Information on EC 4.1.1.6 - aconitate decarboxylase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
4.1.1.6
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RECOMMENDED NAME
GeneOntology No.
aconitate decarboxylase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
cis-aconitate = itaconate + CO2
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
C5-Branched dibasic acid metabolism
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itaconate biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
cis-aconitate carboxy-lyase (itaconate-forming)
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CAS REGISTRY NUMBER
COMMENTARY hide
9025-01-8
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene cadA
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
no activity in Ashbya gossypii
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
metabolism
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
cis-aconitate
?
show the reaction diagram
cis-aconitate
itaconate + CO2
show the reaction diagram
citrate
itaconate + CO2
show the reaction diagram
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-
-
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D-isocitrate
itaconate + CO2
show the reaction diagram
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-
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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
cis-aconitate
?
show the reaction diagram
cis-aconitate
itaconate + CO2
show the reaction diagram
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Fluorocitrate
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inhibits citrate decarboxylation, no inhibition of decarboxylation of cis-aconitate
L-Isocitric acid
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competitive inhibition
p-chloromercuribenzoate
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trans-aconitate
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slight inhibition of decarboxylation of citrate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.45
cis-aconitate
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pH 6.2, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
a novel assay method
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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in human gastric cancer cell lines SGC7901
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
52720
calculated from amino acid sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
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recombinant enzyme in cell free extract, 20 min, inactivation
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
no loss of activity after dialysis for 2 h at 0°C against 0.05 M phosphate buffer, pH 7. Inactivation after 15 h
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
espressed as recombinant protein in Escherichia coli
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expressed in Escherichia coli BL21(DE3) cells and in Aspergillus niger strain AB 1.13
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expressed in Saccharomyces cerevisiae
gene cadA, heterologous expression in Aspergillus niger strain N201, expression of two previously identified Aspergillus terreus genes encoding putative organic acid transporters, genes mttA and mfsA, increases itaconic acid production in an Aspergillus niger cis-aconitate decarboxylase expressing strain, production method optimization, overview
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gene cadA, heterologous functional expression in citric acid producing Aspergillus niger under various constitutive promoters of different expression strength, heterologous expression of the gene in Saccharomyces cerevisiae
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gene cadA, the cadA gene of is located in a gene cluster together with two transporters, one a putative mitochondrial carrier, the other a putative plasma membrane carrier, cloning in Escherichia coli strain TOP10, heterologous mitochondrial and cytosolic expression of the enzyme in Aspergillus niger strain ATCC 1015, the mitochondrial expression doubles the enzyme productivity compared to the cytosolic expression. Co-expression of a cytosolic or a mitochondrial aconitase with cytosolic CadA leads to a significant increase of itaconic acid production compared to cytsolic CadA expression alone. The rate-limiting step for itaconic acid production under these conditions appears to be both the provision of cis-aconitate as a substrate for the CadA as well as the CAD activity itself
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purification with Ni-NTA resin under denaturing conditions
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
industry
economic production of itaconic acid which is a supplement in many products