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Information on EC 3.7.1.3 - kynureninase
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3.7.1.3 kynureninaseIUBMB Comments
A pyridoxal-phosphate protein. Also acts on 3'-hydroxy-L-kynurenine and some other (3-arylcarbonyl)-alanines.
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Word Map
- 3.7.1.3
-
3-hydroxyanthranilic
- medicine
- 3-hydroxykynurenine
-
quinolinic
-
anthranilic
-
kynurenic
- indoleamine
- l-tryptophan
-
3-monooxygenase
-
ido
-
3,4-dioxygenase
-
3-hydroxylase
-
xanthurenic
- aminocarboxymuconate-semialdehyde
-
quin
-
pyrrolase
-
quinonoid
-
kynurenine-3-hydroxylase
-
b6-deficient
- synthesis
- marginalis
- indoleamine-2,3-dioxygenase
- drug development
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
HsKynase, Kynase, KYNU, kynureninase, L-kynurenine hydrolase, PfKynase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Kynase
kynureninase
L-kynurenine hydrolase
L-kynurenine hydrolase
-
-
-
-
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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 SOURCE
PATHWAYS
BRENDA
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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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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
-
-
-
-
?
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
-
-
-
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NATURAL SUBSTRATE
NATURAL 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
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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INHIBITOR
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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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Brain Injuries
Kynurenine pathway enzymes in brain: responses to ischemic brain injury versus systemic immune activation.
Brain Ischemia
Kynurenine pathway enzymes in brain: responses to ischemic brain injury versus systemic immune activation.
Breast Neoplasms
A novel role of kynureninase in the growth control of breast cancer cells and its relationships with breast cancer.
Carcinoma
Down-regulation of kynureninase restrains cutaneous squamous cell carcinoma proliferation and represses PI3K/AKT pathway.
Carcinoma, Squamous Cell
Down-regulation of kynureninase restrains cutaneous squamous cell carcinoma proliferation and represses PI3K/AKT pathway.
Dementia
Comparative inhibition by substrate analogues 3-methoxy- and 3-hydroxydesaminokynurenine and an improved 3 step purification of recombinant human kynureninase.
Encephalitis
A mechanism of quinolinic acid formation by brain in inflammatory neurological disease. Attenuation of synthesis from L-tryptophan by 6-chlorotryptophan and 4-chloro-3-hydroxyanthranilate.
Epilepsy
Epilepsy as a pyridoxine-dependent condition: quantified urinary biomarkers for status evaluation and monitoring antiepileptic treatment.
Essential Hypertension
A rare variant at the KYNU gene is associated with kynureninase activity and essential hypertension in the Han Chinese population.
Essential Hypertension
[A polymorphism of kynureninase gene in a hypertensive candidate chromosomal region is associated with essential hypertension]
Hypertension
A rare variant at the KYNU gene is associated with kynureninase activity and essential hypertension in the Han Chinese population.
Hypertension
Kynureninase is a novel candidate gene for hypertension in spontaneously hypertensive rats.
Ichthyosis
Ichthyosis molecular fingerprinting shows profound TH17 skewing and a unique barrier genomic signature.
Infections
Increased mRNA expression of kynurenine pathway enzymes in human placentae exposed to bacterial endotoxin.
Ischemic Attack, Transient
Mechanism of delayed increases in kynurenine pathway metabolism in damaged brain regions following transient cerebral ischemia.
kynureninase deficiency
The urinary ratio of 3-hydroxykynurenine/3-hydroxyanthranilic acid is an index to predicting the adverse effects of D-tryptophan in rats.
kynureninase deficiency
Xanthurenic aciduria due to a mutation in KYNU encoding kynureninase.
Meningitis, Pneumococcal
The cerebral protective effect and mechanism of action of vitamin B6 adjuvant ceftriaxone in experimental pneumococcal meningitis.
Metabolic Diseases
A novel role of kynureninase in the growth control of breast cancer cells and its relationships with breast cancer.
Myocardial Infarction
Sarcopenia and sarcopenic obesity as prognostic predictors in hospitalized elderly patients with acute myocardial infarction.
Neoplasms
A novel role of kynureninase in the growth control of breast cancer cells and its relationships with breast cancer.
Neoplasms
Reversal of indoleamine 2,3-dioxygenase-mediated cancer immune suppression by systemic kynurenine depletion with a therapeutic enzyme.
Neoplasms
Tryptophan PET Imaging of the Kynurenine Pathway in Patient-Derived Xenograft Models of Glioblastoma.
Neoplasms
Tryptophan pyrrolase, kynureninase and kynurenine transaminase activities of human renal tumours.
Neoplasms
[Importance of E-cadherin; expression in the inmunohistochemical diagnosis of breast cancer]
Neuralgia
Pharmacological Inhibition of Indoleamine 2,3-Dioxygenase-2 and Kynurenine 3-Monooxygenase, Enzymes of the Kynurenine Pathway, Significantly Diminishes Neuropathic Pain in a Rat Model.
Obesity
The kynurenine pathway is activated in human obesity and shifted toward kynurenine monooxygenase activation.
Pellagra
[Inhibiting effect of amino acids on kynureninase and its significance in the pathogenesis of pellagra.]
Phenylketonurias
[Kynureninase activity and pyridoxine elimination in rats with experimental phenylketonuria]
Psoriasis
Gene expression of enzymes for tryptophan degradation pathway is upregulated in the skin lesions of patients with atopic dermatitis or psoriasis.
Psoriasis
Ichthyosis molecular fingerprinting shows profound TH17 skewing and a unique barrier genomic signature.
Renal Insufficiency
Mechanism of increases in L-kynurenine and quinolinic acid in renal insufficiency.
Seizures
Epilepsy as a pyridoxine-dependent condition: quantified urinary biomarkers for status evaluation and monitoring antiepileptic treatment.
Vitamin B 6 Deficiency
High-performance liquid chromatographic assay of human lymphocyte kynureninase activity levels.
Vitamin B 6 Deficiency
Inhibition of kynureninase by oestrogen conjugates: evidence that oestrogens do not cause vitamin B6 deficiency.
Vitamin B 6 Deficiency
LIVER kynureninase activity and tryptophan metabolism in vitamin B6 deficiency.
Vitamin B 6 Deficiency
The relation of liver kynureninase to tryptophan metabolism in pyridoxine deficiency.
Vitamin B Deficiency
Inhibition of kynureninase (L-kynurenine hydrolase, EC 3 . 7. 1 . 3) by oestrone sulphate: an alternative explanation for abnormal results of tryptophan load tests in women receiving oestrogenic steroids.
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
289260, 289268, 289271, 289277, 289278, 289280, 289281, 289282, 289287, 34546, 657495, 658345, 673094, 673130, 719066
-
-
brenda
male normolipidemic and diet-induced hyperlipidemic New Zealand rabbits; male Watanabe heritable hyperlipidemic rabbits
-
-
brenda
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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
brenda
-
the catalytic activity of kynureninase is very low in most tissue with exception of liver and kidney
brenda
-
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
brenda
-
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
brenda
-
the catalytic activity of kynureninase is very low in most tissue with exception of liver and kidney
brenda
-
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
brenda
-
-
brenda
-
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
brenda
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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
Show AA Sequence and Transmembrane Helices (9530 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
52400
95000
100000
105000
110000
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SUBUNIT
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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PROTEIN VARIANTS
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
additional information
-
cosmid pRA3 corrects trpA, trpB and trpC mutants in Escherichia coli
additional information
-
cosmid pRA3 corrects trpA mutants of Rhizobium leguminosarum