3.5.1.9: arylformamidase
This is an abbreviated version!
For detailed information about arylformamidase, go to the full flat file.
Word Map on EC 3.5.1.9
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3.5.1.9
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organophosphorus
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l-tryptophan
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formylation
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teratogen
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n-formyl-l-kynurenine
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teratogenesis
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methylcarbamate
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l-kynurenine
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diazinon
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parvulus
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pyrimidinyls
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kynurenic
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xanthurenic
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triesters
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degradation
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formyltransferase
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crotonamide
- 3.5.1.9
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organophosphorus
- l-tryptophan
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formylation
-
teratogen
- n-formyl-l-kynurenine
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teratogenesis
- methylcarbamate
- l-kynurenine
- diazinon
- parvulus
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pyrimidinyls
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kynurenic
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xanthurenic
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triesters
- degradation
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formyltransferase
- crotonamide
Reaction
Synonyms
AFMID, Bna7p, FKF, formamidase I, formamidase II, formyl kynurenine formamidase, formylase, formylkynureninase, formylkynurenine formamidase, KFA, KFase, KynB, kynurenine formamidase, kynurine formamidase
ECTree
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General Information on EC 3.5.1.9 - arylformamidase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
malfunction
metabolism
physiological function
maintaining or regulating kynurenine metabolism through the molecular and biochemical regulation of the enzyme, overview
additional information
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
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
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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
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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
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the enzyme catalyzes the second step of the biosynthesis of NAD+ from L-tryptophan
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metabolism
Gallus gallus White leghorns
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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
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metabolism
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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
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metabolism
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the enzyme is involved in the tryptophan-to-anthranilate pathway
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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
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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
