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(2-nitrophenyl)acetate + H2O
2-nitrophenol + acetic acid
-
-
-
?
2-chloro-N-(1-naphthyl)acetamide + H2O
chloroacetate + 1-naphthylamine
-
low activity
-
?
2-methylformanilide + H2O
2-methylaniline + formate
5-hydroxyformyl-DL-kynurenine + H2O
5-hydroxy-DL-kynurenine + formate
-
-
-
?
acetanilide + H2O
acetate + aniline
-
formation of alcohol esters in the presence of alcohols
-
?
formanilide + H2O
formate + aniline
-
poor activity
-
?
N-acetylanthranilic acid + H2O
acetate + anthranilic acid
-
formation of alcohol esters in the presence of alcohols
-
?
N-formyl-2-aminobenzenesulfonic acid + H2O
formate + 2-aminobenzenesulfonic acid
-
low activity
-
?
N-formyl-4-(methylamino)-benzoic acid + H2O
4-methylaminobenzoic acid + formate
N-formyl-DL-kynurenine + H2O
L-kynurenine + formate + N-formyl-D-kynurenine
N-formyl-L-kynurenine + H2O
formate + L-kynurenine
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
N-formyl-m-aminobenzoic acid + H2O
formate + m-aminobenzoic acid
-
very low activity
-
?
N-formyl-o-aminoacetophenone + H2O
formate + o-aminoacetophenone
N-formyl-o-aminonitrobenzene + H2O
formate + o-nitroaniline
-
low activity
-
?
N-formylanthranilic acid + H2O
formate + anthranilic acid
N-formylnitroaniline + H2O
formate + nitroaniline
-
low activity
-
?
N1,Nalpha-diformyl-L-kynurenine + H2O
formate + N-alpha-L-kynurenine
additional information
?
-
-
an enzyme other than the aryl formamidase additionally catalyzes the formation of L-kynurenine in kidney
-
-
?
2-methylformanilide + H2O
2-methylaniline + formate
-
-
-
-
?
2-methylformanilide + H2O
2-methylaniline + formate
-
-
-
-
?
N-formyl-4-(methylamino)-benzoic acid + H2O
4-methylaminobenzoic acid + formate
-
-
-
-
?
N-formyl-4-(methylamino)-benzoic acid + H2O
4-methylaminobenzoic acid + formate
-
-
-
-
?
N-formyl-DL-kynurenine + H2O
L-kynurenine + formate + N-formyl-D-kynurenine
-
mixture of equal amounts of D- and L-kynurenine
N-formyl-D-kynurenine might inhibit activity
?
N-formyl-DL-kynurenine + H2O
L-kynurenine + formate + N-formyl-D-kynurenine
-
mixture of equal amounts of D- and L-kynurenine
N-formyl-D-kynurenine might inhibit activity
?
N-formyl-L-kynurenine + H2O
formate + L-kynurenine
-
-
-
?
N-formyl-L-kynurenine + H2O
formate + L-kynurenine
-
-
-
?
N-formyl-L-kynurenine + H2O
formate + L-kynurenine
-
-
-
?
N-formyl-L-kynurenine + H2O
formate + L-kynurenine
the enzyme forms part of the kynurenine pathway which metabolises tryptophan to anthranilate
-
-
?
N-formyl-L-kynurenine + H2O
formate + L-kynurenine
-
-
-
?
N-formyl-L-kynurenine + H2O
formate + L-kynurenine
the enzyme forms part of the kynurenine pathway which metabolises tryptophan to anthranilate
-
-
?
N-formyl-L-kynurenine + H2O
formate + L-kynurenine
-
-
-
?
N-formyl-L-kynurenine + H2O
formate + L-kynurenine
analysis of enzyme-substrate complex structure using the crystal structure of enzyme-inhibitor PMSF complex and molecular docking, overview
-
-
?
N-formyl-L-kynurenine + H2O
formate + L-kynurenine
-
-
-
?
N-formyl-L-kynurenine + H2O
formate + L-kynurenine
-
-
-
?
N-formyl-L-kynurenine + H2O
formate + L-kynurenine
Gallus gallus White leghorns
-
-
-
?
N-formyl-L-kynurenine + H2O
formate + L-kynurenine
-
-
-
-
?
N-formyl-L-kynurenine + H2O
formate + L-kynurenine
-
-
-
?
N-formyl-L-kynurenine + H2O
formate + L-kynurenine
-
step in tryptophan metabolism and biosynthesis of kynurenine-derived derivatives, e.g. kynurenic acid, quinolinic acid, nicotinamide, NAD+, and NADP+, pathway disruption causes neurotoxicity and immunotoxicity, overview
-
-
?
N-formyl-L-kynurenine + H2O
formate + L-kynurenine
-
-
-
?
N-formyl-L-kynurenine + H2O
formate + L-kynurenine
-
-
-
?
N-formyl-L-kynurenine + H2O
formate + L-kynurenine
-
-
-
-
?
N-formyl-L-kynurenine + H2O
formate + L-kynurenine
-
-
-
?
N-formyl-L-kynurenine + H2O
formate + L-kynurenine
-
-
-
?
N-formyl-L-kynurenine + H2O
formate + L-kynurenine
-
-
-
?
N-formyl-L-kynurenine + H2O
formate + L-kynurenine
-
-
-
?
N-formyl-L-kynurenine + H2O
formate + L-kynurenine
-
-
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
-
-
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
-
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
-
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
involved in the pathway of tryptophan degradation
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
formation of alcohol esters in the presence of alcohols
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
unable to transfer a formyl group directly to tetrahydrofolic acid
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
-
-
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
-
-
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
-
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
-
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
-
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
-
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
-
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
-
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
-
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
-
-
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
-
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
-
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
-
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
-
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
-
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
involved in the pathway of tryptophan degradation
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
-
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
-
-
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
-
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
-
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
-
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
-
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
-
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
-
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
-
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
-
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
-
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
-
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
-
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
preferred substrate, involved in formation of antibiotics and NAD+
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
formamidase II is an integral component of the actinomycin-synthesizing system
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
-
-
?
N-formyl-o-aminoacetophenone + H2O
formate + o-aminoacetophenone
-
-
-
?
N-formyl-o-aminoacetophenone + H2O
formate + o-aminoacetophenone
-
low activity
-
?
N-formyl-o-aminoacetophenone + H2O
formate + o-aminoacetophenone
-
22% of activity compared to N-formyl-L-kynurenine
-
?
N-formyl-o-aminoacetophenone + H2O
formate + o-aminoacetophenone
-
-
-
?
N-formyl-o-aminoacetophenone + H2O
formate + o-aminoacetophenone
-
60% of activity compared to N-formyl-L-kynurenine
-
?
N-formyl-o-aminoacetophenone + H2O
formate + o-aminoacetophenone
-
low activity for both formamidases I and II
-
?
N-formyl-o-aminoacetophenone + H2O
formate + o-aminoacetophenone
-
low activity for both formamidases I and II
-
?
N-formyl-o-aminoacetophenone + H2O
formate + o-aminoacetophenone
-
the only substrate
-
?
N-formylanthranilic acid + H2O
formate + anthranilic acid
-
-
-
?
N-formylanthranilic acid + H2O
formate + anthranilic acid
-
formation of alcohol esters in the presence of alcohols
-
?
N-formylanthranilic acid + H2O
formate + anthranilic acid
-
involvement in anthranilate cycle
-
?
N-formylanthranilic acid + H2O
formate + anthranilic acid
-
involvement in anthranilate cycle
-
?
N-formylanthranilic acid + H2O
formate + anthranilic acid
-
involvement in anthranilate cycle
-
?
N-formylanthranilic acid + H2O
formate + anthranilic acid
-
24% of activity compared to N-formyl-L-kynurenine
-
?
N-formylanthranilic acid + H2O
formate + anthranilic acid
-
involvement in anthranilate cycle
-
?
N-formylanthranilic acid + H2O
formate + anthranilic acid
-
10times slower hydrolysis than for N-formyl-L-kynurenine
-
?
N-formylanthranilic acid + H2O
formate + anthranilic acid
-
low activity
-
?
N-formylanthranilic acid + H2O
formate + anthranilic acid
-
-
-
?
N-formylanthranilic acid + H2O
formate + anthranilic acid
-
13.5% activity compared to N-formyl-L-kynurenine
-
?
N-formylanthranilic acid + H2O
formate + anthranilic acid
-
involvement in anthranilate cycle
-
?
N-formylanthranilic acid + H2O
formate + anthranilic acid
-
involvement in anthranilate cycle
-
?
N-formylanthranilic acid + H2O
formate + anthranilic acid
-
involvement in anthranilate cycle
-
?
N-formylanthranilic acid + H2O
formate + anthranilic acid
-
involvement in anthranilate cycle
-
?
N-formylanthranilic acid + H2O
formate + anthranilic acid
-
involvement in anthranilate cycle
-
?
N1,Nalpha-diformyl-L-kynurenine + H2O
formate + N-alpha-L-kynurenine
-
-
-
?
N1,Nalpha-diformyl-L-kynurenine + H2O
formate + N-alpha-L-kynurenine
-
-
-
?
N1,Nalpha-diformyl-L-kynurenine + H2O
formate + N-alpha-L-kynurenine
-
lower activity for formamidases I and II than for its natural substrate
-
?
N1,Nalpha-diformyl-L-kynurenine + H2O
formate + N-alpha-L-kynurenine
-
lower activity for formamidases I and II than for its natural substrate
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
5-hydroxyformyl-DL-kynurenine + H2O
5-hydroxy-DL-kynurenine + formate
-
-
-
?
N-formyl-L-kynurenine + H2O
formate + L-kynurenine
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
N-formyl-m-aminobenzoic acid + H2O
formate + m-aminobenzoic acid
-
very low activity
-
?
N-formyl-o-aminoacetophenone + H2O
formate + o-aminoacetophenone
N-formyl-o-aminonitrobenzene + H2O
formate + o-nitroaniline
-
low activity
-
?
N-formylanthranilic acid + H2O
formate + anthranilic acid
additional information
?
-
-
an enzyme other than the aryl formamidase additionally catalyzes the formation of L-kynurenine in kidney
-
-
?
N-formyl-L-kynurenine + H2O
formate + L-kynurenine
-
-
-
?
N-formyl-L-kynurenine + H2O
formate + L-kynurenine
-
-
-
?
N-formyl-L-kynurenine + H2O
formate + L-kynurenine
the enzyme forms part of the kynurenine pathway which metabolises tryptophan to anthranilate
-
-
?
N-formyl-L-kynurenine + H2O
formate + L-kynurenine
the enzyme forms part of the kynurenine pathway which metabolises tryptophan to anthranilate
-
-
?
N-formyl-L-kynurenine + H2O
formate + L-kynurenine
-
-
-
?
N-formyl-L-kynurenine + H2O
formate + L-kynurenine
-
-
-
?
N-formyl-L-kynurenine + H2O
formate + L-kynurenine
Gallus gallus White leghorns
-
-
-
?
N-formyl-L-kynurenine + H2O
formate + L-kynurenine
-
-
-
?
N-formyl-L-kynurenine + H2O
formate + L-kynurenine
-
step in tryptophan metabolism and biosynthesis of kynurenine-derived derivatives, e.g. kynurenic acid, quinolinic acid, nicotinamide, NAD+, and NADP+, pathway disruption causes neurotoxicity and immunotoxicity, overview
-
-
?
N-formyl-L-kynurenine + H2O
formate + L-kynurenine
-
-
-
?
N-formyl-L-kynurenine + H2O
formate + L-kynurenine
-
-
-
?
N-formyl-L-kynurenine + H2O
formate + L-kynurenine
-
-
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
-
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
-
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
involved in the pathway of tryptophan degradation
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
formation of alcohol esters in the presence of alcohols
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
unable to transfer a formyl group directly to tetrahydrofolic acid
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
-
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
-
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
-
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
-
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
-
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
-
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
-
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
-
-
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
-
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
-
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
-
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
-
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
-
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
involved in the pathway of tryptophan degradation
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
-
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
-
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
-
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
-
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
-
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
-
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
-
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
-
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
-
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
-
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
-
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
preferred substrate, involved in formation of antibiotics and NAD+
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
formamidase II is an integral component of the actinomycin-synthesizing system
-
?
N-formyl-L-kynurenine + H2O
L-kynurenine + formate
-
-
-
?
N-formyl-o-aminoacetophenone + H2O
formate + o-aminoacetophenone
-
-
-
?
N-formyl-o-aminoacetophenone + H2O
formate + o-aminoacetophenone
-
low activity
-
?
N-formyl-o-aminoacetophenone + H2O
formate + o-aminoacetophenone
-
22% of activity compared to N-formyl-L-kynurenine
-
?
N-formyl-o-aminoacetophenone + H2O
formate + o-aminoacetophenone
-
-
-
?
N-formyl-o-aminoacetophenone + H2O
formate + o-aminoacetophenone
-
60% of activity compared to N-formyl-L-kynurenine
-
?
N-formyl-o-aminoacetophenone + H2O
formate + o-aminoacetophenone
-
low activity for both formamidases I and II
-
?
N-formyl-o-aminoacetophenone + H2O
formate + o-aminoacetophenone
-
low activity for both formamidases I and II
-
?
N-formyl-o-aminoacetophenone + H2O
formate + o-aminoacetophenone
-
the only substrate
-
?
N-formylanthranilic acid + H2O
formate + anthranilic acid
-
-
-
?
N-formylanthranilic acid + H2O
formate + anthranilic acid
-
formation of alcohol esters in the presence of alcohols
-
?
N-formylanthranilic acid + H2O
formate + anthranilic acid
-
involvement in anthranilate cycle
-
?
N-formylanthranilic acid + H2O
formate + anthranilic acid
-
involvement in anthranilate cycle
-
?
N-formylanthranilic acid + H2O
formate + anthranilic acid
-
involvement in anthranilate cycle
-
?
N-formylanthranilic acid + H2O
formate + anthranilic acid
-
24% of activity compared to N-formyl-L-kynurenine
-
?
N-formylanthranilic acid + H2O
formate + anthranilic acid
-
involvement in anthranilate cycle
-
?
N-formylanthranilic acid + H2O
formate + anthranilic acid
-
10times slower hydrolysis than for N-formyl-L-kynurenine
-
?
N-formylanthranilic acid + H2O
formate + anthranilic acid
-
low activity
-
?
N-formylanthranilic acid + H2O
formate + anthranilic acid
-
-
-
?
N-formylanthranilic acid + H2O
formate + anthranilic acid
-
13.5% activity compared to N-formyl-L-kynurenine
-
?
N-formylanthranilic acid + H2O
formate + anthranilic acid
-
involvement in anthranilate cycle
-
?
N-formylanthranilic acid + H2O
formate + anthranilic acid
-
involvement in anthranilate cycle
-
?
N-formylanthranilic acid + H2O
formate + anthranilic acid
-
involvement in anthranilate cycle
-
?
N-formylanthranilic acid + H2O
formate + anthranilic acid
-
involvement in anthranilate cycle
-
?
N-formylanthranilic acid + H2O
formate + anthranilic acid
-
involvement in anthranilate cycle
-
?
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1-pyridine-2-aldoxime 1'-(pyridine-4-aldoxime) dimethyl ether dichloride
-
HS-3, complete inhibition at 0.5 mM
2-pyridine aldoxime
-
31% inhibition at 1 mM
3-hydroxy-DL-kynurenine
-
50% inhibition at 0.2 mM, Ki: 8 mM
3-hydroxykynurenine
-
potent inhibitor
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
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
diethyl dicarbonate
-
90% inhibition at 0.5 mM
diethyl-(4-nitrophenyl)-phosphate
diisopropylfluorophosphate
-
complete inhibition at 0.01 mM
dimethyl sulfoxide
-
inhibition up to 10%, v/v
dioxane
-
inhibition up to 10%, v/v
EDTA
-
0.1 mM, complete inactivation
Fe2+
-
31% inhibition only for formamidase II at 1 mM
hydrosulfite
-
strong inhibition at 1 mM
iodoacetamide
-
slight inhibition at 1 mM for both formamidases I and II
isoleucine
-
19% inhibition at 20 mM
L-tryptophan
-
non-competitive inhibition, Ki: 5.24 mM
methionine
-
20% inhibition at 20 mM
methyl parathion
O,O-dimethyl-O-4-nitrophenyl phosphorothioate
methyl-triphenyl phosphonium bromide
-
-
Mg2+
-
moderate inhibition at 1 mM
N,N-Dimethylformamide
-
inhibition up to 10%, v/v
N-acetylanthranilic acid
-
15% inhibition at 6.7 mM
N-ethyloxycarbonyl-2-ethyloxy-1,2-dihydroquinoline
-
53% inhibition at 1 mM
N-formyl-o-aminotoluene
-
45% inhibition at 6.7 mM
NaCN
-
31% inhibition at 5 mM
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
-
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
phenylmethylsulfonyl fluoride
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
2-aminoacetophenone
active site of the BaKynB-2-aminoacetophenone complex, structure, overview
2-aminoacetophenone
binding structure, overview
2-aminoacetophenone
binding structure, overview
Ag+
-
complete inhibition at 0.1 mM
Ag+
-
complete inhibition at 0.05 mM
Ag+
-
complete inhibition at 0.01 mM
Ag+
-
76% inhibition at 0.1 mM
anthranilic acid
-
9% inhibition at 0.5-1 mM
anthranilic acid
-
29% inhibition at 1-2 mM
anthranilic acid
-
Ki: 1.6 mM
anthranilic acid
-
45% inhibition at 0.5 mM
Co2+
-
moderate inhibition at 1 mM
Co2+
-
moderate inhibition at 1 mM
Co2+
-
moderate inhibitor
Cu2+
-
21% inhibition at 0.1 mM
Cu2+
-
strong inhibition at 0.25 mM, more inhibition for formamidase I than formamidase II
Cu2+
-
moderate inhibition at 1 mM
Cu2+
-
moderate inhibitor
Cu2+
-
31% inhibition at 1 mM
Cu2+
-
complete inhibition at 1 mM
diazinon
-
diazoxon
-
diazoxon
-
highly potent teratogen, Kd: 0.15 mM
dicrotophos
-
potent teratogen, Kd: 3.2 mM
dicrotophos
inhibition due to the teratogen dicrotophos occurred in yolk sac membranes during the period of embryo highest susceptibility to organophosphorus insecticide teratogens; O,O-dimethyl-O-1[E]-methyl-3-(dimethylamino)-3-oxo-1-propenyl phosphate
diethyl-(4-nitrophenyl)-phosphate
-
diethyl-(4-nitrophenyl)-phosphate
-
marked inhibition
Hg2+
-
moderate inhibition at 1 mM
Hg2+
-
57% inhibition at 0.1 mM
Hg2+
-
strong inhibition for both, formamidases I and II
Hg2+
-
strong inhibition at 1 mM
Hg2+
-
20% inhibition at 0.05 mM
Hg2+
-
complete inhibition at 1 mM
Hg2+
-
complete inhibition at 0.05 mM
Hg2+
-
complete inhibition at 1 mM
Hg2+
-
50% inhibition at 0.1 mM
L-kynurenine
-
marked inhibition above 0.1 mM
L-kynurenine
-
competitive inhibition, Ki: 0.26 mM
L-kynurenine
-
potent inhibitor
L-kynurenine
-
15% inhibition at 0.1 mM, Ki: 0.25 mM
L-kynurenine
-
strong non-competitive inhibition
Mn2+
-
strong inhibition at 1 mM
Mn2+
-
strong inhibition at 1 mM
Monocrotophos
-
potent teratogen, Kd: 5.4 mM
N-bromosuccinimide
-
N-bromosuccinimide
-
marked inhibition
Na-bisulfite
-
50% inhibition at 0.18 mM
Na-bisulfite
-
complete inhibition at 4 mM
Na-bisulfite
-
50% inhibition at 0.32 mM
Na-bisulfite
-
strong inhibition 10 mM
Na-Metaarsenite
-
Na-Metaarsenite
-
marked inhibition
Na2S2O4
-
Na2S2O4
-
27% inhibition at 0.04 mM
NaAsO2
-
NaAsO2
-
marked inhibition
NaAsO2
-
25% inhibition at 0.05 mM
NaF
-
42% inhibition at 5 mM
NaF
-
strong inhibition for both formamidases I and II at 1 mM
NaF
-
27% inhibition at 10 mM
NaF
-
at 10 mM: strong inhibition for formamidase I, slight inhibition for formamidase II
NaHSO3
-
50% inhibition at 0.18 mM
NaHSO3
-
complete inhibition at 4 mM
NaHSO3
-
strong inhibition at 1 mM for both formamidases I and II
NaHSO3
-
50% inhibition at 0.32 mM
NaHSO3
-
24% inhibition at 0.04 mM
NaHSO3
-
strong inhibition at at 10 mM
phenylalanine
-
slight inhibition at 20 mM
phenylalanine
-
slight inhibition at 20 mM
phenylmethylsulfonyl fluoride
-
Kd: 3.3 mM
phenylmethylsulfonyl fluoride
-
complete inhibition at 1 mM
phenylmethylsulfonyl fluoride
-
strong inhibition
Urea
-
25% inhibition at 2 M
Urea
-
75% inhibition at 1 M
Zn2+
-
moderate inhibition at 1 mM
Zn2+
-
strong inhibition at 0.1 mM, more for formamidase II than formamidase I
Zn2+
-
strong inhibition at 1 mM
Zn2+
-
complete inhibition of formamidase I at 1 mM, 88% inhibition of formamidase II at 1 mM
additional information
-
no inhibition by PMSF
-
additional information
determination and analysis of organophosphorus insecticides structural requirements to inhibit in ovo chicken embryo yolk sac membrane kynurenine formamidase, inhibition mechanism, plnED50 values, overview. The dominant electrostatic interactions are localized at nitrogen-1, nitrogen-3, nitrogen of 2-amino substituent of the pyrimidinyl of pyrimidinyl phosphorothioates, and the oxygen of crotonamide carbonyl in crotonamide phosphates. Bulkiness of the substituents at carbon-2 and carbon-6 of the pyrimidinyls and/or N-substituents and carbon-3 substituents of crotonamides are the steric structural components that contribute to in ovo inhibition of the enzyme
-
additional information
-
determination and analysis of organophosphorus insecticides structural requirements to inhibit in ovo chicken embryo yolk sac membrane kynurenine formamidase, inhibition mechanism, plnED50 values, overview. The dominant electrostatic interactions are localized at nitrogen-1, nitrogen-3, nitrogen of 2-amino substituent of the pyrimidinyl of pyrimidinyl phosphorothioates, and the oxygen of crotonamide carbonyl in crotonamide phosphates. Bulkiness of the substituents at carbon-2 and carbon-6 of the pyrimidinyls and/or N-substituents and carbon-3 substituents of crotonamides are the steric structural components that contribute to in ovo inhibition of the enzyme
-
additional information
no inhibition by p-chloromercuribenzoate
-
additional information
activity is not affected by Mn2+, Mg2+, Zn2+, Fe2+, Fe3+, ascorbic acid, cysteine, glutathione, p-chloromercuribenzoate, EDTA, KCN, K3Fe(CN)6, Na2S2O6 and sodium formate
-
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physiological function
maintaining or regulating kynurenine metabolism through the molecular and biochemical regulation of the enzyme, overview
evolution
the enzyme belongs to the alpha/beta hydrolase fold family
evolution
the enzyme differs between eukaryotes and prokaryotes
evolution
the enzyme differs between eukaryotes and prokaryotes
evolution
the enzyme differs between eukaryotes and prokaryotes
malfunction
organophosphorus insecticide (OPI) interfer in ovo with the second step of L-tryptophan to NAD+ biosynthesis by inhibiting kynurenine formamidase. Its inhibition due to the teratogen dicrotophos occurs in yolk sac membranes during the period of embryo highest susceptibility to OPI teratogens in contrast to delayed and lower inhibition caused by the nonteratogen methyl parathion. Both OPI affect liver kynurenine formamidase in a similar manner. The onsets of liver enzyme inhibition are delayed by about two days and occur at the time of the reduced embryo susceptibility to teratogens. The early disruption of L-tryptophan metabolism and higher inhibition of kynurenine formamidase in yolk sac membranes may be the factors that determine action of OPI as teratogens in chicken embryos
malfunction
Gallus gallus White leghorns
-
organophosphorus insecticide (OPI) interfer in ovo with the second step of L-tryptophan to NAD+ biosynthesis by inhibiting kynurenine formamidase. Its inhibition due to the teratogen dicrotophos occurs in yolk sac membranes during the period of embryo highest susceptibility to OPI teratogens in contrast to delayed and lower inhibition caused by the nonteratogen methyl parathion. Both OPI affect liver kynurenine formamidase in a similar manner. The onsets of liver enzyme inhibition are delayed by about two days and occur at the time of the reduced embryo susceptibility to teratogens. The early disruption of L-tryptophan metabolism and higher inhibition of kynurenine formamidase in yolk sac membranes may be the factors that determine action of OPI as teratogens in chicken embryos
-
metabolism
second enzyme in the kynurenine pathway of tryptophan metabolism
metabolism
the enzyme is involved in the tryptophan-to-anthranilate pathway
metabolism
the second stage of tryptophan catabolism is catalysed by kynurenine formamidase
metabolism
the second stage of tryptophan catabolism is catalysed by kynurenine formamidase
metabolism
the second stage of tryptophan catabolism is catalysed by kynurenine formamidase
metabolism
the enzyme catalyzes the second step of the biosynthesis of NAD+ from L-tryptophan
metabolism
the enzyme forms part of the kynurenine pathway which metabolises tryptophan to anthranilate. The kynurenine pathway is a critical source of anthranilate and signalling molecules that may regulate Burkholderia pseudomallei virulence
metabolism
the enzyme is involved in the L-tryptophan to NAD+ pathway. Kynurenine formamidase of the Trp to NAD+ metabolism in yolk sac membranes and not in livers is the primary candidate target for organophosphorus insecticide teratogens in NAD-associated teratogenesis in chicken embryos. In ovo treatment of the embryos with organophosphorus insecticide teratogens interferes with the Trp to NAD+ metabolism at the second step of the pathway catalyzed by kynurenine formamidase in both yolk sac membranes and embryo livers. The early disruption of Trp metabolism and higher inhibition of kynurenine formamidase may be the factors that determine action of organophosphorus insecticide teratogens as teratogens in chicken embryos
metabolism
Gallus gallus White leghorns
-
the enzyme catalyzes the second step of the biosynthesis of NAD+ from L-tryptophan
-
metabolism
Gallus gallus White leghorns
-
the enzyme is involved in the L-tryptophan to NAD+ pathway. Kynurenine formamidase of the Trp to NAD+ metabolism in yolk sac membranes and not in livers is the primary candidate target for organophosphorus insecticide teratogens in NAD-associated teratogenesis in chicken embryos. In ovo treatment of the embryos with organophosphorus insecticide teratogens interferes with the Trp to NAD+ metabolism at the second step of the pathway catalyzed by kynurenine formamidase in both yolk sac membranes and embryo livers. The early disruption of Trp metabolism and higher inhibition of kynurenine formamidase may be the factors that determine action of organophosphorus insecticide teratogens as teratogens in chicken embryos
-
metabolism
-
the enzyme forms part of the kynurenine pathway which metabolises tryptophan to anthranilate. The kynurenine pathway is a critical source of anthranilate and signalling molecules that may regulate Burkholderia pseudomallei virulence
-
metabolism
-
the enzyme is involved in the tryptophan-to-anthranilate pathway
-
additional information
active site structure analysis, overview. The enzyme contains a crowded binuclear zinc catalytic site primed to generate a potent nucleophile, the substrate itself may be conformationally restricted to assist binding in the confined space of the active site and for subsequent processing
additional information
active site structure analysis, overview. The enzyme contains a crowded binuclear zinc catalytic site primed to generate a potent nucleophile, the substrate itself may be conformationally restricted to assist binding in the confined space of the active site and for subsequent processing
additional information
active site structure, enzyme ligand binding, and catalytic mechanism, molecular docking study, structure modeling, overview
additional information
-
active site structure, enzyme ligand binding, and catalytic mechanism, molecular docking study, structure modeling, overview
additional information
sequence comparisons. Active site structure analysis, overview. The enzyme contains a crowded binuclear zinc catalytic site primed to generate a potent nucleophile, the substrate itself may be conformationally restricted to assist binding in the confined space of the active site and for subsequent processing
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25000
-
formamidase II, gel filtration
27000
-
formamidase II, gel filtration
28000
-
formamidase II, gel filtration
30500
-
formamidase II, gel filtration
31000
-
formamidase II, gel filtration
34000
-
2 * 34000, formamidase I, SDS-PAGE
34229
x * 34229, sequence calculation
35500
-
1 * 35500, SDS-PAGE
36000
-
formamidase II, gel filtration
36500
-
formamidase II, gel filtration
43000
-
formamidase I, gel filtration
57000
-
formamidase I, gel filtration
58500
-
formamidase I, gel filtration
29000
-
formamidase II, gel filtration
29000
-
formamidase II, gel filtration
29000
-
formamidase II, gel filtration
30000
-
formamidase II, gel filtration
30000
-
formamidase II, gel filtration
30000
-
2 * 30000, SDS-PAGE
40000
2 * 40000, about, recombinant enzyme, SDS-PAGE
40000
2 * 40000, about, recombinant enzyme, SDS-PAGE
40000
2 * 40000, about, recombinant enzyme, SDS-PAGE
54000
-
formamidase I, gel filtration
54000
-
formamidase I, gel filtration
56000
-
formamidase I, gel filtration
56000
-
formamidase I, gel filtration
56000
-
formamidase I, gel filtration
58000
-
formamidase I, gel filtration
58000
-
formamidase I, gel filtration
58000
-
formamidase I, gel filtration
59000
-
gel filtration
59000
-
formamidase I, gel filtration
59000
-
formamidase I, gel filtration
59000
-
formamidase I, gel filtration
59000
-
formamidase I, gel filtration
60000
-
-
60000
-
formamidase I, gel filtration
60000
-
formamidase I, gel filtration
60000
-
formamidase I, gel filtration
80000
about, recombinant enzyme, native PAGE
80000
about, recombinant enzyme, native PAGE
80000
about, recombinant enzyme, native PAGE
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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
-
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
-
-
-
partial
-
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
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
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 techniques
-
to homogeneity, chromatography techniques
-
to homogeneity, chromatography techniques
-
to homogeneity, chromatography techniques, 2 forms
-
to homogeneity, chromatography techniques, 2 forms
-
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Serrano, A.E.; Nagayama, F.
Inhibition studies on liver arylformamidases of rainbow trout and cattle
Comp. Biochem. Physiol. B
99
281-285
1991
Bos taurus, Oncorhynchus mykiss
brenda
Serrano, A.E.; Nagayama, F.
Purification and characterization of liver arylformamidase in rainbow trout and cattle
Comp. Biochem. Physiol. B
98
381-387
1991
Bos taurus, Oncorhynchus mykiss
brenda
Katz, E.; Brown, D.; Hitchcock, M.J.M.
Arylformamidase from Streptomyces parvulus
Methods Enzymol.
142
225-234
1987
Streptomyces parvulus
brenda
Brown, D.; Hitchcock, M.J.M.; Katz, E
Purification and characterization of kynurenine formamidase activities from Streptomyces parvulus
Can. J. Microbiol.
32
465-472
1986
Streptomyces parvulus
brenda
Brown, D.D.; Hitchcock, M.J.M.; Katz, E.
Evidence for a constitutive and inducible form of kynurenine formamidase in an actinomycin-producing strain of Streptomyces parvulus
Arch. Biochem. Biophys.
202
18-22
1980
Streptomyces parvulus
brenda
Seifert, J.; Casida, J.E.
Inhibition and reactivation of chicken kynurenine formamidase: In vitro studies with organophosphates, N-alkylcarbamates, and phenylmethanesulfonyl fluoride
Pestic. Biochem. Physiol.
12
273-279
1979
Gallus gallus
-
brenda
Bode, R.; Birnbaum, D.
Die Formamidase von Hansenula henricii: Isolierung, Charakterisierung und Regulation multipler Formen
Biochem. Physiol. Pflanz.
174
26-38
1979
Ogataea henricii
-
brenda
Bode, R.; Birnbaum, D.
Vorkommen und Verteilung multipler Formen der Formamidase bei verschiedenen Hefen
Z. Allg. Mikrobiol.
19
221-222
1979
Saccharomyces cerevisiae, Meyerozyma guilliermondii, Yarrowia lipolytica, Cyberlindnera jadinii, Cyberlindnera fabianii, Ogataea henricii, Rhodotorula sphaerocarpa, Rhodotorula toruloides, Rhodotorula mucilaginosa
brenda
Menge, U.
Formamidase - Untersuchungen zu Mikroheterogenitt, katalytischen Eigenschaften und Inhibitoren
Hoppe-Seyler's Z. Physiol. Chem.
360
185-196
1979
Rattus sp.
brenda
Moore, G.P.; Sullivan, D.T.
Biochemical and genetic characterization of kynurenine formamidase from Drosophila melanogaster
Biochem. Genet.
16
619-634
1978
Drosophila melanogaster
brenda
Jacobson, K.B.
A new substrate for formylkynurenine formamidase: N'-Nalpha-diformylkynurenine
Arch. Biochem. Biophys.
186
84-88
1978
Neurospora crassa
brenda
Shinohara, R.; Ishiguro, I.
New formamidase having substrate specificity for o-formylaminoacetophenone in pig liver
Biochim. Biophys. Acta
483
409-415
1977
Cavia porcellus, Oryctolagus cuniculus, no activity in Mus musculus, no activity in Rattus sp., Sus scrofa
brenda
Moore, G.P.; Sullivan, D.T.
The characterization of multiple forms of kynurenine formidase in Drosophila melanogaster
Biochim. Biophys. Acta
397
468-477
1975
Bos taurus, Saccharomyces cerevisiae, Gallus gallus, Drosophila melanogaster, Drosophila virilis, Mus musculus, Musca domestica, Lithobates pipiens
brenda
Tsuda, H.; Noguchi, T.; Kido, R.
Formamidase in rat brain
J. Neurochem.
22
679-683
1974
Rattus sp.
brenda
Bailey, C.B.; Wagner, C.
Kynurenine formamidase. Purification and characterization of the adult chicken liver enzyme and immunochemical analyses of the enzyme of developing chicken
J. Biol. Chem.
249
4439-4444
1974
Gallus gallus
brenda
Arndt, R.; Junge, W.; Michelsen, K.; Krisch, K.
Isolation and molecular properties of formamidase from rat liver cytoplasm
Hoppe-Seyler's Z. Physiol. Chem.
354
1583-1590
1973
Rattus sp.
brenda
Shinohara, R.; Ishiguro, I.
The purification and properties of formamidase from rat liver
Biochim. Biophys. Acta
198
324-331
1970
Rattus sp.
brenda
Santti, R.S.
Formamidase in guinea pig liver II. Effect of aliphatic alcohols
Hoppe-Seyler's Z. Physiol. Chem.
350
1279-1285
1969
Cavia porcellus
brenda
Santti, R.; Soini, J.
Kynurenine formamidase and tetrahydrofolic acid
Acta Chem. Scand.
22
3321-3323
1968
Cavia porcellus
brenda
Jakoby, W.B.
Kynurenine fromamidase from Neurospora
J. Biol. Chem.
207
657-663
1954
Neurospora crassa
brenda
Mehler, A.H.; Knox, W.E.
The conversion of tryptophan to kynurenine in liver. II. The enzymatic hydrolysis of formylkynurenine
J. Biol. Chem.
187
431-438
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