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Literature summary for 3.7.1.3 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
Search for more literature for 3.7.1.3

Protein Variants

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

Inhibitors

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

KM Value [mM]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Pseudomonas fluorescens P83788
-
-

Substrates and Products (Substrate)

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

Turnover Number [1/s]

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

Cofactor

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

kcat/KM [mM/s]

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