Information on EC 2.8.3.16 - formyl-CoA transferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.8.3.16
-
RECOMMENDED NAME
GeneOntology No.
formyl-CoA transferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
formyl-CoA + oxalate = formate + oxalyl-CoA
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
coenzyme A transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
oxalate degradation II
-
-
SYSTEMATIC NAME
IUBMB Comments
formyl-CoA:oxalate CoA-transferase
The enzyme from Oxalobacter formigenes can also catalyse the transfer of CoA from formyl-CoA to succinate.
CAS REGISTRY NUMBER
COMMENTARY hide
128826-27-7
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
fragment
UniProt
Manually annotated by BRENDA team
Arquibacter sp.
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
USDA 110, gene frc, no detection of the frc-gene in Klebsiella oxytoca, Bacillus subtilis, Micrococcus luteus, Microvirgula aerodenitrificans, Paracoccus denitrificans, Rhodococcus opacus, Xanthobacter agilis and Pseudomonas aeruginosa
UniProt
Manually annotated by BRENDA team
BTAi1, frc gene
UniProt
Manually annotated by BRENDA team
MG1655
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
caiB3 gene
UniProt
Manually annotated by BRENDA team
Gasser AM63T
Q046G6
UniProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
LB400, frc gene
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
CGA009, frc gene
UniProt
Manually annotated by BRENDA team
2a strain 301, frc gene
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
MA-4680, frc gene
UniProt
Manually annotated by BRENDA team
A3, frc gene
UniProt
Manually annotated by BRENDA team
Py2, Xaut_0487 gene
UniProt
Manually annotated by BRENDA team
frc gene, but no Ca-oxalate utilization
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
formyl-CoA + oxalate
formate + oxalyl-CoA
show the reaction diagram
succinyl-CoA + oxalate
succinate + oxalyl-CoA
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
formyl-CoA + oxalate
formate + oxalyl-CoA
show the reaction diagram
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetyl-CoA
-
-
coenzyme A
N-ethylmaleimide
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20% inhibition at 1 mM
oxalate
p-chloromercuribenzoate
-
91% inhibition at 1 mM, causes precipitation
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
oxalate induces the expression of genes frc and oxc
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.002 - 3
formyl-CoA
0.43 - 18
oxalate
2.3
succinate
-
pH 6.7, 25C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.3 - 4.5
formyl-CoA
4.3 - 5
oxalate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1300
formyl-CoA
in 50 mM potassium phosphate, pH 6.7, at 25C
4.5
oxalate
in 50 mM potassium phosphate, pH 6.7, at 25C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3
Cl-
-
chloride is a weak competitive inhibitor to oxalate
16.7
coenzyme A
-
-
23 - 74
oxalate
additional information
additional information
-
Kis for formate is 17 mM, Kii for formate is 380 mM, Kis for oxalyl-CoA is 0.15 mM, Kii for oxalyl-CoA is 0.28 mM
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.63
-
cytoplasmic fraction
2.15
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purified enyzme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
44000
-
1 * 44000, SDS-PAGE
44700
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gel filtration
45000
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1 * 45000, recombiant enzyme, SDS-PAGE
47000
2 * 47000, His6-tagged enzyme, SDS-PAGE
49610
2 * 49610, electrospray ionization mass spectrometry
50000
-
x * 50000, recombinant enzyme, SDS-PAGE
81000
-
gel filtration
83000
His6-tagged enzyme, gel filtration
99000
calculated from amino acid sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 50000, recombinant enzyme, SDS-PAGE
homodimer
monomer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
His6-tagged enzyme, in complex with CoA, hanging drop vapor diffusion method, using 24% (w/v) PEG 4000 and 100 mM bicine, pH 8.8
beta-aspartyl-CoA thioester intermediate is identified by x-ray crystallography
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crystallization and structure determination of the enzyme/oxalyl-CoA complex, hanging drop technique. Crystallization and structure determination of the D169A, D169E, and D169S mutants
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FRC variants W48F and W48Q, hanging drop vapour diffusion method
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purified recombinant enzyme from overexpression in Escherichia coli, hanging drop method, protein solution: 7.5 mg/ml, 25 mM MES, pH 6.2, 10% glycerol, drop volume 0.002 ml, reservoir solution: 100 mM HEPES, pH 7.5, 26% polyethylene glycol 4000, 0.5 M MgCl2, 291 K, 1 week, X-ray diffraction structure determination and analysis
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purified recombinant selenocysteine-substituted enzyme, hanging drop method, protein solution: 4.75 mg/ml, 25 mM MES, pH 6.2, 10% glycerol, drop volume 0.002 ml, reservoir solution: 100 mM HEPES, pH 7.5, 26% polyethylene glycol 4000, 0.5 M MgCl2, 291 K, 2 weeks, X-ray diffraction structure determination and analysis
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80C, 25 mM sodium phosphate, pH 6.2, 300 mM NaCl, 1 mM dithiothreitol and 10% glycerol
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
31.2fold, to homogeneity
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DEAE anion exchange chromatography, Blue-Sepharose fast flow affinity chromatography, Sephadex G-250 size exclusion chromatography, and QHP anion exchange chromatography
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enzyme recombinantly expressed in Escherichia coli
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His-tagged FRC protein is purified by Ni-nitrilotriacetic acid column and subsequent gel filtration
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His-tagged YfdW protein is purified by metal affinity chromatography and subsequent gel filtration on a Superdex 200 column, eluting with 5 mM HEPES buffer containing 150 mM NaCl, pH 7.5.
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iminodiacetate-Ni2+ Sepharose column chromatography
partial, fractionation
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recombinant from Escherichia coli BL21, to homogeneity
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recombinant from Escherichia coli JM109
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selenocysteine-substituted enzyme mutant, recombinant from Escherichia coli, to homogeneity
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA sequence determination and analysis, monocistronic operon, overexpression in Escherichia coli, activity is similar to the wild-type enzyme
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expressed in Escherichia coli BL21(DE3) cells
expression Escherichia coli BL21-DE3
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expression in Escherichia coli BL21-DE3
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expression in Escherichia coli K12
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expression in Escherichia coli XL1
expression in Escherichia coli XL1; expression in Escherichia coli XL1
expression in Escherichia coli XL1; expression in Escherichia coli XL1; expression in Escherichia coli XL1
gene frc, DNA and amino acid sequence determination and analysis, phylogenetic analysis
gene frc, from strain LA14, DNA and amino acid sequence determination and analysis, overexpression of N-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3)
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gene frc, organized in the oxc operon, DNA and amino acid sequence determination and analysis, transcriptional and quantitative expression analysis, mildly acidic conditions are a prerequisite for frc and oxc transcription, phylogenetic analysis
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selenocysteine-substituted enzyme mutant, expression in Escherichia coli
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stable expression in human embryo kidney 293 cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme is induced by acid stress
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D169A
-
mutant enzyme is correctly folded and forms interlocked dimers, 1300fold decrease in activity
D169E
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mutant enzyme is correctly folded and forms interlocked dimers, inactive mutant enzyme
D169S
-
mutant enzyme is correctly folded and forms interlocked dimers, inactive mutant enzyme
G259A
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site-directed mutagenesis
G260A
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site-directed mutagenesis
Q17A
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site-directed mutagenesis
W48F
-
FRC variant
W48Q
-
FRC variant
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
environmental protection
medicine
molecular biology
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