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Information on EC 3.7.1.3 - kynureninase and Organism(s) Pseudomonas fluorescens and UniProt Accession P83788
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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
-
quinolinic
- 3-hydroxykynurenine
-
kynurenic
-
anthranilic
- indoleamine
-
3-monooxygenase
- l-tryptophan
-
ido
-
3,4-dioxygenase
-
xanthurenic
- aminocarboxymuconate-semialdehyde
-
3-hydroxylase
-
quin
-
excitotoxins
-
quinonoid
-
pyrrolase
- marginalis
- indoleamine-2,3-dioxygenase
- synthesis
-
b6-deficient
- drug development
The taxonomic range for the selected organisms is: Pseudomonas fluorescens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
kynureninase, kynase, pfkynase, l-kynurenine hydrolase, hskynase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
L-kynurenine hydrolase
L-kynurenine hydrolase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of C-C bond
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
L-kynurenine hydrolase
A pyridoxal-phosphate protein. Also acts on 3'-hydroxy-L-kynurenine and some other (3-arylcarbonyl)-alanines.
CAS REGISTRY NUMBER
COMMENTARY
9024-78-6
-
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
(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
-
-
?
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-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-L-kynurenine + H2O
5-bromoanthranilate + L-alanine
-
-
-
?
5-chloro-L-kynurenine + H2O
5-chloroanthranilate + L-alanine
-
-
-
?
(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
-
-
?
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 + ?
-
-
-
?
L-kynurenine + H2O
anthranilate + L-alanine
L-tryptophan metabolism
-
-
?
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
-
-
?
O-benzoyl-L-serine + H2O
benzoate + pyruvate + ammonium
-
-
-
?
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-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
-
-
-
-
?
3-hydroxy-L-kynurenine + H2O
3-hydroxyanthranilate + L-alanine
-
biosynthesis of NAD+
-
-
?
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
-
-
-
-
?
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
-
-
?
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 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
-
-
?
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
-
-
-
?
L-kynurenine + H2O
anthranilate + L-alanine
L-tryptophan metabolism
-
-
?
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
-
biosynthesis of NAD+
-
-
?
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
-
L-tryptophan metabolism
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
pyridoxal 5'-phosphate
-
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(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
5-bromodihydrokynurenine
a potent transition-state analogue inhibitor
S-(2-aminophenyl)-L-cysteine S,S-dioxide
potent competitive inhibitor
(2S)-2-amino-4-oxo-4-phenylbutanoic acid
-
competitive inhibitor of the reaction of L-kynurenine with the enzyme
(S)-(2-amino-4-bromophenyl)-L-cysteine S,S-dioxide
-
competitive inhibition
(S)-(2-amino-5-bromophenyl)-L-cysteine S,S-dioxide
-
competitive inhibition
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-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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
kinetic analysis of kynurenine analogues, overview
-
additional information
additional information
-
kinetic analysis of kynurenine analogues, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.23
3,5-dibromo-L-kynurenine
pH 8.0, 37°C, recombinant enzyme
6.3
5-bromo-3-chloro-DL-kynurenine
pH 8.0, 37°C, recombinant enzyme
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
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
22
5-bromo-3-chloro-DL-kynurenine
pH 8.0, 37°C, recombinant enzyme
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
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
0.0349
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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D132A
D132E
D201A
D201E
S36A
the mutant enzyme can form quinonoid and vinylogous amide intermediates with beta-benzoyl-L-alanine, similar to wild-type enzyme. Mutation results in a 230fold reduction of kcat and 30fold reduction in kcat/Km with L-kynurenine, but very little effect on the reaction of O-benzoyl-L-serine. The rate-determining step in the reaction of thje mutant enzyme the Cbeta-Cgamma bond cleavage
Y226F
D132A
has lower activity and binds pyridoxal 5'-phosphate weakly
D132A
has lower activity and weaklier pyridoxal-5'-phosphate binding than that of wild-type enzyme
D132A
mutation results in reduced catalytic activity with L-kynurenine and beta-benzoyl-L-alanine, but not O-benzoyl-L-serine. The mutant enzyme can form quinonoid and vinylogous amide intermediates with beta-benzoyl-L-alanine, similar to wild-type enzyme. The mutant enzyme reacts more slowly with beta-benzoyl-L-alanine and benzaldehyde to form an aldol product absorbing at 490 nm than wild-type
D132E
has good activity and pyridoxal 5'-phosphate binding stronger than that of the wild-type enzyme
D132E
has good activity and stronger pyridoxal-5'-phosphate binding than that of wild-type enzyme
D132E
mutation results in reduced catalytic activity with L-kynurenine and beta-benzoyl-L-alanine, but not O-benzoyl-L-serine. The mutant enzyme can form quinonoid and vinylogous amide intermediates with beta-benzoyl-L-alanine, similar to wild-type enzyme. The mutant enzyme reacts more slowly with beta-benzoyl-L-alanine and benzaldehyde to form an aldol product absorbing at 490 nm than wild-type
D201A
has very low activity, less than 0.01% of that of the wild-type enzyme, binds pyridoxal 5'-phosphate weakly
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
D201E
has good activity and pyridoxal 5'-phosphate binding stronger than that of the wild-type enzyme
D201E
has good activity and stronger pyridoxal-5'-phosphate binding than that of wild-type enzyme
D201E
mutation results in reduced catalytic activity with L-kynurenine and beta-benzoyl-L-alanine, but not O-benzoyl-L-serine. The mutant enzyme can form quinonoid and vinylogous amide intermediates with beta-benzoyl-L-alanine, similar to wild-type enzyme. The mutant enzyme reacts more slowly with beta-benzoyl-L-alanine and benzaldehyde to form an aldol product absorbing at 490 nm than wild-type
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
Y226F
mutation results in very low activity, about 0.1%, with L-kynurenine
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
4ºC, 5 mM potassium phosphate buffer, 0.2 mM pyridoxal 5'-phosphate, pH 8.0, 1 week, loses 40% of activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli strain DH5alpha
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
-
recombinant enzyme from Escherichia coli strain DH5alpha
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of the recombinant enzyme in Escherichia coli strain DH5alpha
subcloned into pSapKO-WT and transformed into Escherichia coli B834(DE3)
into vector pTZKYN and transformed in Escherichia coli XL-1 Blue cells
-
expression of the recombinant enzyme in Escherichia coli strain DH5alpha
expression of the recombinant enzyme in Escherichia coli strain DH5alpha
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
the enzym eis a target for the design of potent and/or selective inhibitors of bacterial kynureninase
medicine
synthesis
-
of inhibitors of kynureninase could prove to be useful in the development of the successful treatment regimen for neurological disorders such as septicemia, AIDS related dementia, Lyme disease, Huntington's and Alzheimer's disease
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Shetty, A.S.; Gaertner, F.H.
Kynureninase-type enzymes of Penicillium roqueforti, Aspergillus niger, Rhizopus stolonifer, and Pseudomonas fluorescens: Further evidence for distinct kynureninase and hydroxykynureninase activities
J. Bacteriol.
122
235-244
1975
Aspergillus niger, Penicillium roqueforti, Pseudomonas fluorescens, Rhizopus stolonifer
Tanizawa, K.; Soda, K.
The mechanism of kynurenine hydrolysis catalyzed by kynureninase
J. Biochem.
86
1199-1209
1979
Pseudomonas fluorescens
Soda, K.; Tanizawa, K.
Kynureninases: Enzymological properties and regulation mechanism
Adv. Enzymol. Relat. Areas Mol. Biol.
49
1-40
1979
amphibia, Aspergillus niger, aves, Bos taurus, Canis lupus familiaris, Cavia porcellus, Chondrichthyes, Homo sapiens, Mus musculus, Neurospora crassa, Penicillium roqueforti, Pseudomonas fluorescens, Pseudomonas marginalis, Rattus norvegicus, Rhizopus stolonifer, Saccharomyces cerevisiae, Testudines, Xanthomonas arboricola pv. pruni
Palcic, M.M.; Antoun, M.; Tanizawa, K.; Soda, K.; Floss, H.G.
Stereochemistry of the kynureninase reaction
J. Biol. Chem.
260
5248-5251
1985
Pseudomonas fluorescens
Phillips, R.S.; Dua, R.K.
Stereochemistry and mechanism of aldol reactions catalyzed by kynureninase
J. Am. Chem. Soc.
113
7385-7388
1991
Pseudomonas fluorescens
-
Koushik, S.V.; Sundararaju, B.; McGraw, R.A.; Phillips, R.S.
Cloning, sequence, and expression of kynureninase from Pseudomonas fluorescens
Arch. Biochem. Biophys.
34
301-308
1997
Pseudomonas fluorescens
Phillips, R.S.; Sundararaju, B.; Koushik, S.V.
The catalytic mechanism of kynureninase from Pseudomonas fluorescens: Evidence for transient quinonoid and ketimine intermediates from rapid-scanning stopped-flow spectrophotometry
Biochemistry
37
8783-8789
1998
Pseudomonas fluorescens
Koushik, S.V.; Moore III, J.A.; Sundararaju, B.; Phillips, R.S.
The catalytic mechanism of kynureninase from Pseudomonas fluorescens: Insights from the effects of pH and isotopic substitution on steady-state and pre-steady-state kinetics
Biochemistry
37
1376-1382
1998
Pseudomonas fluorescens
Cyr, L.V.; Newton, M.G.; Phillips, R.S
Stereospecificity of Pseudomonas fluorescens kynureninase for diastereomers of beta-methylkynurenine
Bioorg. Med. Chem.
7
1497-1503
1999
Pseudomonas fluorescens
Momany, C.; Levdikov, V.; Blagova, L.; Lima, S.; Phillips, R.S.
Three-dimensional structure of kynureninase from Pseudomonas fluorescens
Biochemistry
43
1193-1203
2004
Pseudomonas fluorescens (P83788), Pseudomonas fluorescens
Gawandi, V.B.; Liskey, D.; Lima, S.; Phillips, R.S.
Reaction of Pseudomonas fluorescens kynureninase with beta-benzoyl-L-alanine: Detection of a new reaction intermediate and a change in rate-determining step
Biochemistry
43
3230-3237
2004
Pseudomonas fluorescens
Fitzgerald, D.H.; Muirhead, K.M.; Botting, N.P.
A comparative study on the inhibition of human and bacterial kynureninase by novel bicyclic kynurenine analogues
Bioorg. Med. Chem.
9
983-989
2001
Homo sapiens, Pseudomonas fluorescens
Walsh, H.A.; O'Shea, K.C.; Botting, N.P.
Comparative inhibition by substrate analogues 3-methoxy- and 3-hydroxydesaminokynurenine and an improved 3 step purification of recombinant human kynureninase
BMC Biochem.
4
13
2003
Homo sapiens, Pseudomonas fluorescens, Rattus norvegicus
Heiss, C.; Anderson, J.; Phillips, R.S.
Differential effects of bromination on substrates and inhibitors of kynureninase from Pseudomonas fluorescens
Org. Biomol. Chem.
1
288-295
2003
Pseudomonas fluorescens
Kumar, S.; Gawandi, V.B.; Capito, N.; Phillips, R.S.
Substituent effects on the reaction of beta-benzoylalanines with Pseudomonas fluorescens kynureninase
Biochemistry
49
7913-7919
2010
Pseudomonas fluorescens
Maitrani, C.; Phillips, R.S.
Substituents effects on activity of kynureninase from Homo sapiens and Pseudomonas fluorescens
Bioorg. Med. Chem.
21
4670-4677
2013
Homo sapiens (Q16719), Homo sapiens, Pseudomonas fluorescens (P83788), Pseudomonas fluorescens
Phillips, R.S.; Scott, I.; Paulose, R.; Patel, A.; Barron, T.C.
The phosphate of pyridoxal-5'-phosphate is an acid/base catalyst in the mechanism of Pseudomonas fluorescens kynureninase
FEBS J.
281
1100-1109
2014
Pseudomonas fluorescens (P83788), Pseudomonas fluorescens
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