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Literature summary for 2.6.1.7 extracted from

  • Asada, Y.; Sawa, Y.; Tanizawa, K.; Soda, K.
    Purification and characterization of yeast L-kynurenine aminotransferase with broad substrate specificity (1986), J. Biochem., 99, 1101-1110.
    View publication on PubMed
Search for more literature for 2.6.1.7

Activating Compound

Activating Compound Comment Organism Structure
pyridoxamine 5'-phosphate activation Hansenula schneggii

Crystallization (Commentary)

Crystallization (Comment) Organism
-
 Hansenula schneggii

General Stability

General Stability Organism
repeated freeze-thawing inactivates enzyme irriversible in dilute solution, below 0.1 mg/ml Hansenula schneggii

Inhibitors

Inhibitors Comment Organism Structure
3-Methyl-2-benzothiazolone hydrazone hydrochloride 0.1 mM, complete inhibition, reversible by pyridoxal phosphate Hansenula schneggii
4-chloromercuribenzoate 1 mM, 78% inhibition Hansenula schneggii
adipate 10 mM, 39% inhibition Hansenula schneggii
Dicarboxylic acids
-
 Hansenula schneggii
Hg2+ 0.1 mM, 89% inhibition Hansenula schneggii
hydroxylamine 0.1 mM, complete inhibition after 30 min Hansenula schneggii
iodoacetate 1 mM, 64% inhibition Hansenula schneggii
L-Cycloserine 0.1 mM, 88% inhibition, reversible by pyridoxal phosphate Hansenula schneggii
L-Penicillamine 0.1 mM, 62% inhibition, reversible by pyridoxal phosphate Hansenula schneggii
additional information not inhibited by EDTA, 2,2'-dipyridyl Hansenula schneggii
N-ethylmaleimide
-
 Hansenula schneggii
phenylhydrazine 0.1 mM, 81% inhibition, reversible by pyridoxal phosphate Hansenula schneggii
pimelate 10 mM, 53% inhibition Hansenula schneggii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0013
-
 pyridoxal 5'-phosphate pH 8.0, 37°C Hansenula schneggii
0.0032
-
 pyridoxamine 5'-phosphate pH 8.0, 37°C Hansenula schneggii
1
-
 2-oxoisocaproate pH 8.0, 37°C, cosubstrate L-kynurenine Hansenula schneggii
1.1
-
 2-oxoglutarate pH 8.0, 37°C, cosubstrate L-kynurenine Hansenula schneggii
1.2
-
 beta-phenylpyruvate pH 8.0, 37°C, cosubstrate L-kynurenine Hansenula schneggii
1.9
-
 3-(2-aminobenzoyl)-L-alanine pH 8.0, 37°C Hansenula schneggii
2.6
-
 L-tryptophan pH 8.0, 37°C, cosubstrate 2-oxoglutarate Hansenula schneggii
5
-
 L-methionine pH 8.0, 37°C, cosubstrate 2-oxoglutarate Hansenula schneggii
5
-
 L-leucine pH 8.0, 37°C, cosubstrate 2-oxoglutarate Hansenula schneggii

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
 amino acid composition Hansenula schneggii
52000
-
 2 * 52000, SDS-PAGE Hansenula schneggii
98000
-
 sedimentation equilibrium Hansenula schneggii
106000
-
 gel filtration Hansenula schneggii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-kynurenine + 2-oxoglutarate Hansenula schneggii initial reaction in quinaldine pathway of kynurenine catabolism kynurenic acid + L-glutamate + H2O
-
 ?
L-kynurenine + 2-oxoglutarate Hansenula schneggii inducible enzyme of tryptophan catabolism kynurenic acid + L-glutamate + H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Hansenula schneggii
-
 yeast
-

Purification (Commentary)

Purification (Comment) Organism
polyethyleneimine, DEAE-cellulose, Bio-Gel P-300, hydroxyapatite, crystallization Hansenula schneggii

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
16.9
-
-
 Hansenula schneggii

Storage Stability

Storage Stability Organism
-20°C, at protein concentrations above 0.6 mg/ml, 0.02 mM pyridoxal phosphate, 0.01% mercaptoethanol, several weeks, no loss of activity Hansenula schneggii
4°C, crystalline enzyme as suspension in 70% saturated ammonium sulfate, pH 7.2, more than 6 months Hansenula schneggii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-kynurenine + 2-oxobutyrate less effective than 2-oxoglutarate Hansenula schneggii kynurenic acid + 2-aminobutanoate + H2O
-
 ?
L-kynurenine + 2-oxoglutarate broad specificity Hansenula schneggii kynurenic acid + L-glutamate + H2O
-
 ir
L-kynurenine + 2-oxoglutarate best substrates Hansenula schneggii kynurenic acid + L-glutamate + H2O
-
 ir
L-kynurenine + 2-oxoglutarate initial reaction in quinaldine pathway of kynurenine catabolism Hansenula schneggii kynurenic acid + L-glutamate + H2O
-
 ?
L-kynurenine + 2-oxoglutarate inducible enzyme of tryptophan catabolism Hansenula schneggii kynurenic acid + L-glutamate + H2O
-
 ?
L-kynurenine + 2-oxohexanoate
-
 Hansenula schneggii kynurenic acid + L-norleucine + H2O
-
 ?
L-kynurenine + 2-oxoisohexanoate
-
 Hansenula schneggii kynurenic acid + 2-aminoisohexanoate + H2O
-
 ?
L-kynurenine + 2-oxopentanoate less effective than 2-oxoglutarate Hansenula schneggii kynurenic acid + L-norvaline + H2O
-
 ?
L-kynurenine + 3-phenyl-2-oxopropanoate
-
 Hansenula schneggii kynurenic acid + L-phenylalanine + H2O
-
 ?
L-kynurenine + 4-methylsulfanyl-2-oxobutyrate
-
 Hansenula schneggii kynurenic acid + L-methionine + H2O
-
 ?
L-leucine + 2-oxoglutarate
-
 Hansenula schneggii 4-methyl-2-oxopentanoate + L-glutamate
-
 ?

Subunits

Subunits Comment Organism
dimer 2 * 52000, SDS-PAGE Hansenula schneggii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60
-
-
 Hansenula schneggii

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
20 60 linear increase of activity Hansenula schneggii

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50
-
 and below, 5 min stable between pH 6.0 and pH 10.0 Hansenula schneggii
65
-
 above, rapid inactivation Hansenula schneggii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
additional information
-
 pI: 4.95 Hansenula schneggii
8
-
-
 Hansenula schneggii

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate Km-value: 0.0013 mM Hansenula schneggii
pyridoxal 5'-phosphate required for activity, 2 mol per mol holoenzyme Hansenula schneggii

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
9.5
-
 pimelate
-
 Hansenula schneggii
13
-
 adipate
-
 Hansenula schneggii