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Literature summary extracted from

  • 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 (2004), Biochemistry, 43, 3230-3237.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.7.1.3 expression in Escherichia coli Pseudomonas fluorescens
3.7.1.3 into vector pTZKYN and transformed in Escherichia coli XL-1 Blue cells Pseudomonas fluorescens

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.7.1.3 (2S)-2-amino-4-oxo-4-phenylbutanoic acid competitive inhibitor of the reaction of L-kynurenine with the enzyme Pseudomonas fluorescens
3.7.1.3 beta-benzoyl-L-alanine competitive inhibition, at 25ºC, pH 7.8 Pseudomonas fluorescens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.7.1.3 0.008
-
 beta-benzoyl-L-alanine at 25ºC, pH 7.8 Pseudomonas fluorescens
3.7.1.3 0.03
-
 L-kynurenine at 25ºC, pH 7.8 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 L-tryptophan metabolism anthranilate + L-alanine
-
 ?

Organism

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

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.7.1.3 no modification
-
 Pseudomonas fluorescens

Purification (Commentary)

EC Number Purification (Comment) Organism
3.7.1.3
-
 Pseudomonas fluorescens
3.7.1.3 by chromatography on phenyl-Sepharose Pseudomonas fluorescens

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.7.1.3 culture medium
-
 Pseudomonas fluorescens
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.7.1.3 additional information
-
 19 U/mg protein Pseudomonas fluorescens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.7.1.3 (2S)-2-amino-4-oxo-4-phenylbutanoic acid + H2O the rate-determining step is Cbeta-Cgamma bond cleavage Pseudomonas fluorescens benzoate + L-alanine
-
 ?
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 L-kynurenine + H2O L-tryptophan metabolism Pseudomonas fluorescens anthranilate + L-alanine
-
 ?
3.7.1.3 L-kynurenine + H2O the rate-determining step is to be deprotonation of the pyruvate-ketimine intermediate Pseudomonas fluorescens anthranilate + L-alanine
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.7.1.3 L-kynurenine hydrolase
-
 Pseudomonas fluorescens

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.7.1.3 0.7
-
 beta-benzoyl-L-alanine
-
 Pseudomonas fluorescens
3.7.1.3 0.7
-
 (2S)-2-amino-4-oxo-4-phenylbutanoic acid at pH 7.8 Pseudomonas fluorescens
3.7.1.3 16
-
 L-kynurenine
-
 Pseudomonas fluorescens
3.7.1.3 16
-
 L-kynurenine at pH 7.8 Pseudomonas fluorescens

Cofactor

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

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.7.1.3 0.01
-
 beta-benzoyl-L-alanine at 25ºC, pH 7.8 Pseudomonas fluorescens
3.7.1.3 0.01
-
 (2S)-2-amino-4-oxo-4-phenylbutanoic acid reaction of L-kynurenine with the enzyme Pseudomonas fluorescens