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Enzyme Nomenclature
Information on EC 3.7.1.3 - kynureninase
for references in articles please use BRENDA:EC3.7.1.3
Word Map on EC 3.7.1.3
- 3.7.1.3
-
3-hydroxyanthranilic
- medicine
-
quinolinic
- 3-hydroxykynurenine
-
anthranilic
-
kynurenic
- l-tryptophan
- indoleamine
-
3-monooxygenase
-
ido
-
3,4-dioxygenase
-
xanthurenic
-
3-hydroxylase
- aminocarboxymuconate-semialdehyde
-
quin
-
pyrrolase
-
kynurenine-3-hydroxylase
- indoleamine-2,3-dioxygenase
- marginalis
-
b6-deficient
- synthesis
- drug development
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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EC NUMBER 
COMMENTARY 
3.7.1.3
-
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RECOMMENDED NAME
GeneOntology No.
kynureninase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-kynurenine + H2O = anthranilate + L-alanine
aldol and retro-aldol reactions; A pyridoxal-phosphate protein.; a pyridoxal-phosphate protein. Also acts on 3'-hydroxykynurenine and some other (3-acrylcarbonyl)-alanines, hydrolytic beta,gamma-cleavage of aryl-substituted gamma-keto-alpha-amino acids
-
-
-
L-kynurenine + H2O = anthranilate + L-alanine
catalytic reaction mechanism via several intermediates, e.g. external aldimine, quinonoid, ketimine, Gem-diolate, and enamine
-
L-kynurenine + H2O = anthranilate + L-alanine
catalytic reaction mechanism via several intermediates, e.g. external aldimine, quinonoid, ketimine, Gem-diolate, and enamine
-
L-kynurenine + H2O = anthranilate + L-alanine
the proposed mechanism of the retro-Claisen reaction requires extensive acid/base catalysis, the phosphate of pyridoxal 5'-phosphate is an acid/base catalyst in the mechanism of Pseudomonas fluorescens kynureninase, Tyr226 hydrogen bonds to the phosphate of the pyridoxal 5'-phosphate cofactor. Tyr226 mediates proton transfer between the substrate and the phosphate, which accelerates formation of external aldimine and gem-diol intermediates, catalytic reaction mechanism via several intermediates, e.g. external aldimine, quinonoid, ketimine, Gem-diolate, and enamine, overview
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of C-C bond
hydrolysis of C-C bond
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
L-kynurenine hydrolase
A pyridoxal-phosphate protein. Also acts on 3'-hydroxy-L-kynurenine and some other (3-arylcarbonyl)-alanines.
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CAS REGISTRY NUMBER
COMMENTARY
9024-78-6
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
289260, 289268, 289271, 289277, 289278, 289280, 289281, 289282, 289287, 34546, 657495, 658345, 673094, 673130, 719066
-
-
male normolipidemic and diet-induced hyperlipidemic New Zealand rabbits; male Watanabe heritable hyperlipidemic rabbits
-
-
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
additional information
-
modeling of 3,5-dibromo-L-kynurenine in the active site of the human enzyme
metabolism
-
the enzyme is a key enzyme in the kynurenine pathway of tryptophan catabolism in both bacteria and animals, and catalyzes the unique beta,gamma-cleavage of aryl substituted gamma-keto-alpha-amino acids
metabolism
-
the enzyme is a key enzyme in the kynurenine pathway of tryptophan catabolism in both bacteria and animals, and catalyzes the unique beta,gamma-cleavage of aryl substituted gamma-keto-alpha-amino acids
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2S)-2-amino-4-oxo-4-phenylbutanoic acid + H2O
benzoate + L-alanine
-
the rate-determining step is Cbeta-Cgamma bond cleavage
-
-
?
(4R)-5-bromodihydro-L-kynurenine + H2O
? + L-alanine
-
slow substrate, no activity with (4S)-5-bromodihydro-L-kynurenine
-
-
?
(alphaS,4R)-dihydrokynurenine + H2O
?
-
the (alphaS,4R) diastereomer is a slow substrate for a retro-aldol reaction, and the (alphaS,4S) isomer is a potent competitive inhibitor, proposed mechanism for reaction of dihydrokynurenine
-
-
?
2-fluorobenzoyl-DL-alanine + H2O
2-fluorobenzoate + beta-alanine
-
-
-
-
?
3-hydroxy-DL-kynurenine + H2O
3-hydroxyanthranilate + DL-alanine
-
-
-
?
4-fluoro-L-kynurenine + H2O
4-fluoroanthranilate + L-alanine
-
-
-
?
5-fluoro-L-kynurenine + H2O
5-fluoroanthranilate + L-alanine
-
-
-
?
5-hydroxy-L-kynurenine + H2O
5-hydroxyanthranilate + L-alanine
-
-
-
?
5-methyl-L-kynurenine + H2O
5-methylanthranilate + L-alanine
-
-
-
?
beta-(4-chlorobenzoyl)-DL-alanine + H2O
4-chlorobenzoate + beta-alanine
-
-
-
-
?
beta-(4-methylbenzoyl)-DL-alanine + H2O
4-methylbenzoate + beta-alanine
-
-
-
-
?
beta-(4-trifluoromethylbenzoyl)-DL-alanine + H2O
4-trifluoromethylbenzoate + beta-alanine
-
-
-
-
?
gamma-(o-aminophenyl)-L-homoserine + H2O
L-alanine + o-aminobenzaldehyde
-
-
-
?
L-kynurenine + benzaldehyde
(2S,4R)-2-amino-4-hydroxy-4-phenylbutanoic acid + ?
-
-
-
?
O-benzoyl-L-serine + H2O
benzoate + pyruvate + ammonium
-
O-benzoyl-L-serine is an alternate substrate for kynureninase, which undergoes a normal beta-elimination reaction, proposed mechanism for reaction of O-benzoyl-L-serine, overview
-
-
?
(4R)-dihydro-L-kynurenine + H2O
2-aminobenzaldehyde + L-alanine
-
-
-
?
(4R)-dihydro-L-kynurenine + H2O
2-aminobenzaldehyde + L-alanine
-
-
-
-
?
3,5-dibromo-L-kynurenine + H2O
3,5-dibromoanthranilate + DL-kynurenine
-
-
-
-
?
3,5-dibromo-L-kynurenine + H2O
3,5-dibromoanthranilate + DL-kynurenine
-
-
-
?
3-bromo-L-kynurenine + H2O
3-bromoanthranilate + L-alanine
-
-
-
?
3-chloro-DL-kynurenine + H2O
3-chloroanthranilate + DL-alanine
-
-
-
?
3-fluoro-DL-kynurenine + H2O
3-fluoroanthranilate + DL-alanine
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-Ala
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-Ala
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-Ala
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-Ala
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-Ala
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-Ala
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-Ala
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-Ala
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-Ala
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-Ala
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-Ala
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-Ala
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-Ala
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-Ala
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-Ala
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-Ala
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-alanine
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-alanine
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-alanine
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-alanine
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-alanine
-
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-alanine
-
preferred substrate
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-alanine
-
biosynthesis of NAD+
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-alanine
-
L-tryptophan metabolism, biosynthesis of nicotinamide nucleotides
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-alanine
-
the hydroxyl group at the 3-position thus appears to be an important recognition element
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-alanine
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-alanine
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-alanine
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-alanine
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-alanine
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-alanine
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-alanine
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-alanine
-
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-alanine
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-alanine
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-alanine
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-alanine
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-alanine
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-alanine
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-alanine
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-alanine
-
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-alanine
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-alanine
-
biosynthesis of NAD+
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-alanine
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-alanine
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-alanine
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-alanine
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-alanine
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-alanine
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-alanine
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-alanine
-
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-alanine
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-alanine
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-alanine
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-alanine
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-alanine
-
-
-
?
3-methyl-DL-kynurenine + H2O
3-methylanthranilate + DL-alanine
-
-
-
?
5-bromo-3-chloro-DL-kynurenine + H2O
5-bromo-3-chloroanthranilate + DL-alanine
-
-
-
-
?
5-bromo-3-chloro-DL-kynurenine + H2O
5-bromo-3-chloroanthranilate + DL-alanine
-
-
-
?
5-bromo-L-kynurenine + H2O
5-bromoanthranilate + L-alanine
-
-
-
?
5-chloro-L-kynurenine + H2O
5-chloroanthranilate + L-alanine
-
-
-
?
beta-benzoyl-L-alanine + H2O
benzoate + L-alanine
-
good substrate
-
-
?
L-alanine + pyridoxal 5'-phosphate
pyruvate + pyridoxamine 5'-phosphate
-
-
-
?
L-alanine + pyridoxal 5'-phosphate
pyruvate + pyridoxamine 5'-phosphate
-
-
-
?
L-alanine + pyridoxal 5'-phosphate
pyruvate + pyridoxamine 5'-phosphate
-
-
-
?
L-kynurenine + H2O
anthranilate + L-alanine
-
the enzyme is involved in the catabolic pathway of L-tryptophan degradation, overview
-
-
?
L-kynurenine + H2O
anthranilate + L-alanine
-
L-tryptophan metabolism
-
-
?
L-kynurenine + H2O
anthranilate + L-alanine
-
-
-
-
?
L-kynurenine + H2O
anthranilate + L-alanine
L-tryptophan metabolism
-
-
?
L-kynurenine + H2O
anthranilate + L-alanine
-
L-tryptophan metabolism
-
-
?
L-kynurenine + H2O
anthranilate + L-alanine
-
the rate-determining step is to be deprotonation of the pyruvate-ketimine intermediate
-
-
?
L-kynurenine + H2O
anthranilate + L-alanine
-
the enzyme catalyzes the hydrolytic Cbeta-Cgamma cleavage of L-kynurenine to alanine and anthranilic acid catalyzing a retro-Claisen reaction
-
-
?
L-kynurenine + H2O
anthranilate + L-alanine
-
L-tryptophan metabolism
-
-
?
N-formyl-L-kynurenine + H2O
N-formylanthranilate + L-alanine
-
-
-
?
N-formyl-L-kynurenine + H2O
N-formylanthranilate + L-alanine
-
-
-
?
N-formyl-L-kynurenine + H2O
N-formylanthranilate + L-alanine
-
-
-
?
N-formyl-L-kynurenine + H2O
N-formylanthranilate + L-alanine
-
-
-
?
N-formyl-L-kynurenine + H2O
N-formylanthranilate + L-alanine
-
-
-
?
N-formyl-L-kynurenine + H2O
N-formylanthranilate + L-alanine
-
-
-
?
N-formyl-L-kynurenine + H2O
N-formylanthranilate + L-alanine
-
-
-
?
additional information
?
-
-
for the human enzyme, 3- and 5-substituted kynurenines have kcat and kcat/Km values higher than L-kynurenine, but less than that of the physiological substrate, 3-hydroxykynurenine. 3,5-Dibromo- and 5-bromo-3-chlorokynurenine have kcat and kcat/Km values close to that of 3-hydroxykynurenine with human kynureninase. The effects of the 3-halo substituents on the reactivity with human kynureninase may be due to electronic effects and/or halogen bonding. 5-Bromo and 5-chloro-L-kynurenine are good substrates the human enzyme, indicating that the enzyme has space for substituents in the active site near C-5. The increased activity of the 5-halokynurenines may be due to van der Waals contacts or hydrophobic effects. The mammalian kynureninase cleaves 3-hydroxy-L-kynurenine more rapidly than L-kynurenine, substrate synthesis and specificity, overview
-
-
-
additional information
?
-
for the bacterial enzyme, 3-methyl-, 3-halo- and 3,5-dihalokynurenines are much poorer substrates, while 3-fluoro, 5-bromo, and 5-chlorokynurenine have kcat and kcat/Km values comparable to that of its physiological substrate, L-kynurenine. 5-Bromo and 5-chloro-L-kynurenine are good substrates for the bacterial enzyme, indicating that the enzyme has space for substituents in the active site near C-5. The increased activity of the 5-halokynurenines may be due to van der Waals contacts or hydrophobic effects. The bacterial kynureninase cleaves L-kynurenine more rapidly than 3-hydroxy-L-kynurenine, substrate synthesis and specificity, overview
-
-
-
additional information
?
-
-
for the bacterial enzyme, 3-methyl-, 3-halo- and 3,5-dihalokynurenines are much poorer substrates, while 3-fluoro, 5-bromo, and 5-chlorokynurenine have kcat and kcat/Km values comparable to that of its physiological substrate, L-kynurenine. 5-Bromo and 5-chloro-L-kynurenine are good substrates for the bacterial enzyme, indicating that the enzyme has space for substituents in the active site near C-5. The increased activity of the 5-halokynurenines may be due to van der Waals contacts or hydrophobic effects. The bacterial kynureninase cleaves L-kynurenine more rapidly than 3-hydroxy-L-kynurenine, substrate synthesis and specificity, overview
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5-hydroxy-L-kynurenine + H2O
5-hydroxyanthranilate + L-alanine
-
-
-
?
5-methyl-L-kynurenine + H2O
5-methylanthranilate + L-alanine
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-Ala
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-Ala
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-Ala
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-Ala
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-Ala
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-Ala
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-Ala
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-Ala
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-Ala
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-Ala
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-Ala
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-Ala
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-Ala
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-Ala
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-Ala
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-Ala
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-alanine
-
biosynthesis of NAD+
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-alanine
-
L-tryptophan metabolism, biosynthesis of nicotinamide nucleotides
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-alanine
-
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-alanine
-
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-alanine
-
biosynthesis of NAD+
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-alanine
-
-
-
-
?
L-alanine + pyridoxal 5'-phosphate
pyruvate + pyridoxamine 5'-phosphate
-
-
-
?
L-alanine + pyridoxal 5'-phosphate
pyruvate + pyridoxamine 5'-phosphate
-
-
-
?
L-alanine + pyridoxal 5'-phosphate
pyruvate + pyridoxamine 5'-phosphate
-
-
-
?
L-kynurenine + H2O
anthranilate + L-alanine
-
the enzyme is involved in the catabolic pathway of L-tryptophan degradation, overview
-
-
?
L-kynurenine + H2O
anthranilate + L-alanine
-
L-tryptophan metabolism
-
-
?
L-kynurenine + H2O
anthranilate + L-alanine
P83788
L-tryptophan metabolism
-
-
?
L-kynurenine + H2O
anthranilate + L-alanine
-
L-tryptophan metabolism
-
-
?
L-kynurenine + H2O
anthranilate + L-alanine
-
L-tryptophan metabolism
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
the phosphate of pyridoxal 5'-phosphate is an acid/base catalyst in the mechanism of kynureninase. Tyr226 hydrogen bonds to the phosphate of the pyridoxal 5'-phosphate cofactor
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2S)-2-amino-4-oxo-4-phenylbutanoic acid
-
competitive inhibitor of the reaction of L-kynurenine with the enzyme
(alphaS,4S)-dihydrokynurenine
-
the (alphaS,4R) diastereomer is a slow substrate for a retro-aldol reaction, and the (alphaS,4S) isomer is a potent competitive inhibitor, proposed mechanism for reaction of dihydrokynurenine
(S)-(2-amino-4-bromophenyl)-L-cysteine S,S-dioxide
-
competitive inhibition
(S)-(2-amino-5-bromophenyl)-L-cysteine S,S-dioxide
-
competitive inhibition
5-bromodihydrokynurenine
-
a potent transition-state analogue inhibitor
lanthellamide
-
about 60% residual activity at 1 mM, about 80% residual activity at 0.5 mM, slight inhibition at 0.125 mM
2-amino-(4-oxo-4-naphthyl)-butyric acid
-
competitive inhibition, reversible inhibition by dilution
2-amino-(4-oxo-4-naphthyl)-butyric acid
-
competitive inhibition, reversible inhibition by dilution
3-hydroxydeaminokynurenine
-
competitive and non competitive inhibition
3-methoxydeaminokynurenine
-
competitive and non competitive inhibition
amino-(1-oxo-1,2,3,4-tetrahydro-2-naphthalenyl)-acetic acid
-
competitive inhibition, reversible inhibition by dilution
amino-(1-oxo-1,2,3,4-tetrahydro-2-naphthalenyl)-acetic acid
-
competitive inhibition, reversible inhibition by dilution
amino-(1-oxo-2,3-dihydro-1H-inden-2-yl)-acetic acid
-
competitive inhibition, reversible inhibition by dilution
amino-(1-oxo-2,3-dihydro-1H-inden-2-yl)-acetic acid
-
competitive inhibition, reversible inhibition by dilution
amino-(4-oxo-3,4-dihydro-2H-chromen-3-yl)-acetic acid
-
competitive inhibition, reversible inhibition by dilution
amino-(4-oxo-3,4-dihydro-2H-chromen-3-yl)-acetic acid
-
competitive inhibition, reversible inhibition by dilution
L-kynurenine
-
competitive inhibition, at low substrate concentrations; non-competitive inhibition, at higher levels of substrate
additional information
-
catabolite repression of the pathway by glucose and glutamate, arginine does not cause repression
-
additional information
-
not inhibited by DL-4-(ethylsulfonyl)benzoylalanine and its active enatiomer (S)-4-(ethylsulfonyl)benzoylalanine
-
additional information
-
lanthellamide does not inhibit the enzyme at concentrations up to 0.0625 mM
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
kynurenine induces both tryptophan oxygenase and kynureninase of the catabolic pathway of L-tryptophan degradation
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0283
3-hydroxy-L-kynurenine
-
wild type enzyme, in 30 mM potassium phosphate, pH 8.0, and 0.04 mM pyridoxal 5'-phosphate, at 37°C
0.2
3-hydroxy-L-kynurenine
-
Km above 0.2 mM, mutant enzyme N333T, in 30 mM potassium phosphate, pH 8.0, and 0.04 mM pyridoxal 5'-phosphate, at 37°C
0.51
3-hydroxy-L-kynurenine
-
Km above 0.51 mM, mutant enzyme S332G/N333T, in 30 mM potassium phosphate, pH 8.0, and 0.04 mM pyridoxal 5'-phosphate, at 37°C
0.327
L-kynurenine
-
mutant enzyme H102W/N333T, in 30 mM potassium phosphate, pH 8.0, and 0.04 mM pyridoxal 5'-phosphate, at 37°C
0.495
L-kynurenine
-
wild type enzyme, in 30 mM potassium phosphate, pH 8.0, and 0.04 mM pyridoxal 5'-phosphate, at 37°C
0.499
L-kynurenine
-
mutant enzyme N333T, in 30 mM potassium phosphate, pH 8.0, and 0.04 mM pyridoxal 5'-phosphate, at 37°C
0.51
L-kynurenine
-
Km above 0.51 mM, mutant enzyme H102W/S332G/N333T, in 30 mM potassium phosphate, pH 8.0, and 0.04 mM pyridoxal 5'-phosphate, at 37°C
0.54
L-kynurenine
-
mutant enzyme S332G/N333T, in 30 mM potassium phosphate, pH 8.0, and 0.04 mM pyridoxal 5'-phosphate, at 37°C
additional information
additional information
-
kinetic analysis of kynurenine analogues, overview
-
additional information
additional information
-
kinetic analysis of kynurenine analogues, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.08
2-amino-4-(2-chlorophenyl)-4-oxobutanoic acid
-
at 37°C in 0.04 M potassium phosphate, pH 7.8
-
0.05
2-amino-4-(2-methoxyphenyl)-4-oxobutanoic acid
-
at 37°C in 0.04 M potassium phosphate, pH 7.8
-
0.38
2-amino-4-(4-methoxyphenyl)-4-oxobutanoic acid
-
at 37°C in 0.04 M potassium phosphate, pH 7.8
-
0.06
2-fluorobenzoyl-DL-alanine
-
at 37°C in 0.04 M potassium phosphate, pH 7.8
-
1.83
beta-(4-chlorobenzoyl)-DL-alanine
-
at 37°C in 0.04 M potassium phosphate, pH 7.8
0.91
beta-(4-methylbenzoyl)-DL-alanine
-
at 37°C in 0.04 M potassium phosphate, pH 7.8
0.001
beta-(4-trifluoromethylbenzoyl)-DL-alanine
-
at 37°C in 0.04 M potassium phosphate, pH 7.8
0.0039
3-hydroxy-L-kynurenine
-
kcat less than 0.0039 1/s, mutant enzyme N333T, in 30 mM potassium phosphate, pH 8.0, and 0.04 mM pyridoxal 5'-phosphate, at 37°C
0.0109
3-hydroxy-L-kynurenine
-
kcat less than 0.0109 1/s, mutant enzyme S332G/N333T, in 30 mM potassium phosphate, pH 8.0, and 0.04 mM pyridoxal 5'-phosphate, at 37°C
3.5
3-hydroxy-L-kynurenine
-
wild type enzyme, in 30 mM potassium phosphate, pH 8.0, and 0.04 mM pyridoxal 5'-phosphate, at 37°C
6.3
5-bromo-3-chloro-DL-kynurenine
-
pH 8.0, 37°C, recombinant enzyme
0.007
L-kynurenine
-
mutant enzyme H102W/N333T, in 30 mM potassium phosphate, pH 8.0, and 0.04 mM pyridoxal 5'-phosphate, at 37°C
0.017
L-kynurenine
-
mutant enzyme S332G/N333T, in 30 mM potassium phosphate, pH 8.0, and 0.04 mM pyridoxal 5'-phosphate, at 37°C
0.018
L-kynurenine
-
Km above 0.51 mM, mutant enzyme H102W/S332G/N333T, in 30 mM potassium phosphate, pH 8.0, and 0.04 mM pyridoxal 5'-phosphate, at 37°C
0.026
L-kynurenine
-
mutant enzyme N333T, in 30 mM potassium phosphate, pH 8.0, and 0.04 mM pyridoxal 5'-phosphate, at 37°C
0.23
L-kynurenine
-
wild type enzyme, in 30 mM potassium phosphate, pH 8.0, and 0.04 mM pyridoxal 5'-phosphate, at 37°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
12
2-amino-4-(2-chlorophenyl)-4-oxobutanoic acid
-
at 37°C in 0.04 M potassium phosphate, pH 7.8
-
1.4
2-amino-4-(2-methoxyphenyl)-4-oxobutanoic acid
-
at 37°C in 0.04 M potassium phosphate, pH 7.8
-
1.6
2-amino-4-(4-methoxyphenyl)-4-oxobutanoic acid
-
at 37°C in 0.04 M potassium phosphate, pH 7.8
-
1.7
2-fluorobenzoyl-DL-alanine
-
at 37°C in 0.04 M potassium phosphate, pH 7.8
-
18
beta-(4-chlorobenzoyl)-DL-alanine
-
at 37°C in 0.04 M potassium phosphate, pH 7.8
28
beta-(4-methylbenzoyl)-DL-alanine
-
at 37°C in 0.04 M potassium phosphate, pH 7.8
0.019
beta-(4-trifluoromethylbenzoyl)-DL-alanine
-
at 37°C in 0.04 M potassium phosphate, pH 7.8
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.01
(2S)-2-amino-4-oxo-4-phenylbutanoic acid
-
reaction of L-kynurenine with the enzyme
0.17
amino-(1-oxo-1,2,3,4-tetrahydro-2-naphthalenyl)-acetic acid
-
at 37ºC, pH 7.5
0.227
amino-(1-oxo-1,2,3,4-tetrahydro-2-naphthalenyl)-acetic acid
-
at 37ºC, pH 7.5
0.0349
amino-(1-oxo-2,3-dihydro-1H-inden-2-yl)-acetic acid
-
at 37ºC, pH 7.5
0.162
amino-(4-oxo-3,4-dihydro-2H-chromen-3-yl)-acetic acid
-
at 37ºC, pH 7.5
0.00003
S-(2-aminophenyl)-L-cysteine dioxide
-
wild-type enzyme, pH 8.0, 37°C
0.00092
S-(2-aminophenyl)-L-cysteine dioxide
-
enzyme mutant Y226F, pH 8.0, 37°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10
additional information
additional information
-
poor activity in cells grown on arginine and on glucose, also in presence of L-tryptophan
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
cells grown in a medium containing L-tryptophan as the sole carbon, nitrogen, and energy source
-
the catalytic activity of kynureninase is very low in most tissue with exception of liver and kidney
-
enzyme activity does not change significantly as compared to controls; enzyme activity does not change significantly in normolipidemic and diet-induced hyperlipidemic animals as compared to controls
-
enzyme activity is very low in newborn rats, but increases in rats of 2-3 months to 18 months of age, without an evident age-related pattern
-
the catalytic activity of kynureninase is very low in most tissue with exception of liver and kidney
-
enzyme activity significantly decreased only per g of fresh tissue as compared to controls; enzyme activity significantly decreased only per g of fresh tissue in the group of diet-induced hyperlipidemic animals as compared to controls
-
-
-
enzyme activity declines with age, similar in newborns and 2-3 month-old rats, activity decreases markedly by ca. 60% and 70% at 12 and 18 months, respectively
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Homo sapiens;
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
52400
95000
100000
105000
110000
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
no modification
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystals of recombinant kynureninase that diffracted to 2.0 A are obtained, and the atomic structure of the PLP-bound holoenzyme is determined by molecular replacement using the Pseudomonas fluorescens structure as the phasing model
-
the wild type enzyme is cocrystallized with 3-hydroxyhippuric acid, using the modified microbatch under oil technique at 25?C, with 0.05 M MgCl2, 0.1 M Tris (pH 8.0), and 25% (w/v) PEG 3000
-
by hanging-drop vapor diffusion method at room temperature, to 1.85 A resolution, Lys-227 is the pyridoxal-5'-phosphate binding residue near the pyridoxal-5'-phosphate nitrogen, but Asp-132 is also strictly conserved and at a similar distance from the pyridinium nitrogen, Tyr-226 donates a hydrogen bond to the phosphate of pyridoxal-5'-phosphate, Trp-256 donates a hydrogen bond to the phosphate through the indole N1-hydrogen; performed using the hanging-drop vapor diffusion technique
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-78ºC, 0.1 mM potassium phosphate buffer, 0.2 mM pyridoxal 5'-phosphate, pH 8.0, 1 year, stable
-78ºC, 5 mM potassium phosphate buffer, 0.2 mM pyridoxal 5'-phosphate, pH 8.0, 1 month, loses 4% of activity
-80ºC, without pyridoxal 5'-phosphate, more than 12 months, no loss of activity
-
4°C, phosphate buffer, pH 7.2, 0.02 mM pyridoxal-5'-phosphate, 1 week
-
4ºC, 5 mM potassium phosphate buffer, 0.2 mM pyridoxal 5'-phosphate, pH 8.0, 1 week, loses 40% of activity
70% saturated solution of ammonium sulfate containing 1 mM EDTA, 1 mM dithiothreitol, and 0.05 mM pyridoxal 5'-phosphate, 2 months
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; recombinant enzyme, by centrifugation, protamine sulfate precipitation, HiTrap Q column, omega-aminohexylagarose column, second HiTrap Q column and phenyl-Sepharose column
by protamine sulfate precipitation, ammonium sulfate precipitation, DEAE-Sepharose 6B column, Sephadex G-100 column, Mono-Q HR 5/5 column, 50-80fold
-
by strong cationic column, strong anion exchange column and hydroxyapatite column
-
recombinant enzyme from Escherichia coli strain DH5alpha
recombinant enzyme, ammonium sulfate precipitation, DEAE-Sepharose CL-6B affinity column, hydroxyapatite column, strong anion-exchange column at pH 8.6, strong cation-exchange column at pH 6.0 strong anion-exchange column at pH 6.0, 60fold
-
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli; into vector pTZKYN and transformed in Escherichia coli XL-1 Blue cells
-
expression in Escherichia coli; subcloned into pSapKO-WT and transformed into Escherichia coli B834(DE3)
expression of the recombinant enzyme in Escherichia coli strain DH5alpha
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
T102I
the mutation leads to a marked decrease in kynureninase activity and causes the red body coloration in the Bombyx mori red blood strain
H102W/N333T
-
the mutant shows complete reversal of substrate specificity between 3-hydroxy-L-kynurenine and L-kynurenine
H102W/S332G/N333T
-
the mutant shows complete reversal of substrate specificity between 3-hydroxy-L-kynurenine and L-kynurenine
N333T
-
the mutant reveals a 9fold decrease in kcat for L-kynurenine, but no change in Km, the mutant has weaker 3-hydroxy-L-kyrenine binding (6fold higher Km) and kcat at least 1100times slower than wild type Kynase
S332G/N333T the
-
mutant shows a very slight preference for L-kynurenine over 3-hydroxy-L-kynurenine
T198A
-
screening of cDNA from KYNU revealed homozygosity for a c.593A>G substitution in exon 7 in the proband, leading to a threonine-to-alanine shift, T198A, in kynureninase
D132A
has lower activity and binds pyridoxal 5'-phosphate weakly; has lower activity and weaklier pyridoxal-5'-phosphate binding than that of wild-type enzyme
D132E
has good activity and pyridoxal 5'-phosphate binding stronger than that of the wild-type enzyme; has good activity and stronger pyridoxal-5'-phosphate binding than that of wild-type enzyme
D201A
has very low activity and binds pyridoxal-5'-phosphate weakly, and expresses poorly, giving large amounts of insoluble inclusion bodies and very low levels of soluble protein; has very low activity, less than 0.01% of that of the wild-type enzyme, binds pyridoxal 5'-phosphate weakly
D201E
has good activity and pyridoxal 5'-phosphate binding stronger than that of the wild-type enzyme; has good activity and stronger pyridoxal-5'-phosphate binding than that of wild-type enzyme
Y226F
-
site-directed mutagenesis, the mutant has approximately 3000fold lower activity than wild-type, and does not show the pKa values of 6.8 on kcat and 6.5 and 8.8 on kcat/Km seen for the wild-type enzyme
additional information