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Information on EC 3.5.1.9 - arylformamidase and Organism(s) Mus musculus and UniProt Accession Q8K4H1

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EC Tree
     3 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.1 In linear amides
                3.5.1.9 arylformamidase
IUBMB Comments
Also acts on other aromatic formylamines.
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This record set is specific for:
Mus musculus
UNIPROT: Q8K4H1
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Word Map
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
kynurenine formamidase, afmid, formylase, kfase, formamidase i, formamidase ii, arylformamidase, formylkynurenine formamidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
AFMID
-
-
formamidase I
-
-
-
-
formamidase II
-
-
-
-
formylase
-
-
-
-
formylkynureninase
-
-
-
-
formylkynurenine formamidase
-
-
-
-
kynurenine formamidase
-
-
kynurine formamidase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
N-formyl-L-kynurenine + H2O = formate + L-kynurenine
show the reaction diagram
the catalytic triad is formed by residues Ser162, Asp247, and His279
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carboxylic acid amide hydrolysis
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
aryl-formylamine amidohydrolase
Also acts on other aromatic formylamines.
CAS REGISTRY NUMBER
COMMENTARY hide
156229-75-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
N-formyl-L-kynurenine + H2O
formate + L-kynurenine
show the reaction diagram
-
-
-
?
N-formyl-L-kynurenine + H2O
formate + 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 SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
N-formyl-L-kynurenine + H2O
formate + L-kynurenine
show the reaction diagram
-
-
-
?
N-formyl-L-kynurenine + H2O
formate + L-kynurenine
show the reaction diagram
-
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
-
-
?
additional information
?
-
-
an enzyme other than the aryl formamidase additionally catalyzes the formation of L-kynurenine in kidney
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.18 - 0.19
N-formyl-L-kynurenine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
42
purified recombinant wild-type enzyme
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
additional information
-
determination of kynurenine pathway metabolites concentrations in plasma of wild-type and mutant mice
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
assay at
7.4
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
KFA_MOUSE
305
0
34229
Swiss-Prot
other Location (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
34229
x * 34229, sequence calculation
36000
-
formamidase II, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 34229, sequence calculation
PROTEIN VARIANTS
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
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
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
Dobrovolsky, V.N.; Bowyer, J.F.; Pabarcus, M.K.; Heflich, R.H.; Williams, L.D.; Doerge, D.R.; Arvidsson, B.; Bergquist, J.; Casida, J.E.
Effect of arylformamidase (kynurenine formamidase) gene inactivation in mice on enzymatic activity, kynurenine pathway metabolites and phenotype
Biochim. Biophys. Acta
1724
163-172
2005
Mus musculus
Manually annotated by BRENDA team
Pabarcus, M.K.; Casida, J.E.
Cloning, expression, and catalytic triad of recombinant arylformamidase
Protein Expr. Purif.
44
39-44
2005
Mus musculus (Q8K4H1), Mus musculus
Manually annotated by BRENDA team