Information on EC 3.5.1.9 - arylformamidase

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

EC NUMBER
COMMENTARY hide
3.5.1.9
-
RECOMMENDED NAME
GeneOntology No.
arylformamidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
N-formyl-L-kynurenine + H2O = formate + L-kynurenine
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carboxylic acid amide hydrolysis
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
3-hydroxy-4-methyl-anthranilate biosynthesis I
-
-
3-hydroxy-4-methyl-anthranilate biosynthesis II
-
-
3-hydroxyquinaldate biosynthesis
-
-
Glyoxylate and dicarboxylate metabolism
-
-
L-tryptophan degradation I (via anthranilate)
-
-
L-tryptophan degradation to 2-amino-3-carboxymuconate semialdehyde
-
-
L-tryptophan degradation XI (mammalian, via kynurenine)
-
-
Metabolic pathways
-
-
quinoxaline-2-carboxylate biosynthesis
-
-
tryptophan metabolism
-
-
Tryptophan metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
aryl-formylamine amidohydrolase
Also acts on other aromatic formylamines.
CAS REGISTRY NUMBER
COMMENTARY hide
156229-75-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene kynB
UniProt
Manually annotated by BRENDA team
strain ATCC 14579
-
-
Manually annotated by BRENDA team
gene kynB
UniProt
Manually annotated by BRENDA team
strain CH34
-
-
Manually annotated by BRENDA team
strain CH34
-
-
Manually annotated by BRENDA team
1form, formamidase I
-
-
Manually annotated by BRENDA team
1 form, formamidase I
-
-
Manually annotated by BRENDA team
2 forms, formamidase I and II
-
-
Manually annotated by BRENDA team
Hansenula henricii
2 forms, formamidase I and II
-
-
Manually annotated by BRENDA team
housefly, formamidase I
-
-
Manually annotated by BRENDA team
no activity in Mus musculus
not present in liver
-
-
Manually annotated by BRENDA team
no activity in Rattus sp.
not present in liver
-
-
Manually annotated by BRENDA team
rainbow trout
-
-
Manually annotated by BRENDA team
frog, formamidase II
-
-
Manually annotated by BRENDA team
Rhodosporidium sphaerocarpum
-
-
-
Manually annotated by BRENDA team
Rhodosporidium toruloides
-
-
-
Manually annotated by BRENDA team
gene SCO3644; gene kynB or SCO3644
UniProt
Manually annotated by BRENDA team
gene SCO3644; gene kynB or SCO3644
UniProt
Manually annotated by BRENDA team
formamidase II
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
metabolism
physiological function
maintaining or regulating kynurenine metabolism through the molecular and biochemical regulation of the enzyme, overview
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2-nitrophenyl)acetate + H2O
2-nitrophenol + acetic acid
show the reaction diagram
-
-
-
?
2-chloro-N-(1-naphthyl)acetamide + H2O
chloroacetate + 1-naphthylamine
show the reaction diagram
-
low activity
-
?
2-methylformanilide + H2O
2-methylaniline + formate
show the reaction diagram
5-hydroxyformyl-DL-kynurenine + H2O
5-hydroxy-DL-kynurenine + formate
show the reaction diagram
-
-
-
?
acetanilide + H2O
acetate + aniline
show the reaction diagram
-
formation of alcohol esters in the presence of alcohols
-
?
formanilide + H2O
formate + aniline
show the reaction diagram
-
poor activity
-
?
N-acetylanthranilic acid + H2O
acetate + anthranilic acid
show the reaction diagram
-
formation of alcohol esters in the presence of alcohols
-
?
N-formyl-2aminobenzenesulfonic acid + H2O
formate + 2-aminobenzenesulfonic acid
show the reaction diagram
-
low activity
-
?
N-formyl-4-(methylamino)-benzoic acid + H2O
4-methylaminobenzoic acid + formate
show the reaction diagram
N-formyl-DL-kynurenine + H2O
L-kynurenine + formate + N-formyl-D-kynurenine
show the reaction diagram
N-formyl-L-kynurenine + H2O
formate + L-kynurenine
show the reaction diagram
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
show the reaction diagram
N-formyl-m-aminobenzoic acid + H2O
formate + m-aminobenzoic acid
show the reaction diagram
-
very low activity
-
?
N-formyl-o-aminoacetophenone + H2O
formate + o-aminoacetophenone
show the reaction diagram
N-formyl-o-aminonitrobenzene + H2O
formate + o-nitroaniline
show the reaction diagram
-
low activity
-
?
N-formylanthranilic acid + H2O
formate + anthranilic acid
show the reaction diagram
N-formylnitroaniline + H2O
formate + nitroaniline
show the reaction diagram
-
low activity
-
?
N1,Nalpha-diformyl-L-kynurenine + H2O
formate + N-alpha-L-kynurenine
show the reaction diagram
additional information
?
-
-
an enzyme other than the aryl formamidase additionally catalyzes the formation of L-kynurenine in kidney
-
-
-
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
5-hydroxyformyl-DL-kynurenine + H2O
5-hydroxy-DL-kynurenine + formate
show the reaction diagram
-
-
-
?
N-formyl-L-kynurenine + H2O
formate + L-kynurenine
show the reaction diagram
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
show the reaction diagram
N-formyl-m-aminobenzoic acid + H2O
formate + m-aminobenzoic acid
show the reaction diagram
-
very low activity
-
?
N-formyl-o-aminoacetophenone + H2O
formate + o-aminoacetophenone
show the reaction diagram
N-formyl-o-aminonitrobenzene + H2O
formate + o-nitroaniline
show the reaction diagram
-
low activity
-
?
N-formylanthranilic acid + H2O
formate + anthranilic acid
show the reaction diagram
additional information
?
-
-
an enzyme other than the aryl formamidase additionally catalyzes the formation of L-kynurenine in kidney
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
dependent
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cd2+
active site-bound
Co3+
-
15-20fold activation
Mn2+
-
15-20fold activation
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-pyridine-2-aldoxime 1'-(pyridine-4-aldoxime) dimethyl ether dichloride
-
HS-3, complete inhibition at 0.5 mM
2-aminoacetophenone
2-pyridine aldoxime
-
31% inhibition at 1 mM
3-Hydroxy-DL-kynurenine
-
50% inhibition at 0.2 mM, Ki: 8 mM
3-pyridine aldoxime O-n-propyl ether
-
43% inhibition at 1 mM
3-pyridine aldoxime O-phenyl ether
-
61% inhibition at 1 mM
acetone
-
inhibition up to 10%, v/v
anthranilic acid
arsenate
-
strong inhibition for formamidase I, slight inhibition for formamidase II at 1 mM
ascorbate
-
50% inhibition at 10 mM
Ba2+
-
strong inhibition at 1 mM
bis(4-nitrophenyl)phosphate
-
slight inhibition at 1 mM after 30 min preincubation
bromphenol blue
-
50% inhibition at 0.024 mM after 5 min preincubation
Carbaryl
-
moderately potent teratogen, Kd: 0.085 mM
diazinon
diazoxon
dichlorvos
-
dicrotophos
diethyl dicarbonate
-
90% inhibition at 0.5 mM
diethyl-(4-nitrophenyl)-phosphate
-
marked inhibition
diisopropylfluorophosphate
-
complete inhibition at 0.01 mM
Dimethoate
-
dimethyl sulfoxide
-
inhibition up to 10%, v/v
dioxane
-
inhibition up to 10%, v/v
EDTA
-
0.1 mM, complete inactivation
ethylpirimiphos
-
-
etrimfos
-
-
Fe2+
-
31% inhibition only for formamidase II at 1 mM
hydrosulfite
-
strong inhibition at 1 mM
iodoacetamide
Hansenula henricii
-
slight inhibition at 1 mM for both formamidases I and II
isoleucine
-
19% inhibition at 20 mM
L-kynurenine
L-tryptophan
-
non-competitive inhibition, Ki: 5.24 mM
leptophos
-
-
methamidophos
-
methionine
-
20% inhibition at 20 mM
methyl-triphenyl phosphonium bromide
-
-
methylchlorpyriphos
-
methylparathion
-
methylpirimiphos
-
Mg2+
-
moderate inhibition at 1 mM
Monocrotophos
N,N-Dimethylformamide
-
inhibition up to 10%, v/v
N-acetylanthranilic acid
-
15% inhibition at 6.7 mM
N-bromosuccinimide
-
marked inhibition
N-ethyloxycarbonyl-2-ethyloxy-1,2-dihydroquinoline
-
53% inhibition at 1 mM
N-formyl-o-aminotoluene
-
45% inhibition at 6.7 mM
Na-bisulfite
Na-Metaarsenite
-
marked inhibition
Na2S2O4
-
27% inhibition at 0.04 mM
NaAsO2
NaCN
-
31% inhibition at 5 mM
NaHSO3
NH2OH*HCl
-
14% inhibition at 3 mM
O,O-Diethyl-O-(4-nitrophenyl)phosphate
-
E600, complete inhibition at 1 mM
o-aminobenzamidine
-
62% inhibition at 0.5 mM
p-chloromercuribenzoate
Hansenula henricii
-
strong inhibition at 0.1 mM for both formamidases I and II
p-hydroxymercuribenzoate
-
complete inhibition at 1 mM
p-nitrophenyldiethyl phosphoric acid
-
92% inhibition at 10 mM
-
phenyl saligenin cyclic phosphate
-
Kd: 0.00083 mM
phenylalanine
phenylmethylsulfonyl fluoride
Phosphamidon
-
PMSF
binding structure analysis, overview
Salicyl aldoxime
-
71% inhibition at 1 mM
tetraethyl diphosphate
-
Kd: 67 mM
tetraheptylammonium bromide
-
94% inhibition at 2.5 mM
tetrahexylammonium bromide
-
56% inhibition at 5 mM
tetraoctylammoniumbromide
-
94% inhibition at 2.5 mM
tetraphenyl phosphonium bromide
-
22% inhibition at 5 mM
threonine
-
19% inhibition at 20 mM
trimethyl-n-decylammonium bromide
-
65% inhibition at 5 mM
trimethyl-n-decylammonium chloride
-
65% inhibition at 5 mM
trimethyl-n-hexadecylammonium bromide
-
100% inhibition at 5 mM
trimethylhexadecylammonium chloride
-
100% inhibition at 5 mM
trimethylphenylammonium bromide
-
20% inhibition at 5 mM
trimethylphenylammonium chloride
-
20% inhibition at 5 mM
valine
-
slight inhibition at 20 mM
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
arginine
-
30% activation at 20 mM
ascorbate
-
57% activation at 100 mM
butanol
-
activation e.g. between 0.75-2.5%, v/v, depending on substrate
ethanol
-
activation e.g. between 2.5-12%, v/v, depending on substrate
L-tryptophan
-
activation from 5-20 mM
lysine
-
30% activation at 20 mM
methanol
-
optimal activation e.g. between 5-15%, v/v, depending on substrate
methionine
-
20% activation at 20 mM
o-aminophenol
-
activation at 0.2 mM
Propanol
-
activation e.g. between 1.5-5%, v/v, depending on substrate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1
2-Chloro-N-(1-naphthyl)acetamide
-
-
0.4
5-hydroxy-DL-kynurenine
-
-
0.45
N-formyl-DL-kynurenine
-
-
0.05 - 5
N-formyl-L-kynurenine
7.7
N-formyl-m-aminobenzoic acid
-
-
2.8 - 8.1
N-formyl-o-aminoacetophenone
2.5
N-formyl-o-aminonitrobenzene
-
-
0.21 - 3.3
N-formylanthranilic acid
0.39
N1,Nalpha-diformyl-L-kynurenine
-
-
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
26.4 - 161
N-formyl-L-kynurenine
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
77.1 - 126.4
N-formyl-L-kynurenine
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8
3-Hydroxy-DL-kynurenine
-
-
10
ascorbate
-
-
0.024
bromphenol blue
-
after 5 min preincubation
0.1
Hg2+
-
-
0.25
L-kynurenine
-
-
5.24
L-tryptophan
-
non-competitive inhibition
0.18 - 0.32
Na-bisulfite
0.32
NaHSO3
-
-
additional information
additional information
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00002
-
liver knockout mutant enzyme
0.00087
-
kidney knockout mutant enzyme
0.0038
-
kidney heterozygous mutant enzyme
0.0067
-
kidney wild-type enzyme
0.0083
-
liver heterozygous mutant enzyme
0.0156
-
liver wild-type enzyme
0.26
-
formamidase I
0.33
-
-
0.48
-
formamidase II
0.59
Hansenula henricii
-
-
0.8
-
-
3
pH 7.4, temperature not specified in the publication, purified recombinant His6-tagged enzyme
3.5
-
1 mM N-formyl-L-kynurenine, pH 7.4, 37C
4.7
-
1 mM N-formyl-L-kynurenine, pH 7.4, 37C
5.9
-
1 mM N-formyl-L-kynurenine, pH 7.4, 37C
8.33
-
formamidase I
22.8
-
-
26.8
-
formamidase II
42
purified recombinant wild-type enzyme
303
-
-
346
-
-
425
-
-
additional information
-
determination of kynurenine pathway metabolites concentrations in plasma of wild-type and mutant mice
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 7
Hansenula henricii
-
formamidase II
5.5 - 8.5
-
-
6 - 9
-
-
6.5 - 8
-
formamidase II
6.7 - 7.8
-
formamidase I
7 - 8
Hansenula henricii
-
formamidase I
7 - 8
-
formamidase I
7
-
formamidase II
7.3 - 7.8
-
-
8.5
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 9
-
optimum range
6 - 8.5
-
active within
6.2 - 9.3
-
high activity within
6.5 - 7.5
-
high activity within
6.5 - 11
-
high activity within
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
formamidase II
50
-
formamidase I
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35 - 60
-
activity constant within
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25000
-
formamidase II, gel filtration
27000
-
formamidase II, gel filtration
28000
Hansenula henricii
-
formamidase II, gel filtration
30500
-
formamidase II, gel filtration
31000
-
formamidase II, gel filtration
31700
-
gel filtration
34700
-
gel filtration
34900
-
SDS-PAGE
36000
-
formamidase II, gel filtration
36500
-
formamidase II, gel filtration
42600
-
gel filtration
43000
-
formamidase I, gel filtration
57000
Rhodosporidium toruloides
-
formamidase I, gel filtration
58500
-
formamidase I, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 34229, sequence calculation
monomer
-
1 * 35500, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified detagged recombinant enzyme, hanging drop vapour diffusion method, mixing of 4.0 mg/ml protein in 20 mM Tris-HCl, pH 7.4, and 200 mM NaCl, and 8 mM kynurenine, in a 1.1 ratio with reservoir solution containing 100 mM Tris-HCl, pH 8.5, 150 mM MgCl2, 30% w/v PEG 4000 and 1.5% v/v dioxane, final volume 0.002-0.004 ml, 20C, 5 days, X-ray diffraction structure determination and analysis at 1.95 A resolution
purified detagged recombinant enzyme, sitting drop vapour diffusion method, mixing of 7.5 mg/ml protein in 25 mM Tris-HCl, pH 7.5, and 100 mM NaCl, and kynurenine, in a 1.1 ratio with reservoir solution containing 10-16% w/v PEG 3350, 5 mM CoCl2, 5 mM CdCl2, 5 mM MgCl2 and 5 mM NiCl2, final volume 0.002-0.004 ml, 5 days at room temperature, X-ray diffraction structure determination and analysis at 1.60 A resolution
enzyme in complex with inhibitor PMSF, X-ray diffraction structure determination and analysis, molecular replacement using structure PDB ID 2PBL
purified detagged recombinant enzyme, sitting drop vapour diffusion method, mixing of 7.5 mg/ml protein in 25 mM Tris-HCl, pH 7.5, and 100 mM NaCl, and kynurenine, in a 1.1 ratio with reservoir solution containing 0.1M HEPES, pH 7.5, 20% w/v PEG 4000 and 10% v/v propan-2-ol, final volume 0.002-0.004 ml, 5 days at room temperature, X-ray diffraction structure determination and analysis at 2.37 A resolution, molecular replacement
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
activity of formamidase II declines sharp at higher temperatures
45
Hansenula henricii
-
50% activity after 40 min for formamidase I, complete inactivation for formamidase II
56
-
30% inactivation after 2 min
65
-
inactivation in 35 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
formamidase I more heat-stable than formamidase II
-
ionic strength affects enzyme activity
sensitive to repeated freezing and thawing
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0-2C, 3 weeks
-
4C, 60% of activity recovered after seven months
-
4C, fully active within seven months
-
5C, no inactivation during prolonged storage
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme from liver cytosol, recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli by anion exchange chromatography, gel filtration, and nickel affinity chromatography, to high purity, recombinant wild-type enzyme 90fold
near homogeneity, chromatography techniques
-
near homogeneity, chromatography techniques, isoelectric focusing
-
partial
recombinant enzyme from Escherichia coli by affinity chromatography, ion exchange chromatography, and gel filtration
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3)pLysS by nickel affinity chromatography and gel filtration
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3)pLysS by nickel affinity chromatography, cleavage of the tag by tobacco etch virus, followed by another step of nickel affinity chromatography, gel filtration of the eluate
to homogeneity, chromatography steps
-
to homogeneity, chromatography steps, isoelectric focusing
-
to homogeneity, chromatography techniques
to homogeneity, chromatography techniques, 2 forms
to homogeneity, chromatography techniques, preparative disc gel electrophoresis
-
to homogeneity: formamidase I, partial: formamidase II, chromatography techniques
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and anlysis, expression of His6-tagged wild-type and mutant enzymes in Escherichia coli strain DH10B
expressed in Escherichia coli
expression of putative kynBAU in Escherichia coli
-
gene CG9542, cloning from larvae, DNA and amino acid sequence determination and analysis, recombinant expression in Escherichia coli
gene kynB or SCO3644, gene expression analysis, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)pLysS
gene kynB, recombinant expression of the His6-tagged enzyme in Escherichia coli K12 strain BL21(DE3)pLysS, codon optimization
gene kynB, sequence comparison, recombinant expression of the His6-tagged enzyme in Escherichia coli K12 strain BL21(DE3)pLysS, codon optimization
kynB gene, expression in Escherichia coli as N-terminal His6 tag fusions
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
kynurenine formamidase shows enhanced expression in the forewing band of Heliconius melpomene during forewing ommochrome pigmentation with highest levels of expression in LM wings, and specifically in the distal wing region. Kynurenine formamidase is also upregulated in the early melanin band region
-
tryptophan positively affects kynB transcription
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D247A
site-directed mutagenesis, inactive mutant
H279A
site-directed mutagenesis, inactive mutant
S162A
site-directed mutagenesis, inactive mutant
additional information
-
construction of heterozygous and knockout enzyme-deficient mutants, inactivation through the removal of a shared bidirectional promoter region regulating expression of the Afmid gene and the thymidine kinase gene, phenotype overview, Afmid knockout mice show 13% residual enzyme activity in kidney due to a distinct enzyme activity
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
degradation
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