Literature summary extracted from

Tanizawa, K.; Asada, Y.; Soda, K.
L-Kynurenine transaminase from Hansenula schneggii (1985), Methods Enzymol., 113, 90-95.

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
2.6.1.7	-	Hansenula schneggii

Inhibitors

EC Number	Inhibitors	Comment	Organism
2.6.1.7	4-chloromercuribenzoate	-	Hansenula schneggii
2.6.1.7	Dicarboxylic acids	-	Hansenula schneggii
2.6.1.7	Hg2+	-	Hansenula schneggii
2.6.1.7	iodoacetate	-	Hansenula schneggii
2.6.1.7	additional information	not inhibited by EDTA, 2,2'-dipyridyl	Hansenula schneggii
2.6.1.7	N-ethylmaleimide	-	Hansenula schneggii

KM Value [mM]

EC Number	KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism
2.6.1.7	1	-	2-oxoisocaproate	-	Hansenula schneggii
2.6.1.7	1.1	-	2-oxoglutarate	-	Hansenula schneggii
2.6.1.7	1.2	-	beta-phenylpyruvate	-	Hansenula schneggii
2.6.1.7	2.6	-	L-tryptophan	-	Hansenula schneggii
2.6.1.7	5	-	L-methionine	-	Hansenula schneggii
2.6.1.7	5	-	L-leucine	-	Hansenula schneggii

Molecular Weight [Da]

EC Number	Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
2.6.1.7	98000	-	sedimentation equilibrium	Hansenula schneggii
2.6.1.7	102000	-	native PAGE	Hansenula schneggii
2.6.1.7	106000	-	gel filtration	Hansenula schneggii

Organism

EC Number	Organism	UniProt	Comment	Textmining
2.6.1.7	Cutaneotrichosporon cutaneum	-	low activity	-
2.6.1.7	Debaryomyces hansenii	-	yeast	-
2.6.1.7	Diutina rugosa	-	low activity	-
2.6.1.7	Hansenula schneggii	-	yeast	-
2.6.1.7	Kluyveromyces marxianus	-	-	-
2.6.1.7	Naganishia albida	-	low activity	-
2.6.1.7	Saccharomyces cerevisiae	-	-	-
2.6.1.7	Saccharomyces fragilis	-	low activity	-
2.6.1.7	Schwanniomyces occidentalis	-	low activity	-
2.6.1.7	Schwanniomyces polymorphus	-	yeast	-
2.6.1.7	Torulaspora globosa	-	low activity	-

Purification (Commentary)

EC Number	Purification (Comment)	Organism
2.6.1.7	-	Hansenula schneggii

Specific Activity [micromol/min/mg]

EC Number	Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
2.6.1.7	16.9	-	-	Hansenula schneggii

Storage Stability

EC Number	Storage Stability	Organism
2.6.1.7	-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
2.6.1.7	4°C, crystalline enzyme as suspension in 70% saturated ammonium sulfate, pH 7.2, more than 6 months	Hansenula schneggii

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
2.6.1.7	L-2-aminohexane-1,6-dioate + 2-oxoglutarate	at about 60% the rate of L-kynurenine	Hansenula schneggii	2-oxohexane-1,6-dioate + L-glutamate	-	?
2.6.1.7	L-3-hydroxykynurenine + 2-oxoglutarate	at about 45% the rate of L-kynurenine	Hansenula schneggii	xanthurenic acid + L-glutamate	-	?
2.6.1.7	L-kynurenine + 2-oxoglutarate	-	Saccharomyces fragilis	kynurenic acid + L-glutamate + H2O	-	?
2.6.1.7	L-kynurenine + 2-oxoglutarate	-	Cutaneotrichosporon cutaneum	kynurenic acid + L-glutamate + H2O	-	?
2.6.1.7	L-kynurenine + 2-oxoglutarate	-	Schwanniomyces occidentalis	kynurenic acid + L-glutamate + H2O	-	?
2.6.1.7	L-kynurenine + 2-oxoglutarate	-	Diutina rugosa	kynurenic acid + L-glutamate + H2O	-	?
2.6.1.7	L-kynurenine + 2-oxoglutarate	-	Naganishia albida	kynurenic acid + L-glutamate + H2O	-	?
2.6.1.7	L-kynurenine + 2-oxoglutarate	-	Torulaspora globosa	kynurenic acid + L-glutamate + H2O	-	?
2.6.1.7	L-kynurenine + 2-oxoglutarate	-	Saccharomyces cerevisiae	kynurenic acid + L-glutamate + H2O	via o-aminobenzoylpyruvic acid which is immediately converted to the intramolecularly dehydrated and cyclized form kynurenic acid	?
2.6.1.7	L-kynurenine + 2-oxoglutarate	-	Kluyveromyces marxianus	kynurenic acid + L-glutamate + H2O	via o-aminobenzoylpyruvic acid which is immediately converted to the intramolecularly dehydrated and cyclized form kynurenic acid	?
2.6.1.7	L-kynurenine + 2-oxoglutarate	-	Debaryomyces hansenii	kynurenic acid + L-glutamate + H2O	via o-aminobenzoylpyruvic acid which is immediately converted to the intramolecularly dehydrated and cyclized form kynurenic acid	?
2.6.1.7	L-kynurenine + 2-oxoglutarate	-	Schwanniomyces polymorphus	kynurenic acid + L-glutamate + H2O	via o-aminobenzoylpyruvic acid which is immediately converted to the intramolecularly dehydrated and cyclized form kynurenic acid	?
2.6.1.7	L-kynurenine + 2-oxoglutarate	best substrates	Hansenula schneggii	kynurenic acid + L-glutamate + H2O	via o-aminobenzoylpyruvic acid which is immediately converted to the intramolecularly dehydrated and cyclized form kynurenic acid	?
2.6.1.7	L-kynurenine + 2-oxohexanedioate	-	Hansenula schneggii	kynurenic acid + 2-aminohexanedioate + H2O	-	?
2.6.1.7	L-kynurenine + 2-oxoisohexanoate	-	Hansenula schneggii	kynurenic acid + 2-aminoisohexanoate + H2O	-	?
2.6.1.7	L-kynurenine + 3-indole-2-oxopropanoate	-	Hansenula schneggii	kynurenic acid + L-tryptophan + H2O	-	?
2.6.1.7	L-kynurenine + 3-phenyl-2-oxopropanoate	-	Hansenula schneggii	kynurenic acid + L-phenylalanine + H2O	-	?
2.6.1.7	L-kynurenine + 4-methylsulfanyl-2-oxobutyrate	-	Hansenula schneggii	kynurenic acid + L-methionine + H2O	-	?
2.6.1.7	L-leucine + 2-oxoglutarate	at about 85% the rate of L-kynurenine	Hansenula schneggii	4-methyl-2-oxopentanoate + L-glutamate	-	?
2.6.1.7	L-methionine + 2-oxoglutarate	at about 36% the rate of L-kynurenine	Hansenula schneggii	4-methylsulfanyl-2-oxobutanoate + glutamate	-	?
2.6.1.7	L-tryptophan + 2-oxoglutarate	at about 60% the rate of L-kynurenine	Hansenula schneggii	3-indole-2-oxopropanoate + L-glutamate	-	?

Temperature Optimum [°C]

EC Number	Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
2.6.1.7	37	-	assay at	Hansenula schneggii

Temperature Stability [°C]

EC Number	Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
2.6.1.7	50	-	and below, 5 min stable between pH 6.0 and pH 10.0	Hansenula schneggii

Cofactor

EC Number	Cofactor	Comment	Organism	Structure
2.6.1.7	pyridoxal 5'-phosphate	-	Hansenula schneggii