EC Number | Application | Comment | Organism |
---|---|---|---|
3.7.1.3 | drug development | the enzym eis a target for the design of potent and/or selective inhibitors of bacterial kynureninase | Pseudomonas fluorescens |
3.7.1.3 | drug development | the enzyme is a target for the design of potent and/or selective inhibitors of human kynureninase | Homo sapiens |
EC Number | Cloned (Comment) | Organism |
---|---|---|
3.7.1.3 | expression of the recombinant enzyme in Escherichia coli strain BL21(DE3) | Homo sapiens |
3.7.1.3 | expression of the recombinant enzyme in Escherichia coli strain DH5alpha | Pseudomonas fluorescens |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.7.1.3 | additional information | - |
additional information | kinetic analysis of kynurenine analogues, overview | Homo sapiens | |
3.7.1.3 | additional information | - |
additional information | kinetic analysis of kynurenine analogues, overview | Pseudomonas fluorescens |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.7.1.3 | 3-hydroxy-L-kynurenine + H2O | Homo sapiens | - |
3-hydroxyanthranilate + L-alanine | - |
? | |
3.7.1.3 | L-kynurenine + H2O | Pseudomonas fluorescens | - |
anthranilate + L-alanine | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.7.1.3 | Homo sapiens | Q16719 | - |
- |
3.7.1.3 | Pseudomonas fluorescens | P83788 | gene kynU | - |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.7.1.3 | recombinant enzyme from Escherichia coli strain BL21(DE3) | Homo sapiens |
3.7.1.3 | recombinant enzyme from Escherichia coli strain DH5alpha | Pseudomonas fluorescens |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
3.7.1.3 | L-kynurenine + H2O = anthranilate + L-alanine | catalytic reaction mechanism via several intermediates, e.g. external aldimine, quinonoid, ketimine, Gem-diolate, and enamine | Homo sapiens | |
3.7.1.3 | L-kynurenine + H2O = anthranilate + L-alanine | catalytic reaction mechanism via several intermediates, e.g. external aldimine, quinonoid, ketimine, Gem-diolate, and enamine | Pseudomonas fluorescens |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.7.1.3 | 3,5-dibromo-L-kynurenine + H2O | - |
Homo sapiens | 3,5-dibromoanthranilate + DL-kynurenine | - |
? | |
3.7.1.3 | 3,5-dibromo-L-kynurenine + H2O | - |
Pseudomonas fluorescens | 3,5-dibromoanthranilate + DL-kynurenine | - |
? | |
3.7.1.3 | 3-bromo-L-kynurenine + H2O | - |
Homo sapiens | 3-bromoanthranilate + L-alanine | - |
? | |
3.7.1.3 | 3-bromo-L-kynurenine + H2O | - |
Pseudomonas fluorescens | 3-bromoanthranilate + L-alanine | - |
? | |
3.7.1.3 | 3-chloro-DL-kynurenine + H2O | - |
Homo sapiens | 3-chloroanthranilate + DL-alanine | - |
? | |
3.7.1.3 | 3-chloro-DL-kynurenine + H2O | - |
Pseudomonas fluorescens | 3-chloroanthranilate + DL-alanine | - |
? | |
3.7.1.3 | 3-fluoro-DL-kynurenine + H2O | - |
Homo sapiens | 3-fluoroanthranilate + DL-alanine | - |
? | |
3.7.1.3 | 3-fluoro-DL-kynurenine + H2O | - |
Pseudomonas fluorescens | 3-fluoroanthranilate + DL-alanine | - |
? | |
3.7.1.3 | 3-hydroxy-L-kynurenine + H2O | - |
Homo sapiens | 3-hydroxyanthranilate + L-alanine | - |
? | |
3.7.1.3 | 3-hydroxy-L-kynurenine + H2O | - |
Pseudomonas fluorescens | 3-hydroxyanthranilate + L-alanine | - |
? | |
3.7.1.3 | 3-methyl-DL-kynurenine + H2O | - |
Homo sapiens | 3-methylanthranilate + DL-alanine | - |
? | |
3.7.1.3 | 3-methyl-DL-kynurenine + H2O | - |
Pseudomonas fluorescens | 3-methylanthranilate + DL-alanine | - |
? | |
3.7.1.3 | 5-bromo-3-chloro-DL-kynurenine + H2O | - |
Homo sapiens | 5-bromo-3-chloroanthranilate + DL-alanine | - |
? | |
3.7.1.3 | 5-bromo-3-chloro-DL-kynurenine + H2O | - |
Pseudomonas fluorescens | 5-bromo-3-chloroanthranilate + DL-alanine | - |
? | |
3.7.1.3 | 5-bromo-L-kynurenine + H2O | - |
Homo sapiens | 5-bromoanthranilate + L-alanine | - |
? | |
3.7.1.3 | 5-bromo-L-kynurenine + H2O | - |
Pseudomonas fluorescens | 5-bromoanthranilate + L-alanine | - |
? | |
3.7.1.3 | 5-chloro-L-kynurenine + H2O | - |
Homo sapiens | 5-chloroanthranilate + L-alanine | - |
? | |
3.7.1.3 | 5-chloro-L-kynurenine + H2O | - |
Pseudomonas fluorescens | 5-chloroanthranilate + L-alanine | - |
? | |
3.7.1.3 | L-kynurenine + H2O | - |
Homo sapiens | anthranilate + L-alanine | - |
? | |
3.7.1.3 | L-kynurenine + H2O | - |
Pseudomonas fluorescens | anthranilate + L-alanine | - |
? | |
3.7.1.3 | 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 | Pseudomonas fluorescens | ? | - |
? | |
3.7.1.3 | 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 | Homo sapiens | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.7.1.3 | HsKynase | - |
Homo sapiens |
3.7.1.3 | PfKynase | - |
Pseudomonas fluorescens |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.7.1.3 | 37 | - |
assay at | Homo sapiens |
3.7.1.3 | 37 | - |
assay at | Pseudomonas fluorescens |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.7.1.3 | 0.23 | - |
L-kynurenine | pH 8.0, 37°C, recombinant enzyme | Homo sapiens | |
3.7.1.3 | 0.23 | - |
3-fluoro-DL-kynurenine | pH 8.0, 37°C, recombinant enzyme | Homo sapiens | |
3.7.1.3 | 0.23 | - |
3,5-dibromo-L-kynurenine | pH 8.0, 37°C, recombinant enzyme | Pseudomonas fluorescens | |
3.7.1.3 | 0.33 | - |
3-methyl-DL-kynurenine | pH 8.0, 37°C, recombinant enzyme | Homo sapiens | |
3.7.1.3 | 0.47 | - |
5-chloro-L-kynurenine | pH 8.0, 37°C, recombinant enzyme | Homo sapiens | |
3.7.1.3 | 0.63 | - |
5-bromo-L-kynurenine | pH 8.0, 37°C, recombinant enzyme | Homo sapiens | |
3.7.1.3 | 0.67 | - |
3-chloro-DL-kynurenine | pH 8.0, 37°C, recombinant enzyme | Homo sapiens | |
3.7.1.3 | 0.71 | - |
3-chloro-DL-kynurenine | pH 8.0, 37°C, recombinant enzyme | Pseudomonas fluorescens | |
3.7.1.3 | 1 | - |
3-hydroxy-L-kynurenine | pH 8.0, 37°C, recombinant enzyme | Pseudomonas fluorescens | |
3.7.1.3 | 1.2 | - |
3,5-dibromo-L-kynurenine | pH 8.0, 37°C, recombinant enzyme | Homo sapiens | |
3.7.1.3 | 1.3 | - |
5-bromo-3-chloro-DL-kynurenine | pH 8.0, 37°C, recombinant enzyme | Homo sapiens | |
3.7.1.3 | 1.5 | - |
3-methyl-DL-kynurenine | pH 8.0, 37°C, recombinant enzyme | Pseudomonas fluorescens | |
3.7.1.3 | 1.9 | - |
3-bromo-L-kynurenine | pH 8.0, 37°C, recombinant enzyme | Homo sapiens | |
3.7.1.3 | 3.5 | - |
3-hydroxy-L-kynurenine | pH 8.0, 37°C, recombinant enzyme | Homo sapiens | |
3.7.1.3 | 6.3 | - |
5-bromo-3-chloro-DL-kynurenine | pH 8.0, 37°C, recombinant enzyme | Pseudomonas fluorescens | |
3.7.1.3 | 6.9 | - |
3-fluoro-DL-kynurenine | pH 8.0, 37°C, recombinant enzyme | Pseudomonas fluorescens | |
3.7.1.3 | 8.7 | - |
5-chloro-L-kynurenine | pH 8.0, 37°C, recombinant enzyme | Pseudomonas fluorescens | |
3.7.1.3 | 11 | - |
3-bromo-L-kynurenine | pH 8.0, 37°C, recombinant enzyme | Pseudomonas fluorescens | |
3.7.1.3 | 11.9 | - |
5-bromo-L-kynurenine | pH 8.0, 37°C, recombinant enzyme | Pseudomonas fluorescens | |
3.7.1.3 | 16 | - |
L-kynurenine | pH 8.0, 37°C, recombinant enzyme | Pseudomonas fluorescens |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.7.1.3 | 8 | - |
assay at | Homo sapiens |
3.7.1.3 | 8 | - |
assay at | Pseudomonas fluorescens |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
3.7.1.3 | pyridoxal 5'-phosphate | dependent on | Homo sapiens | |
3.7.1.3 | pyridoxal 5'-phosphate | dependent on | Pseudomonas fluorescens |
EC Number | General Information | Comment | Organism |
---|---|---|---|
3.7.1.3 | 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 | Homo sapiens |
3.7.1.3 | 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 | Pseudomonas fluorescens |
3.7.1.3 | additional information | modeling of 3,5-dibromo-L-kynurenine in the active site of the human enzyme | Homo sapiens |
EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.7.1.3 | 0.465 | - |
L-kynurenine | pH 8.0, 37°C, recombinant enzyme | Homo sapiens | |
3.7.1.3 | 1.1 | - |
5-chloro-L-kynurenine | pH 8.0, 37°C, recombinant enzyme | Homo sapiens | |
3.7.1.3 | 1.5 | - |
5-bromo-L-kynurenine | pH 8.0, 37°C, recombinant enzyme | Homo sapiens | |
3.7.1.3 | 1.8 | - |
3-methyl-DL-kynurenine | pH 8.0, 37°C, recombinant enzyme | Homo sapiens | |
3.7.1.3 | 2.5 | - |
3-hydroxy-L-kynurenine | pH 8.0, 37°C, recombinant enzyme | Pseudomonas fluorescens | |
3.7.1.3 | 2.7 | - |
3-fluoro-DL-kynurenine | pH 8.0, 37°C, recombinant enzyme | Homo sapiens | |
3.7.1.3 | 4.4 | - |
3-bromo-L-kynurenine | pH 8.0, 37°C, recombinant enzyme | Homo sapiens | |
3.7.1.3 | 5.5 | - |
3-bromo-L-kynurenine | pH 8.0, 37°C, recombinant enzyme | Pseudomonas fluorescens | |
3.7.1.3 | 6.5 | - |
5-bromo-3-chloro-DL-kynurenine | pH 8.0, 37°C, recombinant enzyme | Homo sapiens | |
3.7.1.3 | 7.9 | - |
3,5-dibromo-L-kynurenine | pH 8.0, 37°C, recombinant enzyme | Homo sapiens | |
3.7.1.3 | 8.2 | - |
3-chloro-DL-kynurenine | pH 8.0, 37°C, recombinant enzyme | Homo sapiens | |
3.7.1.3 | 11 | - |
3-chloro-DL-kynurenine | pH 8.0, 37°C, recombinant enzyme | Pseudomonas fluorescens | |
3.7.1.3 | 21 | - |
3,5-dibromo-L-kynurenine | pH 8.0, 37°C, recombinant enzyme | Pseudomonas fluorescens | |
3.7.1.3 | 22 | - |
3-methyl-DL-kynurenine | pH 8.0, 37°C, recombinant enzyme | Pseudomonas fluorescens | |
3.7.1.3 | 22 | - |
5-bromo-3-chloro-DL-kynurenine | pH 8.0, 37°C, recombinant enzyme | Pseudomonas fluorescens | |
3.7.1.3 | 90 | - |
3-fluoro-DL-kynurenine | pH 8.0, 37°C, recombinant enzyme | Pseudomonas fluorescens | |
3.7.1.3 | 123 | - |
3-hydroxy-L-kynurenine | pH 8.0, 37°C, recombinant enzyme | Homo sapiens | |
3.7.1.3 | 600 | - |
L-kynurenine | pH 8.0, 37°C, recombinant enzyme | Pseudomonas fluorescens | |
3.7.1.3 | 1800 | - |
5-chloro-L-kynurenine | pH 8.0, 37°C, recombinant enzyme | Pseudomonas fluorescens | |
3.7.1.3 | 3300 | - |
5-bromo-L-kynurenine | pH 8.0, 37°C, recombinant enzyme | Pseudomonas fluorescens |