Information on EC 2.1.3.1 - methylmalonyl-CoA carboxytransferase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
2.1.3.1
-
RECOMMENDED NAME
GeneOntology No.
methylmalonyl-CoA carboxytransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(S)-methylmalonyl-CoA + pyruvate = propanoyl-CoA + oxaloacetate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carboxyl group transfer
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
pyruvate fermentation to propanoate I
-
-
propionate fermentation
-
-
Propanoate metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
(S)-methylmalonyl-CoA:pyruvate carboxytransferase
A biotinyl-protein, containing cobalt and zinc.
CAS REGISTRY NUMBER
COMMENTARY hide
9029-86-1
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
immobilized in a fibrous-bed bioreactor
-
-
Manually annotated by BRENDA team
subsp. shermanii, gene mmc
-
-
Manually annotated by BRENDA team
Propionibacterium sp.
-
-
-
Manually annotated by BRENDA team
strain T1558
-
-
Manually annotated by BRENDA team
strain T1558
-
-
Manually annotated by BRENDA team
activity is located on the alpha-subunit of membrane-bound methylmalonyl-CoA decarboxylase EC 4.1.1.41
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
physiological function
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
3-fluoropropionyl-CoA + oxaloacetate
acrylyl-CoA + pyruvate + F- + CO2
show the reaction diagram
Propionibacterium sp.
-
no F-release if pyruvate or malate are substituted for oxaloacetate
-
-
acetoacetyl-CoA + oxaloacetate
3-oxoglutaryl-CoA + pyruvate
show the reaction diagram
acetyl-CoA + oxaloacetate
malonyl-CoA + pyruvate
show the reaction diagram
butyryl-CoA + oxaloacetate
ethylmalonyl-CoA + pyruvate
show the reaction diagram
propionyl-CoA + oxaloacetate
(S)-methylmalonyl-CoA + pyruvate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
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
propionyl-CoA + oxaloacetate
(S)-methylmalonyl-CoA + pyruvate
show the reaction diagram
Propionibacterium sp.
-
-
-
r
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
biotin
additional information
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
Mn2+
-
activates AP3 production slightly at 5 mM
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(S)-methylmalonyl-CoA
Propionibacterium sp.
-
-
2-oxobutyrate
Propionibacterium sp.
-
-
3-methyloxaloacetate
Propionibacterium sp.
-
strong
Avidin
-
Co2+
-
inhibits AP3 production at 0.5-2 mM
coenzyme A
Propionibacterium sp.
-
-
Cu2+
-
inhibits AP3 production slightly at 0.5 mM
oxalate
Propionibacterium sp.
-
-
oxaloacetate
Propionibacterium sp.
-
-
propionyl pantetheine
Propionibacterium sp.
-
-
propionyl-CoA
Propionibacterium sp.
-
-
pyruvate
Propionibacterium sp.
-
-
SH-reagents
Propionibacterium sp.
-
weak
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0077
(2S)-methylmalonyl-coenzyme A
0.5
acetyl-CoA
Propionibacterium sp.
-
-
0.25
Butyryl-CoA
Propionibacterium sp.
-
-
0.035
malonyl-CoA
Propionibacterium sp.
-
-
0.063
oxaloacetate
Propionibacterium sp.
-
-
0.034
propionyl-CoA
Propionibacterium sp.
-
-
0.0044 - 0.77
pyruvate
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
Propionibacterium freudenreichii subsp. shermanii
-
2530 nmol oxaloacetate per nmol biotin per min
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00004
(S)-methylmalonyl-CoA
Propionibacterium sp.
-
-
0.025
2-oxobutyrate
Propionibacterium sp.
-
-
0.003
3-methyloxaloacetate
Propionibacterium sp.
-
-
0.0063
coenzyme A
Propionibacterium sp.
-
-
0.000018
oxalate
Propionibacterium sp.
-
-
0.0007
oxaloacetate
Propionibacterium sp.
-
-
0.003 - 0.007
propionyl pantetheine
Propionibacterium sp.
-
-
0.00049
propionyl-CoA
Propionibacterium sp.
-
-
0.0089
pyruvate
Propionibacterium sp.
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.075
-
carbon source: glucose
0.15
-
carbon source: starch
0.19
-
carbon source: rapeseed oil
40
Propionibacterium sp.
-
-
43
-
recombinant 5S subunit + assembly-promotin factor, overall reaction
323
-
5S subunit, partial reaction 2
330
-
recombinant 5S subunit, partial reaction 2
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 7.8
Propionibacterium sp.
-
broad
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 7.5
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28
Propionibacterium sp.
-
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.9
-
determined by 2D gel electrophoresis, 1.3S subunit
5.12
-
determined by 2D gel electrophoresis, 5S subunit
5.15
-
determined by 2D gel electrophoresis, 12S subunit
5.18
-
calculated pI-value, 1.3S subunit
5.26
-
calculated pI-value, 12S subunit
5.27
-
calculated pI-value, 5S subunit
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
not heart muscle
Manually annotated by BRENDA team
additional information
-
not ox liver
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
12370
-
calculated molecular mass, 1.3S subunit
55000
-
native recombinant protein after intein tag cleavage
55620
-
calculated molecular mass, 5S subunit
55700
-
5S subunit, 505 amino acids
56400
-
calculated molecular mass, 12S subunit
58000
-
determined by SDS-PAGE
63000
-
determined by 2D gel electrophoresis, 5S subunit
67000
-
determined by 2D gel electrophoresis, 12S subunit
95000
-
5S subunit, recombinant fusion protein, 505 amino acids
110000
-
5S subunit, outer subunit, six per complex
330000
-
12S subunit, central hexameric core
additional information
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 55620, calculated, x * 55623, ESI-MS, x * 55500, SDS-PAGE of 5S subunit
multimer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
side-chain modification
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
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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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5
-
26S-form stable
485819, 485820
6.5
-
stable, at pH 8 enzyme dissociates
485818
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
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
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
glycerol, 20% retards dissociation of 12S and 6S-biotinyl subunit
Propionibacterium sp.
-
polyvalent anions stabilize
Propionibacterium sp.
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
oxygen prevents reassembly of dissociated subunits
-
485820
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
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; affinity chromatography on avidin-Sepharose
-
a deletion mutant and recombinant enzyme
-
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
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recombinant 5S subunit, single step purification using Intein mediated protein ligation method and cleavage from beads by dithiothreitol; the expressed 5S subunit is purified to apparent homogeneity by a single step process by using Intein mediated protein ligation method
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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
-
recombinant enzyme and mutant 1.3S subunit; separation of transcarboxylase complexes from uncombined 12S, 5S and 1.3S subunits by gel filtration
-
using a chelating Sepharose FF column with immobilized Ni2+
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
1.3S subunit cloned and expressed in Escherichia coli
-
1.3S subunit cloned and expressed in Escherichia coli; 5S subunit cloned and expressed in Escherichia coli
-
12S subunit cloned and expressed in Escherichia coli
-
5S subunit cloned and expressed in Escherichia coli
-
5S subunit of enzyme; the gene encoding the 5S subunit is cloned into the pTXB1 vector
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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
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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
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the dtsR1 gene is subcloned from a pUC19 plasmid carrying the dtsR1 gene into the pET26b+ expression vector
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
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
M88T
-
Km not significantly changed, significantly reduced kcat
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
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
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