Information on EC 2.3.3.5 - 2-methylcitrate synthase

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

EC NUMBER
COMMENTARY hide
2.3.3.5
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RECOMMENDED NAME
GeneOntology No.
2-methylcitrate synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
propanoyl-CoA + H2O + oxaloacetate = (2S,3S)-2-hydroxybutane-1,2,3-tricarboxylate + CoA
show the reaction diagram
; the enzyme acts on acetyl-CoA, propanoyl-CoA, butanoyl-CoA and pentanoyl-CoA. The relative rate of condensation of acetyl-CoA and oxaloacetate is 140% of that of propanoyl-CoA and oxaloacetate, but the enzyme has been separated from EC 2.3.3.1 citrate (Si) synthase. Oxaloacetate cannot be replaced by glyoxylate, pyruvate or 2-oxoglutarate
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-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
condensation
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
2-methylcitrate cycle I
-
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2-methylcitrate cycle II
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Propanoate metabolism
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propionate fermentation
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SYSTEMATIC NAME
IUBMB Comments
propanoyl-CoA:oxaloacetate C-propanoyltransferase (thioester-hydrolysing, 1-carboxyethyl-forming)
The enzyme acts on acetyl-CoA, propanoyl-CoA, butanoyl-CoA and pentanoyl-CoA. The relative rate of condensation of acetyl-CoA and oxaloacetate is 140% of that of propanoyl-CoA and oxaloacetate, but the enzyme is distinct from EC 2.3.3.1, citrate (Si)-synthase. Oxaloacetate cannot be replaced by glyoxylate, pyruvate or 2-oxoglutarate.
CAS REGISTRY NUMBER
COMMENTARY hide
57827-78-8
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
psychrotolerant antarctic eubacterium, strain DS2-3R
-
-
Manually annotated by BRENDA team
IFO 6662
-
-
Manually annotated by BRENDA team
contig261
-
-
Manually annotated by BRENDA team
contig261
-
-
Manually annotated by BRENDA team
Burkholderia sacchari
Burkholderia sacchari IPT101
strain IPT101
-
-
Manually annotated by BRENDA team
CBS 565, IFO 0720, CBS 1904, CBS 2015, CBS 6174, OM-102
-
-
Manually annotated by BRENDA team
IFO 0569
-
-
Manually annotated by BRENDA team
IFO 0753
-
-
Manually annotated by BRENDA team
IFO 0661
-
-
Manually annotated by BRENDA team
IFO 0966
-
-
Manually annotated by BRENDA team
IFO 0651
-
-
Manually annotated by BRENDA team
IFO 0732
-
-
Manually annotated by BRENDA team
IFO 0545
-
-
Manually annotated by BRENDA team
IAM 4094
-
-
Manually annotated by BRENDA team
IAM 4094
-
-
Manually annotated by BRENDA team
IFO 0032
-
-
Manually annotated by BRENDA team
JM109
-
-
Manually annotated by BRENDA team
K12
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
IFO 0586, IFO 0882
-
-
Manually annotated by BRENDA team
IFO 0678
-
-
Manually annotated by BRENDA team
IFO 0561
-
-
Manually annotated by BRENDA team
Mucor rouxianus
IFO 5773
-
-
Manually annotated by BRENDA team
IFO 6067
-
-
Manually annotated by BRENDA team
no activity in Candida rugosa
IFO 0750, NPA-1, IFO 1364
-
-
Manually annotated by BRENDA team
no activity in Sus scrofa
pig
-
-
Manually annotated by BRENDA team
IFO 0799
-
-
Manually annotated by BRENDA team
IFO 0947
-
-
Manually annotated by BRENDA team
PAO
-
-
Manually annotated by BRENDA team
contig267
-
-
Manually annotated by BRENDA team
contig267
-
-
Manually annotated by BRENDA team
Pseudomonas putida contig10768
contig10768
-
-
Manually annotated by BRENDA team
contig5376
-
-
Manually annotated by BRENDA team
contig5376
-
-
Manually annotated by BRENDA team
IAM 6003
-
-
Manually annotated by BRENDA team
R-10 (DSM 4252)
-
-
Manually annotated by BRENDA team
CBS 8066
-
-
Manually annotated by BRENDA team
SANK 50182
-
-
Manually annotated by BRENDA team
IFO 1711, IFO 1744
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
IFO 1363
-
-
Manually annotated by BRENDA team
contig93
-
-
Manually annotated by BRENDA team
contig93
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-
Manually annotated by BRENDA team
IFO 0381
-
-
Manually annotated by BRENDA team
Ustilago crus-galli
F-B-6
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-
Manually annotated by BRENDA team
Ustilago crus-galli F-B-6
F-B-6
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-
Manually annotated by BRENDA team
Ustilago utriculosa
F-B-5
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-
Manually annotated by BRENDA team
Ustilago utriculosa F-B-5
F-B-5
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-
Manually annotated by BRENDA team
IFO 0121
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-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
-
methylcitrate cycle
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
acetyl-CoA + H2O + oxaloacetate
?
show the reaction diagram
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-
-
?
acetyl-CoA + H2O + oxaloacetate
? + CoA
show the reaction diagram
-
-
-
-
?
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
show the reaction diagram
butyryl-CoA + H2O + oxaloacetate
?
show the reaction diagram
-
-
-
?
n-butyryl-CoA + H2O + oxaloacetate
2-ethylcitrate + CoA
show the reaction diagram
n-valeryl-CoA + H2O + oxaloacetate
2-propylcitrate + CoA
show the reaction diagram
-
-
-
-
r
propanoyl-CoA + H2O + oxaloacetate
(2S,3S)-2-methylcitrate + CoA
show the reaction diagram
propanoyl-CoA + H2O + oxaloacetate
2-methylcitrate + CoA
show the reaction diagram
propionyl-CoA + H2O + oxaloacetate
(2R,3S)-2-hydroxybutane-1,2,3-tricarboxylate + CoA
show the reaction diagram
valeryl-CoA + H2O + oxaloacetate
?
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
propanoyl-CoA + H2O + oxaloacetate
(2S,3S)-2-methylcitrate + CoA
show the reaction diagram
-
reaction is followed by isomerization of (2S,3S)-2-methylcitrate, i.e. (2S,3S)-2-hydroxybutane-1,2,3-tricarboxylate, to (2R,3S)-2-methylisocitrate, i.e. (2R,3S)-2-hydroxybutane-1,2,3-tricarboxylate, via cis-2-methylaconitate, key enzyme in the methylcitrate cycle for alpha-oxidation of propionate to pyruvate, overview
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-
ir
propanoyl-CoA + H2O + oxaloacetate
2-methylcitrate + CoA
show the reaction diagram
propionyl-CoA + H2O + oxaloacetate
(2R,3S)-2-hydroxybutane-1,2,3-tricarboxylate + CoA
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
1 mM, relative activity 104%
Fe2+
-
0.02 mM, relative activity 104%
Mg2+
-
1 mM, relative activity 102%
additional information
-
Mg2+, Cu2+, Ni2+, Co2+, and EDTA do not have any effect on the enzyme
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetyl-CoA
competitive to CoA
ADP
-
slight inhibition
Monoiodoacetamide
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-
p-chloromercuribenzoate
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Propionate
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propionyl-CoA
competitive to CoA
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
isocitrate
-
1 mM, relative activity 101%
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00126 - 0.35
acetyl-CoA
0.022
Butyryl-CoA
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-
0.0085 - 0.0325
CoA
0.00063 - 0.025
oxaloacetate
0.0017 - 0.061
propanoyl-CoA
0.00188 - 0.037
propionyl-CoA
0.025
valeryl-CoA
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.87 - 29.9
acetyl-CoA
23
oxaloacetate
Aspergillus nidulans
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pH 8.0, 25C, purified native enzyme
8.25 - 23
propanoyl-CoA
12.5 - 15.9
propionyl-CoA
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7.05
acetyl-CoA
Salmonella enterica subsp. enterica serovar Typhimurium
Q56063
in 50 mM HEPES pH 8.0, at 30C
29
183
propanoyl-CoA
Salmonella enterica subsp. enterica serovar Typhimurium
Q56063
in 50 mM HEPES pH 8.0, at 30C
782
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.053
propionyl-CoA
versus CoA
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.002
-
CBS 1904, CBS 2015
0.003
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wild-type strain, carbon source glucose
0.004
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complemented methylcitrate synthase mutant 11/12 B1, carbon source glucose
0.005
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OM-102
0.0051
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nuclei-free homogenate, glucose grown cells
0.006
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CBS 6174
0.0092
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nuclei-free homogenate, n-alkane grown cells
0.019
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heavy particulate fraction, glucose grown cells
0.025
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-
0.028
-
IFO 1457
0.029
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complemented methylcitrate synthase mutant 11/12 B1, carbon source olive oil
0.034
-
IFO 1542
0.042
-
CBS 0882
0.052
-
R-2, propionyl-CoA
0.053
Ustilago crus-galli
-
-
0.056
-
CBS 0586
0.085
-
wild-type strain, carbon source peptone
0.12
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partially purified preparation
0.13
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strain SMI45
0.165
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complemented methylcitrate synthase mutant 11/12 B1, carbon source peptone
0.2
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strain SMB/acuA
0.21
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IFO 1659, acetyl-CoA
0.22
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R-2, acetyl-CoA
0.436
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substrate propionyl-CoA
0.623
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substrate acetyl-CoA
14.5
-
purified native enzyme, with oxaloacetate and propionyl-CoA
15.31
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propionyl-CoA
17.7
purified native enzyme, with oxaloacetate and propionyl-CoA
19.05
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acetyl-CoA
19.55
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propionyl-CoA
36.6
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acetyl-CoA
41.5
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purified native enzyme, with oxaloacetate and acetyl-CoA
48
purified native enzyme, with oxaloacetate and acetyl-CoA
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 10.5
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-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45 - 50
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
49 - 54
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.82
calculated from sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Coxiella burnetii (strain RSA 493 / Nine Mile phase I)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
42570
prpC1, amino acid sequence calculated from cDNA
42600
prpC2, amino acid sequence calculated from cDNA
42690
Burkholderia sacchari
-
amino acid sequence calculated from cDNA
42720
-
amino acid sequence
43000
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SDS-PAGE
43100
amino acid sequence calculated from cDNA
90000
-
native enzyme, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
-
N-terminal processing of the mitochondrial signal import sequence
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 9
3 h, stable
661700
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
3 h, stable up to
50
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activity completely lost after 10 min
52 - 60
the enzyme has a melting temperature of 52C. Tm increases to 60C when the enzyme is preincubated with 0.1 mM oxaloacetate
60
half-life 11 min
95
-
half-life at 90C is 12 min, active even at mesophilic temperatures, at 40C enzyme retains 20-30% of the maximum activity
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme 136fold to homogeneity
native enzyme 72.5fold from strain SMB/acuA
-
on a gravity-flow Ni-NTA agarose column
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
gene mscA, DNA and amino acid sequence determination and analysis, overexpression in Aspergillus nidulans
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gene prpC sequenced
gene prpC sequenced; pRES1, prpC gene cloned into mutant Escherichia coli W620
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gene sequenced
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genome sequencing, prpDBC gene cluster, prpC2 gene for 2-methylcitrate synthase, cloned into vector pTrc99a and expressed in Escherichia coli
into the pCR2.1 and pUChph1 vectors
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into the vector pJET1.2 for sequencing, into a modified pET43.1a vector for expression in Escherichia coli BL21DE3 Rosetta 2 cells
prpC cloned, sequenced and expressed in Escherichia coli
Burkholderia sacchari
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prpC encoded enzyme complements a prpC mutant of Salmonella enterica serovar Typhimurium, transduction of genomic DNA ligated into the cosmid pHC79 to Escherichia coli S17-1
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the chromosomal gene encoding the 2-methyl-cis-aconitate hydratase is disrupted by direct insertion of a copy of an additional 2-methylcitrate synthase gene (prpc). 2-Methylcitrate synthase is expressed under the control of the constitutive kanamycin-resistance gene resulting in up to 20fold higher specific 2-methylcitrate synthase activities in comparison to the wild-type. The disruption of the acnM gene by insertion of prpC leads to a propionate- and levulinate-negative phenotype of the engineered strains and accumulation of 2-methylcitrate in the medium
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
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implications for propionate as an antifungal agent
medicine
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invasive aspergillosis is a life-threatening disease mainly caused by the fungus Aspergillus fumigatus, blocking of methylcitrate synthase abrogates fungal growth and provides a suitable target for new antifungals
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