudenreichii in human microbiota. Rapid quantification of bacteria by real time PCR using enzyme operon
diagnostics
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monitoring propionibacteria population and propionic fermentation in human trials constitutes a crucial step in determining Propionibacterium freudenreichii ability to prevent intestinal disorders
medicine
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use of enzyme as a molecular marker for specific detection of Propionibacterium freudenreichii in human microbiota. Rapid quantification of bacteria by real time PCR using enzyme operon. Propionibacterium freudenreichii not only survives but remains metabolically active in the human gut
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Herve, C.; Fondrevez, M.; Cheron, A.; Barloy-Hubler, F.; Jan, G.
Transcarboxylase mRNA: a marker which evidences P. freudenreichii survival and metabolic activity during its transit in the human gut
Int. J. Food Microbiol.
113
303-314
2007
Propionibacterium freudenreichii
Manually annotated by BRENDA team
Wang, Z.; Lin, M.; Wang, L.; Ammar, E.; Yang, S.
Metabolic engineering of Propionibacterium freudenreichii subsp. shermanii for enhanced propionic acid fermentation: Effects of overexpressing three biotin-dependent carboxylases
Process Biochem.
50
194-204
2015
Propionibacterium freudenreichii, Propionibacterium freudenreichii DSM 4902
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Manually annotated by BRENDA team