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Information on EC 2.1.3.1 - methylmalonyl-CoA carboxytransferase
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EC Tree
2.1.3.1 methylmalonyl-CoA carboxytransferaseIUBMB 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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Word Map
- 2.1.3.1
- biotin
- propionibacterium
- shermanii
- propionyl-coa
-
biotin-containing
-
biotin-dependent
- carboxylases
- freudenreichii
-
propionyl
- carboxybiotin
-
transcarboxylation
-
biotin-binding
- medicine
- analysis
- diagnostics
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
transcarboxylase, dtsr1, methylmalonyl-coa carboxyltransferase, 5s subunit of transcarboxylase, carboxyltransferase subunit of acetyl-coa carboxylase, methylmalonyl-coa carboxytransferase, methylmalonyl-coa transcarboxylase, methylmalonyl coa-oxalacetate transcarboxylase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
carboxyltransferase, methylmalonyl coenzyme A
-
-
-
-
MCT
methylmalonyl CoA carboxyltransferase
-
-
-
-
methylmalonyl CoA-oxalacetate transcarboxylase
-
-
methylmalonyl coenzyme A carboxyltransferase
-
-
-
-
methylmalonyl-CoA carboxyltransferase
methylmalonyl-CoA transcarboxylase
-
-
-
-
MMC
oxalacetic transcarboxylase
-
-
-
-
transcarboxylase
methylmalonyl-CoA carboxyltransferase
-
-
-
transcarboxylase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(S)-methylmalonyl-CoA + pyruvate = propanoyl-CoA + oxaloacetate
mechanism
-
(S)-methylmalonyl-CoA + pyruvate = propanoyl-CoA + oxaloacetate
mechanism
-
(S)-methylmalonyl-CoA + pyruvate = propanoyl-CoA + oxaloacetate
partial reaction 1 is catalysed specifically by the 12S subunit, partial reaction 2 is catalysed specifically by the 5S subunit
-
(S)-methylmalonyl-CoA + pyruvate = propanoyl-CoA + oxaloacetate
homology model of human pyruvate carboxyltransferase, conserved mechanism
(S)-methylmalonyl-CoA + pyruvate = propanoyl-CoA + oxaloacetate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
carboxyl group transfer
carboxyl group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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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.
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CAS REGISTRY NUMBER
COMMENTARY
9029-86-1
-
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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
3-fluoropropionyl-CoA + oxaloacetate
acrylyl-CoA + pyruvate + F- + CO2
-
no F-release if pyruvate or malate are substituted for oxaloacetate
-
?
(S)-methylmalonyl-CoA + pyruvate
propanoyl-CoA + oxaloacetate
-
-
-
-
?
(S)-methylmalonyl-CoA + pyruvate
propanoyl-CoA + oxaloacetate
-
-
-
-
r
(S)-methylmalonyl-CoA + pyruvate
propanoyl-CoA + oxaloacetate
Propionibacterium freudenreichii DSM 4902
-
-
-
-
?
(S)-methylmalonyl-CoA + pyruvate
propanoyl-CoA + oxaloacetate
-
-
-
-
?
(S)-methylmalonyl-CoA + pyruvate
propanoyl-CoA + oxaloacetate
-
-
-
-
r
(S)-methylmalonyl-CoA + pyruvate
propanoyl-CoA + oxaloacetate
-
-
-
-
r
acetoacetyl-CoA + oxaloacetate
3-oxoglutaryl-CoA + pyruvate
-
-
-
?
acetoacetyl-CoA + oxaloacetate
3-oxoglutaryl-CoA + pyruvate
-
-
-
?
acetoacetyl-CoA + oxaloacetate
3-oxoglutaryl-CoA + pyruvate
-
carboxylation at about 2.5% the rate of propionyl-CoA
-
?
acetyl-CoA + oxaloacetate
malonyl-CoA + pyruvate
-
-
-
?
acetyl-CoA + oxaloacetate
malonyl-CoA + pyruvate
-
-
-
-
?
acetyl-CoA + oxaloacetate
malonyl-CoA + pyruvate
-
-
-
?
acetyl-CoA + oxaloacetate
malonyl-CoA + pyruvate
-
carboxylation at about 50% the rate of propionyl-CoA
-
r
butyryl-CoA + oxaloacetate
ethylmalonyl-CoA + pyruvate
-
-
-
?
butyryl-CoA + oxaloacetate
ethylmalonyl-CoA + pyruvate
-
-
-
-
?
butyryl-CoA + oxaloacetate
ethylmalonyl-CoA + pyruvate
-
-
-
?
butyryl-CoA + oxaloacetate
ethylmalonyl-CoA + pyruvate
-
carboxylation at about 10% the rate of propionyl-CoA
-
?
propionyl-CoA + oxaloacetate
(S)-methylmalonyl-CoA + pyruvate
-
-
-
r
propionyl-CoA + oxaloacetate
(S)-methylmalonyl-CoA + pyruvate
-
-
-
r
propionyl-CoA + oxaloacetate
(S)-methylmalonyl-CoA + pyruvate
-
-
-
r
propionyl-CoA + oxaloacetate
(S)-methylmalonyl-CoA + pyruvate
-
-
-
r
propionyl-CoA + oxaloacetate
(S)-methylmalonyl-CoA + pyruvate
-
-
-
r
propionyl-CoA + oxaloacetate
(S)-methylmalonyl-CoA + pyruvate
-
spontaneous decarboxylation follows
-
r
propionyl-CoA + oxaloacetate
(S)-methylmalonyl-CoA + pyruvate
-
two partial reactions
-
r
propionyl-CoA + oxaloacetate
(S)-methylmalonyl-CoA + pyruvate
-
two partial reactions
-
r
propionyl-CoA + oxaloacetate
(S)-methylmalonyl-CoA + pyruvate
-
two partial reactions
-
r
propionyl-CoA + oxaloacetate
(S)-methylmalonyl-CoA + pyruvate
-
two partial reactions
-
r
propionyl-CoA + oxaloacetate
(S)-methylmalonyl-CoA + pyruvate
-
two partial reactions
-
r
propionyl-CoA + oxaloacetate
(S)-methylmalonyl-CoA + pyruvate
-
two partial reactions
-
r
propionyl-CoA + oxaloacetate
(S)-methylmalonyl-CoA + pyruvate
-
two partial reactions
-
r
propionyl-CoA + oxaloacetate
(S)-methylmalonyl-CoA + pyruvate
-
two partial reactions
-
r
propionyl-CoA + oxaloacetate
(S)-methylmalonyl-CoA + pyruvate
-
two partial reactions
-
r
propionyl-CoA + oxaloacetate
(S)-methylmalonyl-CoA + pyruvate
-
-
-
r
propionyl-CoA + oxaloacetate
(S)-methylmalonyl-CoA + pyruvate
-
-
enzyme specific for the S isomer
r
propionyl-CoA + oxaloacetate
(S)-methylmalonyl-CoA + pyruvate
-
-
-
?
propionyl-CoA + oxaloacetate
(S)-methylmalonyl-CoA + pyruvate
-
-
-
?
additional information
?
-
-
structural requirements of the C1-donor: carbonyl group in beta-position to carboxyl group being donated and adjacent either to another carboxyl group or to coenzyme A
-
-
?
additional information
?
-
-
structural requirements of the C1-donor: carbonyl group in beta-position to carboxyl group being donated and adjacent either to another carboxyl group or to coenzyme A
-
-
?
additional information
?
-
-
2-oxobutyrate, 2-oxovalerate, 2-oxoglutarate, 3-oxoglutarate cannot replace pyruvate and is no C1-donor
-
-
?
additional information
?
-
-
enzyme catalyses the formation of the precursor of tylosin, protylonoide
-
-
?
additional information
?
-
-
enzyme involved in the biosynthesis of the tylosin
-
-
?
additional information
?
-
-
enzyme catalyses the formation of the precursor of tylosin, protylonoide
-
-
?
additional information
?
-
-
enzyme involved in the biosynthesis of the tylosin
-
-
?
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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
propionyl-CoA + oxaloacetate
(S)-methylmalonyl-CoA + pyruvate
-
-
-
r
(S)-methylmalonyl-CoA + pyruvate
propanoyl-CoA + oxaloacetate
-
-
-
-
?
(S)-methylmalonyl-CoA + pyruvate
propanoyl-CoA + oxaloacetate
-
-
-
-
r
(S)-methylmalonyl-CoA + pyruvate
propanoyl-CoA + oxaloacetate
Propionibacterium freudenreichii DSM 4902
-
-
-
-
?
(S)-methylmalonyl-CoA + pyruvate
propanoyl-CoA + oxaloacetate
-
-
-
-
?
(S)-methylmalonyl-CoA + pyruvate
propanoyl-CoA + oxaloacetate
-
-
-
-
r
(S)-methylmalonyl-CoA + pyruvate
propanoyl-CoA + oxaloacetate
-
-
-
-
r
additional information
?
-
-
enzyme involved in the biosynthesis of the tylosin
-
-
?
additional information
?
-
-
enzyme involved in the biosynthesis of the tylosin
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
biotin
-
requirement
biotin
-
biotinyl-enzyme, 6 mol per 18S and 4 mol per 16S enzyme species
biotin
-
covalently linked to the 1.3 subunit to the epsilon-amino group of Lys-89, which lies in the conserved sequence Ala-Met-Lys-Met
biotin
-
biotin containing subunit of enzyme acts as a carboxyl carrier between the CoA ester sites on the central 12S subunit of enzyme and keto acid sites on outer 5S subunit of enzyme and links the 12S and 5S subunits together to form a 26S multisubunit enzyme complex, biotin content: 28%
additional information
-
no ATP requirement
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Mg2+
-
MCT activity is inhibited at 48 h by Mg2+, and then enhanced to a higher level compared with the control, increase of AP3 production is optimally at 2 mM
Zn2+
additional information
Co2+
-
requirement
Co2+
-
3 types of Co2+: tightly i.e. catalytic, not so tightly, and weakly bound, above 2 mM, stabilizes quarternary structure, no exchange between catalytic and stabilizing Co2+
additional information
-
cell growth in presence of different metal ions, overview
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Guanidinium chloride
-
Co2+ protects
additional information
-
loss of assembly-promoting factor activity after digestion with trypsin, V8 protease, pronase
-
additional information
-
no inhibition by metal chelating agents, such as EDTA
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Carcinoma
A Proposed Physiopathological Pathway to Hyperammonemic Encephalopathy in a Non-Cirrhotic Patient with Fibrolamellar Hepatocellular Carcinoma without Ornithine Transcarbamylase (OTC) Mutation.
Carcinoma, Ehrlich Tumor
Binding of radiolabeled N-(phosphonacetyl)-L-aspartate to aspartate transcarbamylase from Ehrlich ascites tumor cells.
methylmalonyl-coa carboxytransferase deficiency
Development of Gene Therapy Vectors: Remaining Challenges.
Neoplasms
Binding of radiolabeled N-(phosphonacetyl)-L-aspartate to aspartate transcarbamylase from Ehrlich ascites tumor cells.
Urea Cycle Disorders, Inborn
A Proposed Physiopathological Pathway to Hyperammonemic Encephalopathy in a Non-Cirrhotic Patient with Fibrolamellar Hepatocellular Carcinoma without Ornithine Transcarbamylase (OTC) Mutation.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kinetics and mechanism
-
additional information
additional information
-
kinetic deuterium and 13C-isotope effects
-
additional information
additional information
-
kinetic parameters of wild-type and mutant enzyme
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
2530 nmol oxaloacetate per nmol biotin per min
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.3
330
-
recombinant 5S subunit, partial reaction 2
43
-
recombinant 5S subunit + assembly-promotin factor, overall reaction
48
additional information
2.3
-
recombinant 5S subunit, overall reaction
additional information
-
comparison of wild-type and mutant enzymes
additional information
-
comparison of wild-type and truncated forms
additional information
-
the recombinant 5S subunit is active in partial reaction 2 but not in overall enzyme reaction and not able to form a enzyme complex
additional information
-
specific activity depends on the carbon source and increases during culture time
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
activity is located on the alpha-subunit of membrane-bound methylmalonyl-CoA decarboxylase EC 4.1.1.41
-
-
brenda
enzyme is expressed during propionic fermentation, ceases in starved cells and is not affected by digestive stress
-
-
brenda
-
485817, 485818, 485819, 485820, 485822, 485825, 485826, 485827, 485828, 485829, 485830, 485831, 485832, 485834, 657477, 676760, 689897, 756213
-
-
brenda
5S metalloenzyme subunit
Uniprot
brenda
i.e. Propionibacterium freudenreichii
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
metabolism
-
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
metabolism
-
the enzyme provides an alternative pathway for malonyl-CoA synthesis and increases fatty acid production. The enzyme efficiently directs tricarboxylic acid cycle intermediates towards fatty acid synthesis during the acetyl-CoA carboxylation bypass
metabolism
Propionibacterium freudenreichii DSM 4902
-
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
-
metabolism
-
the enzyme provides an alternative pathway for malonyl-CoA synthesis and increases fatty acid production. The enzyme efficiently directs tricarboxylic acid cycle intermediates towards fatty acid synthesis during the acetyl-CoA carboxylation bypass
-
physiological function
-
the enzyme is involved in production of anticancer ansamitocin P-3, AP-3 by submerged cultures of Actinosynnema pretiosum in medium containing agro-industrial residues. The production is increased by addition of metal ions, especially Mg2+
physiological function
-
the enzyme is involved in production of anticancer ansamitocin P-3, AP-3 by submerged cultures of Actinosynnema pretiosum in medium containing agro-industrial residues. The production is increased by addition of metal ions, especially Mg2+
-
Show AA Sequence and Transmembrane Helices (2155 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
110000
-
5S subunit, outer subunit, six per complex
12000
120000
-
the 26S holoenzyme consists of a hexameric central 12S subunit, 360000 Da and six peripheral dimeric 5S subunits, 6 * 120000 Da each of which is linked to the central subunit by 2 biotinyl 1.3S subunits, 12 * MW 12000
330000
-
12S subunit, central hexameric core
55000
-
native recombinant protein after intein tag cleavage
55500
-
x * 55620, calculated, x * 55623, ESI-MS, x * 55500, SDS-PAGE of 5S subunit
55620
55623
-
x * 55620, calculated, x * 55623, ESI-MS, x * 55500, SDS-PAGE of 5S subunit
95000
-
5S subunit, recombinant fusion protein, 505 amino acids
additional information
12000
-
1.3S subunit, biotinyl subunit, 12 per complex
55620
-
x * 55620, calculated, x * 55623, ESI-MS, x * 55500, SDS-PAGE of 5S subunit
additional information
-
two active forms of enzyme: 18S and 26S
additional information
-
two active forms of enzyme: 18S and 16S, the 16S species arises from 18S species by loss of a 6S biotin, Co, Zn subunit
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 55620, calculated, x * 55623, ESI-MS, x * 55500, SDS-PAGE of 5S subunit
multimer
additional information
multimer
-
the central cylindrical hexameric 12S subunit, the outer six dimeric 5S subunit, and the twelve 1.3S linkers
additional information
-
existence of a novel, previously unidentified subunit, a assemply-promoting factor, APF, which is nessessary for the assemply of enzyme, MW: 60000 Da, SDS-PAGE
additional information
-
MW of 12S hexamer: 338000Da
additional information
-
amino acid sequence of biotinyl subunit
additional information
-
amino acid sequence of biotinyl subunit
additional information
-
amino acid sequence of biotinyl subunit
additional information
-
the 26S holoenzyme consists of a hexameric central 12S subunit, 360000 Da and six peripheral dimeric 5S subunits, 6 * 120000 Da each of which is linked to the central subunit by 2 biotinyl 1.3S subunits, 12 * MW 12000
additional information
-
the 26S holoenzyme consists of a hexameric central 12S subunit, 360000 Da and six peripheral dimeric 5S subunits, 6 * 120000 Da each of which is linked to the central subunit by 2 biotinyl 1.3S subunits, 12 * MW 12000
additional information
-
the 26S holoenzyme consists of a hexameric central 12S subunit, 360000 Da and six peripheral dimeric 5S subunits, 6 * 120000 Da each of which is linked to the central subunit by 2 biotinyl 1.3S subunits, 12 * MW 12000
additional information
-
the 26S holoenzyme consists of a hexameric central 12S subunit, 360000 Da and six peripheral dimeric 5S subunits, 6 * 120000 Da each of which is linked to the central subunit by 2 biotinyl 1.3S subunits, 12 * MW 12000
additional information
-
the 26S holoenzyme consists of a hexameric central 12S subunit, 360000 Da and six peripheral dimeric 5S subunits, 6 * 120000 Da each of which is linked to the central subunit by 2 biotinyl 1.3S subunits, 12 * MW 12000
additional information
-
the 26S holoenzyme consists of a hexameric central 12S subunit, 360000 Da and six peripheral dimeric 5S subunits, 6 * 120000 Da each of which is linked to the central subunit by 2 biotinyl 1.3S subunits, 12 * MW 12000
additional information
-
the 26S holoenzyme consists of a hexameric central 12S subunit, 360000 Da and six peripheral dimeric 5S subunits, 6 * 120000 Da each of which is linked to the central subunit by 2 biotinyl 1.3S subunits, 12 * MW 12000
additional information
-
the 26S holoenzyme consists of a hexameric central 12S subunit, 360000 Da and six peripheral dimeric 5S subunits, 6 * 120000 Da each of which is linked to the central subunit by 2 biotinyl 1.3S subunits, 12 * MW 12000
additional information
-
5S subunit with a native MW 120000 Da, gel filtration and a subunit MW 60000 Da, SDS-PAGE
additional information
-
5S subunit is a dimer of identical monomers, contains Co2+ and Zn2+ and assembles with two 1.3 subunits to form a stable complex termed the 6S subunit
additional information
-
5S subunit is a dimer of identical monomers, contains Co2+ and Zn2+ and assembles with two 1.3 subunits to form a stable complex termed the 6S subunit
additional information
-
1.3 S is homogen, SDS-PAGE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
side-chain modification
side-chain modification
-
deletion of residues 10 to 48 of 1.3S subunit, not necessary for catalysis of the partial reaction
side-chain modification
-
a series of truncated forms of the 1.3S subunit is prepared and the effect on the first and the second partial reaction and the overall enzyme reaction measured, result: the sequence 59-78 of 1.3S subunit is necessary for the carboxylation of biotin of the 1.3 S subunit, the inability of the truncated peptides to form enzyme complexes explains the activity loss in the overall reaction
side-chain modification
-
97 amino acids deleted of the carboxyl-terminal region of the monomer of the 12S subunit, 46% loss of activity because of a reduces stability of the 12S subunit and a decrease in binding of 6S subunit to the 12 subunit
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DtsR1 is crystallized by the sitting-drop vapour-diffusion method using polyethylene glycol 6000 as a precipitant
-
5S-subunit, native, with His-tag and selenomethionine-protein with His-tag. Crystallization of native 5S subunit requires addition of lithium sulfate, with in turn prevents crystallization of His-tagged subunit
-
central 12S hexameric core, in complex with substrate methylmalonyl-CoA. Structure shows two stacked trimers, and a domain duplication in the monomer
of 5S metalloenzyme subunit, free and in complex with substrate pyruvate, product oxaloacetate, or inhibitor 2-ketobutyrate. Dimer of beta8alpha8 barrels with active site cobalt ion
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A87G
-
Km not significantly changed, significantly reduced kcat
M88A
-
Km not significantly changed, significantly reduced kcat
M88C
-
Km not significantly changed, significantly reduced kcat
M88L
M88T
-
Km not significantly changed, significantly reduced kcat
M90L
additional information
M88L
-
Km not significantly changed, significantly reduced kcat
M88L
-
partial reaction 1: 99% loss activity, partial reaction 2: 65% loss of activity, possibly alterations in the microenvironment of the biocytin
M90L
-
Km and kcat not significantly changed
M90L
-
partial reaction 1: 50% loss of activity, partial reaction 2: 115% activity compared to the 1.3 wild-type enzyme
additional information
-
mutant enzyme obtained by adaptation of Propionibacterium acidipropionici immobilized in a fibrous-bed bioreactor for fed-batch fermentation of glucose. Mutant shows enhanced specific activity of methylmalonyl-CoA carboxytransferase and propionyl-CoA:succinyltransferase and lower sensitivity to propionic acid inhibition. Mutant cells have a threefold increase in length and a 24% decrease in diameter
additional information
-
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 WoodWerkman 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
additional information
Propionibacterium freudenreichii DSM 4902
-
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 WoodWerkman 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
-
additional information
-
double mutant A87M and M88A
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8
-
dilute solution, 50 mM buffer, 25°C: enzyme dissociates into subunits and rapidly loses activity, Co2+ protects, Zn2+ protects slightly
485820
9
-
enzyme dissociates into 12SH, 5SE, 6SE and 6SH subunits, in the presence of Co2+: the 6SE subunits binds to 12SH subunit
485820
additional information
-
effect of pH on the overall conformation of the 1.3 subunit, below 3.5 and above 9.0: the N-terminus of the 1.3S protein undergoes a transition into a random coil or unordered conformation
485825
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
-
dissociation and rapid loss of activity in dilute solution in alkaline 50 mM buffer (t1/2: 12 min), Co2+ protects, Zn2+ protects slightly (t1/2: 22 min)
50
-
denaturation within 1 min, Co2+ protects, Zn2+ protects slightly
additional information
-
assembly-promoting factor heat stable
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
alkaline pH, low ionic strength, monovalent ions, low protein concentration and elevated temperatures favor dissociation to inactive 5S, 6S and 1.3S subunits
alkaline pH, low ionic strength, monovalent ions, low protein concentration and elevated temperatures favor dissociation to inactive 5S, 6S and 1.3S subunits
-
alkaline pH, low ionic strength, monovalent ions, low protein concentration and elevated temperatures favor dissociation to inactive 5S, 6S and 1.3S subunits
-
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
oxygen prevents reassembly of dissociated subunits
-
485820
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-12°C, partially purified at least 1 month
-
-70°C, recombinant 5S subunit purified using Intein mediated protein ligation method and cleavage from beads by dithiothreitol, stable for months
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
affinity chromatography on avidin-Sepharose
on chitin column beads, the intein tag is removed by auto-splicing
-
radioactive labeling of Propionibacterium freudenreichii proteins is performed, analysis of the proteins by two-dimensional gel electrophoresis follows
-
recombinant 5S subunit, single step purification using Intein mediated protein ligation method and cleavage from beads by dithiothreitol
-
recombinant enzyme and mutant 1.3S subunit
-
recombinant enzyme and mutant 1.3S subunit, affinity chromatography on avidin(monomeric)-agarose, copurification of apo and biotinylated 1.3S forms
-
separation of transcarboxylase complexes from uncombined 12S, 5S and 1.3S subunits by gel filtration
-
the expressed 5S subunit is purified to apparent homogeneity by a single step process by using Intein mediated protein ligation method
-
affinity chromatography on avidin-Sepharose
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
1.3S subunit cloned and expressed in Escherichia coli
-
12S subunit cloned and expressed in Escherichia coli
-
5S subunit cloned and expressed in Escherichia coli
-
a prokaryotic expression system for the production of a 13C- and 15N-labeled 1.3S subunit mutant that is suitable for structure determination and functional studies by NMR
-
expressed in Escherichia coli strain SBF15
-
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%
-
the 5S subunit protein is expressed as intein fusion protein in pTXB1 vector at the N-terminus in BL21DE3 Escherichia coli cells
-
the dtsR1 gene is subcloned from a pUC19 plasmid carrying the dtsR1 gene into the pET26b+ expression vector
-
the gene encoding the 5S subunit is cloned into the pTXB1 vector
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
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
-
monitoring propionibacteria population and propionic fermentation in human trials constitutes a crucial step in determining Propionibacterium freudenreichii ability to prevent intestinal disorders
medicine
medicine
-
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
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Wood, H.G.
Transcarboxylase
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
6
83-115
1972
Propionibacterium sp.
-
brenda
Swick, R.W.; Wood, H.G.
The role of transcarboxylase in propionic acid ermentation
Proc. Natl. Acad. Sci. USA
46
28-41
1960
Canis lupus familiaris, Propionibacterium freudenreichii subsp. shermanii, Propionibacterium freudenreichii subsp. shermanii 52W
brenda
Berger, M.; Wood, H.G.
Purification of the subunits of transcarboxylase by affinity chromatography on avidin-sepharose
J. Biol. Chem.
250
927-933
1975
Propionibacterium freudenreichii subsp. shermanii
brenda
Maloy, W.L.; Bowien, B.U.; Zwolinski, G.K.; Kumar, K.G.; Wood, H.G.; Ericsson, L.H.; Walsh, K.A.
Amino acid sequence of the biotinyl subunit from transcarboxylase
J. Biol. Chem.
254
11615-11622
1979
Propionibacterium freudenreichii subsp. shermanii
brenda
Harmon, F.R.; Goss, N.H.; Wood, H.G.
Stabilization of the quaternary structure of transcarboxylase by cobalt (II) ions
Biochemistry
21
2847-2852
1982
Propionibacterium freudenreichii subsp. shermanii
brenda
Stubbe, J.; Fish, S.; Abeles, R.H.
Are carboxylations involving biotin concerted or nonconcerted?
J. Biol. Chem.
255
236-242
1980
Propionibacterium sp.
brenda
Shenoy, B.C.; Xie, Y.; Park, V.L.; Kumar, G.K.; Beegen, H.; Wood, H.G.; Samols, D.
The importance of methionine residues for the catalysis of the biotin enzyme, transcarboxylase. Analysis by site-directed mutagenesis
J. Biol. Chem.
267
18407-18412
1992
Propionibacterium freudenreichii subsp. shermanii
brenda
O'Keefe, S.J.; Knowles, J.R.
Biotin-dependent carboxylation catalyzed by transcarboxylase is a stepwise process [published erratum appears in Biochemistry 1987 Sep 8;26(18):5952]
Biochemistry
25
6077-6084
1986
Propionibacterium freudenreichii subsp. shermanii
brenda
Rivera-Hainaj, R.E.; Pusztai-Carey, M.; Reddy, D.V.; Choowongkomon, K.; Soennichsen, F.D.; Carey, P.R.
Characterization of the carboxylate delivery module of transcarboxylase: following spontaneous decarboxylation of the 1.3S-CO2- subunit by NMR and FTIR spectroscopies
Biochemistry
41
2191-2197
2002
Propionibacterium freudenreichii subsp. shermanii
brenda
Zheng, X.; Rivera-Hainaj, R.E.; Zheng, Y.; Pusztai-Carey, M.; Hall, P.R.; Yee, V.C.; Carey, P.R.
Substrate binding induces a cooperative conformational change in the 12S subunit of transcarboxylase: raman crystallographic evidence
Biochemistry
41
10741-10746
2002
Propionibacterium freudenreichii subsp. shermanii
brenda
Shenoy, B.C.; Kumar, G.K.; Samols, D.
Dissection of the biotinyl subunit of transcarboxylase into regions essential for activity and assembly
J. Biol. Chem.
268
2232-2238
1993
Propionibacterium freudenreichii subsp. shermanii
brenda
Shenoy, B.C.; Magner, W.J.; Kumar, G.K.; Phillips, N.F.B.; Haase, F.C.; Samols, D.
The nonbiotinylated form of the 1.3 S subunit of transcarboxylase binds to avidin (monomeric)-agarose: Purification and separation from the biotinylated 1.3 S subunit
Protein Expr. Purif.
4
85-94
1993
Propionibacterium freudenreichii subsp. shermanii
brenda
Shenoy, B.C.; Samols, D.; Kumar, G.K.
The conserved methionines of the 1.3 S biotinyl subunit of transcarboxylase: effect of mutations on conformation and activity
Arch. Biochem. Biophys.
304
359-366
1993
Propionibacterium freudenreichii subsp. shermanii
brenda
Woo, S.B.; Shenoy, B.C.; Wood, H.G.; Magner, W.J.; Kumar, G.K.; Beegen, H.; Samols, D.
Effect of deletion from the carboxyl terminus of the 12 S subunit on activity of transcarboxylase
J. Biol. Chem.
268
16413-16419
1993
Propionibacterium freudenreichii subsp. shermanii
brenda
Xie, Y.; Shenoy, B.C.; Magner, W.J.; Hejlik, D.P.; Samols, D.
Purification and characterization of the recombinant 5 S subunit of transcarboxylase from Escherichia coli
Protein Expr. Purif.
4
456-464
1993
Propionibacterium freudenreichii subsp. shermanii
brenda
Shenoy, B.C.; Xie, Y.; Sha, D.; Samols, D.
Identification and characterization of a factor which is essential for assembly of transcarboxylase
Biochemistry
32
10750-10756
1993
Propionibacterium freudenreichii subsp. shermanii
brenda
Choi, D.B.; Park, Y.; Okabe, M.
Effects of rapeseed oil on activity of methylmalonyl-CoA carboxyltransferase in culture of Streptomyces fradiae
Biosci. Biotechnol. Biochem.
62
902-906
1998
Streptomyces fradiae, Streptomyces fradiae T1558
brenda
Jank, M.M.; Bokorny, S.; Rohm, K.H.; Berger, S.
Expression and biotinylation of a mutant of the transcarboxylase carrier protein from Propioni shermanii
Protein Expr. Purif.
17
123-127
1999
Propionibacterium freudenreichii subsp. shermanii
brenda
Hall, P.R.; Zheng, R.; Pusztai-Carey, M.; van den Akker, F.; Carey, P.R.; Yee, V.C.
Expression and crystallization of several forms of the Propionibacterium shermanii transcarboxylase 5S subunit
Acta Crystallogr. Sect. D
D60
521-523
2004
Propionibacterium freudenreichii subsp. shermanii
brenda
Hall, P.R.; Wang, Y.F.; Rivera-Hainaj, R.E.; Zheng, X.; Pustai-Carey, M.; Carey, P.R.; Yee, V.C.
Transcarboxylase 12S crystal structure: hexamer assembly and substrate binding to a multienzyme core
EMBO J.
22
2334-2347
2003
Propionibacterium freudenreichii subsp. shermanii (Q8GBW6), Propionibacterium freudenreichii subsp. shermanii
brenda
Hall, P.R.; Zheng, R.; Antony, L.; Pusztai-Carey, M.; Carey, P.R.; Yee, V.C.
Transcarboxylase 5S structures: assembly and catalytic mechanism of a multienzyme complex subunit
EMBO J.
23
3621-3631
2004
Propionibacterium freudenreichii subsp. shermanii (Q70AC7), Propionibacterium freudenreichii subsp. shermanii
brenda
Suwannakham, S.; Yang, S.T.
Enhanced propionic acid fermentation by Propionibacterium acidipropionici mutant obtained by adaptation in a fibrous-bed bioreactor
Biotechnol. Bioeng.
91
325-337
2005
Acidipropionibacterium acidipropionici
brenda
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
brenda
Kumar Bhat, R.; Berger, S.
New and easy strategy for cloning, expression, purification, and characterization of the 5S subunit of transcarboxylase from Propionibacterium f. shermanii
Prep. Biochem. Biotechnol.
37
13-26
2007
Propionibacterium freudenreichii subsp. shermanii
brenda
Yamada, M.; Natsume, R.; Nakamatsu, T.; Horinouchi, S.; Kawasaki, H.; Senda, T.
Crystallization and preliminary crystallographic analysis of DtsR1, a carboxyltransferase subunit of acetyl-CoA carboxylase from Corynebacterium glutamicum
Acta Crystallogr. Sect. F
63
120-122
2007
Corynebacterium glutamicum
brenda
Bhat, R.K.; Berger, S.
The 5S subunit of transcarboxylase interacts with free biotin as studied by transferred-NOESY and Saturation Transfer Difference NMR
Protein Pept. Lett.
15
624-629
2008
Propionibacterium freudenreichii subsp. shermanii
brenda
Jia, Y.; Zhong, J.J.
Enhanced production of ansamitocin P-3 by addition of Mg2+ in fermentation of Actinosynnema pretiosum
Biores. Technol.
102
10147-10150
2011
Actinosynnema pretiosum, Actinosynnema pretiosum ATCC 31565
brenda
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
-
brenda
Shin, K.S.; Lee, S.K.
Introduction of an acetyl-CoA carboxylation bypass into Escherichia coli for enhanced free fatty acid production
Biores. Technol.
245
1627-1633
2017
Propionibacterium freudenreichii subsp. shermanii, Propionibacterium freudenreichii subsp. shermanii KCTC5753
brenda
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EXTERNAL LINKS (specific for EC-Number 2.1.3.1)
Transporter Classification Database (TCDB): 3.B.1.1.6
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Release 2023.1 (January 2023)
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