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Literature summary extracted from

  • Phillips, R.; Crocker, M.; Lin, R.; Idowu, O.; McCannon, D.; Lima, S.
    The roles of Ser-36, Asp-132 and Asp-201 in the reaction of Pseudomonas fluorescens kynureninase (2019), Biochim. Biophys. Acta Proteins Proteom., 1867, 722-731 .
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
3.7.1.3 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 Pseudomonas fluorescens
3.7.1.3 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 Pseudomonas fluorescens
3.7.1.3 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 Pseudomonas fluorescens
3.7.1.3 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 Pseudomonas fluorescens
3.7.1.3 Y226F mutation results in very low activity, about 0.1%, with L-kynurenine Pseudomonas fluorescens

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.7.1.3 3-hydroxyhippurate
-
 Pseudomonas fluorescens
3.7.1.3 S-(2-aminophenyl)-L-cysteine S,S-dioxide potent competitive inhibitor Pseudomonas fluorescens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.7.1.3 0.0035
-
 L-kynurenine pH 8.0, 37°C, mutant enzyme S36A Pseudomonas fluorescens
3.7.1.3 0.009
-
 beta-benzoyl-L-alanine pH 8.0, 37°C, wild-type enzyme Pseudomonas fluorescens
3.7.1.3 0.011
-
 L-kynurenine pH 8.0, 37°C, mutant enzyme Y226F Pseudomonas fluorescens
3.7.1.3 0.025
-
 L-kynurenine pH 8.0, 37°C, wild-type enzyme Pseudomonas fluorescens
3.7.1.3 0.071
-
 O-benzoyl-L-serine pH 8.0, 37°C, mutant enzyme S36A Pseudomonas fluorescens
3.7.1.3 0.23
-
 O-benzoyl-L-serine pH 8.0, 37°C, wild-type enzyme Pseudomonas fluorescens
3.7.1.3 2.4
-
 O-benzoyl-L-serine pH 8.0, 37°C, mutant enzyme Y226F Pseudomonas fluorescens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.7.1.3 L-kynurenine + H2O Pseudomonas fluorescens
-
 anthranilate + L-alanine
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.7.1.3 Pseudomonas fluorescens P83788
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.7.1.3 beta-benzoyl-L-alanine + H2O
-
 Pseudomonas fluorescens benzoate + L-alanine
-
 ?
3.7.1.3 L-kynurenine + H2O
-
 Pseudomonas fluorescens anthranilate + L-alanine
-
 ?
3.7.1.3 O-benzoyl-L-serine + H2O
-
 Pseudomonas fluorescens benzoate + pyruvate + ammonium
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.7.1.3 0.0058
-
 L-kynurenine pH 8.0, 37°C, mutant enzyme Y226F Pseudomonas fluorescens
3.7.1.3 0.069
-
 L-kynurenine pH 8.0, 37°C, mutant enzyme S36A Pseudomonas fluorescens
3.7.1.3 0.1
-
 O-benzoyl-L-serine pH 8.0, 37°C, mutant enzyme Y226F Pseudomonas fluorescens
3.7.1.3 0.7
-
 beta-benzoyl-L-alanine pH 8.0, 37°C, wild-type enzyme Pseudomonas fluorescens
3.7.1.3 1.7
-
 O-benzoyl-L-serine pH 8.0, 37°C, mutant enzyme S36A Pseudomonas fluorescens
3.7.1.3 2.5
-
 O-benzoyl-L-serine pH 8.0, 37°C, wild-type enzyme Pseudomonas fluorescens
3.7.1.3 16
-
 L-kynurenine pH 8.0, 37°C, wild-type enzyme Pseudomonas fluorescens

Cofactor

EC Number Cofactor Comment Organism Structure
3.7.1.3 pyridoxal 5'-phosphate activity depends on Pseudomonas fluorescens

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.7.1.3 0.041
-
 O-benzoyl-L-serine pH 8.0, 37°C, mutant enzyme Y226F Pseudomonas fluorescens
3.7.1.3 0.53
-
 L-kynurenine pH 8.0, 37°C, mutant enzyme Y226F Pseudomonas fluorescens
3.7.1.3 11
-
 O-benzoyl-L-serine pH 8.0, 37°C, wild-type enzyme Pseudomonas fluorescens
3.7.1.3 20
-
 L-kynurenine pH 8.0, 37°C, mutant enzyme S36A Pseudomonas fluorescens
3.7.1.3 24
-
 O-benzoyl-L-serine pH 8.0, 37°C, mutant enzyme S36A Pseudomonas fluorescens
3.7.1.3 80
-
 beta-benzoyl-L-alanine pH 8.0, 37°C, wild-type enzyme Pseudomonas fluorescens
3.7.1.3 630
-
 L-kynurenine pH 8.0, 37°C, wild-type enzyme Pseudomonas fluorescens