Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.5.1.9 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)

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

Crystallization (Commentary)

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

Inhibitors

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

KM Value [mM]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Drosophila melanogaster Q9VMC9 gene CG9542
-

Purification (Commentary)

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

Reaction

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N-formyl-L-kynurenine + H2O
-
Drosophila melanogaster formate + L-kynurenine
-
?
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

Synonyms Comment Organism
formylkynurenine formamidase
-
Drosophila melanogaster
KFase
-
Drosophila melanogaster
kynurenine formamidase
-
Drosophila melanogaster

Temperature Optimum [°C]

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

Turnover Number [1/s]

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

pH Optimum

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

Ki Value [mM]

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

pI Value

Organism Comment pI Value Maximum pI Value
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

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

kcat/KM [mM/s]

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