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Literature summary extracted from

  • Han, Q.; Robinson, H.; Li, J.
    Biochemical identification and crystal structure of kynurenine formamidase from Drosophila melanogaster (2012), Biochem. J., 446, 253-260.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.1.9 gene CG9542, cloning from larvae, DNA and amino acid sequence determination and analysis, recombinant expression in Escherichia coli Drosophila melanogaster

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.5.1.9 enzyme in complex with inhibitor PMSF, X-ray diffraction structure determination and analysis, molecular replacement using structure PDB ID 2PBL Drosophila melanogaster

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.5.1.9 diazinon
-
 Drosophila melanogaster
3.5.1.9 diazoxon
-
 Drosophila melanogaster
3.5.1.9 PMSF binding structure analysis, overview Drosophila melanogaster

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.1.9 0.32
-
 N-formyl-L-kynurenine pH 7.4, 22°C, recombinant enzyme Drosophila melanogaster

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.1.9 N-formyl-L-kynurenine + H2O Drosophila melanogaster
-
 formate + L-kynurenine
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.9 Drosophila melanogaster Q9VMC9 gene CG9542
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.1.9 recombinant enzyme from Escherichia coli by affinity chromatography, ion exchange chromatography, and gel filtration Drosophila melanogaster

Reaction

EC Number Reaction Comment Organism Reaction ID
3.5.1.9 N-formyl-L-kynurenine + H2O = formate + L-kynurenine via tetrahedral intermediate, enzyme structure and catalytic mechanism, overview Drosophila melanogaster
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.9 N-formyl-L-kynurenine + H2O
-
 Drosophila melanogaster formate + L-kynurenine
-
 ?
3.5.1.9 N-formyl-L-kynurenine + H2O analysis of enzyme-substrate complex structure using the crystal structure of enzyme-inhibitor PMSF complex and molecular docking, overview Drosophila melanogaster formate + L-kynurenine
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.5.1.9 formylkynurenine formamidase
-
 Drosophila melanogaster
3.5.1.9 KFase
-
 Drosophila melanogaster
3.5.1.9 kynurenine formamidase
-
 Drosophila melanogaster

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.5.1.9 22
-
 assay at Drosophila melanogaster

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.5.1.9 26.4
-
 N-formyl-L-kynurenine pH 7.4, 22°C, recombinant enzyme Drosophila melanogaster

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.1.9 7.4
-
 assay at Drosophila melanogaster

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.5.1.9 additional information
-
 additional information inhibition kinetics, overview Drosophila melanogaster

pI Value

EC Number Organism Comment pI Value Maximum pI Value
3.5.1.9 Drosophila melanogaster spectral changes do not lead to an exact isosbestic point, which might be due to the formation of intermediates or an initial protein conformation change caused by addition of the substrate
-
 additional information

General Information

EC Number General Information Comment Organism
3.5.1.9 evolution the enzyme belongs to the alpha/beta hydrolase fold family Drosophila melanogaster
3.5.1.9 metabolism second enzyme in the kynurenine pathway of tryptophan metabolism Drosophila melanogaster
3.5.1.9 additional information active site structure, enzyme ligand binding, and catalytic mechanism, molecular docking study, structure modeling, overview Drosophila melanogaster
3.5.1.9 physiological function maintaining or regulating kynurenine metabolism through the molecular and biochemical regulation of the enzyme, overview Drosophila melanogaster

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.5.1.9 82.5
-
 N-formyl-L-kynurenine pH 7.4, 22°C, recombinant enzyme Drosophila melanogaster