UniProt functional annotation for Q17CS8



	UniProt functional annotation for Q17CS8

UniProt code: Q17CS8.

Organism: Aedes aegypti (Yellowfever mosquito) (Culex aegypti).

Taxonomy: Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae; Culicinae; Aedini; Aedes; Stegomyia.

Function: Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA) (PubMed:12110301, PubMed:15556614). Also catalyzes the irreversible transamination of several amino acids including cysteine, tyrosine, glutamine, methionine, histidine and phenylalanine (PubMed:15556614). Can use various keto-acids as the amino group acceptor (PubMed:15556614, PubMed:12110301). {ECO:0000269|PubMed:12110301, ECO:0000269|PubMed:15556614}.

Catalytic activity: Reaction=L-kynurenine + pyruvate = H2O + kynurenate + L-alanine; Xref=Rhea:RHEA:65916, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, ChEBI:CHEBI:57959, ChEBI:CHEBI:57972, ChEBI:CHEBI:58454; Evidence={ECO:0000269|PubMed:12110301, ECO:0000269|PubMed:15556614};

Catalytic activity: Reaction=2-oxoglutarate + L-kynurenine = H2O + kynurenate + L- glutamate; Xref=Rhea:RHEA:65560, ChEBI:CHEBI:15377, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57959, ChEBI:CHEBI:58454; EC=2.6.1.7; Evidence={ECO:0000269|PubMed:12110301, ECO:0000269|PubMed:15556614};

Catalytic activity: Reaction=glyoxylate + L-kynurenine = glycine + H2O + kynurenate; Xref=Rhea:RHEA:65896, ChEBI:CHEBI:15377, ChEBI:CHEBI:36655, ChEBI:CHEBI:57305, ChEBI:CHEBI:57959, ChEBI:CHEBI:58454; EC=2.6.1.63; Evidence={ECO:0000269|PubMed:15556614};

Catalytic activity: Reaction=2-oxobutanoate + L-kynurenine = (2S)-2-aminobutanoate + H2O + kynurenate; Xref=Rhea:RHEA:66044, ChEBI:CHEBI:15377, ChEBI:CHEBI:16763, ChEBI:CHEBI:57959, ChEBI:CHEBI:58454, ChEBI:CHEBI:74359; Evidence={ECO:0000269|PubMed:15556614};

Catalytic activity: Reaction=2-oxobutanoate + L-cysteine = (2S)-2-aminobutanoate + 2-oxo-3- sulfanylpropanoate; Xref=Rhea:RHEA:66108, ChEBI:CHEBI:16763, ChEBI:CHEBI:35235, ChEBI:CHEBI:57678, ChEBI:CHEBI:74359; Evidence={ECO:0000269|PubMed:15556614};

Catalytic activity: Reaction=2-oxobutanoate + L-tyrosine = (2S)-2-aminobutanoate + 3-(4- hydroxyphenyl)pyruvate; Xref=Rhea:RHEA:66112, ChEBI:CHEBI:16763, ChEBI:CHEBI:36242, ChEBI:CHEBI:58315, ChEBI:CHEBI:74359; Evidence={ECO:0000269|PubMed:15556614};

Catalytic activity: Reaction=2-oxobutanoate + L-glutamine = (2S)-2-aminobutanoate + 2- oxoglutaramate; Xref=Rhea:RHEA:66116, ChEBI:CHEBI:16763, ChEBI:CHEBI:16769, ChEBI:CHEBI:58359, ChEBI:CHEBI:74359; Evidence={ECO:0000269|PubMed:15556614};

Catalytic activity: Reaction=2-oxobutanoate + L-methionine = (2S)-2-aminobutanoate + 4- methylsulfanyl-2-oxobutanoate; Xref=Rhea:RHEA:66120, ChEBI:CHEBI:16723, ChEBI:CHEBI:16763, ChEBI:CHEBI:57844, ChEBI:CHEBI:74359; Evidence={ECO:0000269|PubMed:15556614};

Catalytic activity: Reaction=2-oxobutanoate + L-histidine = (2S)-2-aminobutanoate + 3- (imidazol-5-yl)pyruvate; Xref=Rhea:RHEA:66124, ChEBI:CHEBI:16763, ChEBI:CHEBI:57595, ChEBI:CHEBI:58133, ChEBI:CHEBI:74359; Evidence={ECO:0000269|PubMed:15556614};

Catalytic activity: Reaction=2-oxobutanoate + L-phenylalanine = (2S)-2-aminobutanoate + 3- phenylpyruvate; Xref=Rhea:RHEA:66128, ChEBI:CHEBI:16763, ChEBI:CHEBI:18005, ChEBI:CHEBI:58095, ChEBI:CHEBI:74359; Evidence={ECO:0000269|PubMed:15556614};

Catalytic activity: Reaction=indole-3-pyruvate + L-kynurenine = H2O + kynurenate + L- tryptophan; Xref=Rhea:RHEA:66052, ChEBI:CHEBI:15377, ChEBI:CHEBI:17640, ChEBI:CHEBI:57912, ChEBI:CHEBI:57959, ChEBI:CHEBI:58454; Evidence={ECO:0000269|PubMed:15556614};

Catalytic activity: Reaction=2-oxohexanoate + L-kynurenine = H2O + kynurenate + L-2- aminohexanoate; Xref=Rhea:RHEA:66060, ChEBI:CHEBI:15377, ChEBI:CHEBI:35177, ChEBI:CHEBI:57959, ChEBI:CHEBI:58454, ChEBI:CHEBI:58455; Evidence={ECO:0000269|PubMed:15556614};

Catalytic activity: Reaction=4-methyl-2-oxopentanoate + L-kynurenine = H2O + kynurenate + L-leucine; Xref=Rhea:RHEA:66068, ChEBI:CHEBI:15377, ChEBI:CHEBI:17865, ChEBI:CHEBI:57427, ChEBI:CHEBI:57959, ChEBI:CHEBI:58454; Evidence={ECO:0000269|PubMed:15556614};

Catalytic activity: Reaction=2-oxopentanoate + L-kynurenine = H2O + kynurenate + L-2- aminopentanoate; Xref=Rhea:RHEA:66076, ChEBI:CHEBI:15377, ChEBI:CHEBI:28644, ChEBI:CHEBI:57959, ChEBI:CHEBI:58441, ChEBI:CHEBI:58454; Evidence={ECO:0000269|PubMed:15556614};

Catalytic activity: Reaction=L-kynurenine + oxaloacetate = H2O + kynurenate + L-aspartate; Xref=Rhea:RHEA:66084, ChEBI:CHEBI:15377, ChEBI:CHEBI:16452, ChEBI:CHEBI:29991, ChEBI:CHEBI:57959, ChEBI:CHEBI:58454; Evidence={ECO:0000269|PubMed:15556614};

Catalytic activity: Reaction=3-phenylpyruvate + L-kynurenine = H2O + kynurenate + L- phenylalanine; Xref=Rhea:RHEA:66092, ChEBI:CHEBI:15377, ChEBI:CHEBI:18005, ChEBI:CHEBI:57959, ChEBI:CHEBI:58095, ChEBI:CHEBI:58454; Evidence={ECO:0000269|PubMed:15556614};

Catalytic activity: Reaction=3-(4-hydroxyphenyl)pyruvate + L-kynurenine = H2O + kynurenate + L-tyrosine; Xref=Rhea:RHEA:66100, ChEBI:CHEBI:15377, ChEBI:CHEBI:36242, ChEBI:CHEBI:57959, ChEBI:CHEBI:58315, ChEBI:CHEBI:58454; Evidence={ECO:0000269|PubMed:15556614};

Cofactor: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:15853804, ECO:0000269|PubMed:18186649};

Activity regulation: Competitive inhibition of L-kynurenine transamination by glutamine, methionine and histidine but not by tyrosine and phenylalanine (PubMed:15556614). Cysteine concentration between 0.31-2.5 mM increases L-kynurenine transamination while concentration above 2.5 mM inhibits L-kynurenine transamination (PubMed:15556614). Keto-acids as amino acceptors modulate the transamination activity toward L-kynurenine (PubMed:15556614). {ECO:0000269|PubMed:15556614}.

Biophysicochemical properties: Kinetic parameters: KM=1.3 mM for cysteine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate) {ECO:0000269|PubMed:15556614}; KM=0.9 mM for tyrosine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate) {ECO:0000269|PubMed:15556614}; KM=3.8 mM for glutamine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate) {ECO:0000269|PubMed:15556614}; KM=1.4 mM for methionine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate) {ECO:0000269|PubMed:15556614}; KM=1.5 mM for histidine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate) {ECO:0000269|PubMed:15556614}; KM=3.5 mM for phenylalanine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate) {ECO:0000269|PubMed:15556614}; KM=4.3 mM for kynurenine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate) {ECO:0000269|PubMed:15556614}; KM=6.1 mM for asparagine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate) {ECO:0000269|PubMed:15556614}; KM=12.9 mM for tryptophan (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate) {ECO:0000269|PubMed:15556614}; KM=34.5 mM for leucine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate) {ECO:0000269|PubMed:15556614}; KM=32.7 mM for serine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate) {ECO:0000269|PubMed:15556614}; KM=246 mM for alanine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate) {ECO:0000269|PubMed:15556614}; KM=92.7 mM for amino-butyrate (at 45 degrees Celsius, at pH 8.5 and with pyruvate as cosubstrate) {ECO:0000269|PubMed:15556614}; Note=kcat is 206 min(-1) for cysteine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate) (PubMed:15556614). kcat is 139 min(-1) for tyrosine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate) (PubMed:15556614). kcat is 561 min(-1) for glutamine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate) (PubMed:15556614). kcat is 163 min(-1) for methionine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate) (PubMed:15556614). kcat is 168 min(-1) for histidine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate) (PubMed:15556614). kcat is 283 min(-1) for cysteine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate) (PubMed:15556614). kcat is 172 min(-1) for kynurenine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate) (PubMed:15556614). kcat is 230 min(-1) for asparagine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate) (PubMed:15556614). kcat is 283 min(-1) for tryptophan (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate) (PubMed:15556614). kcat is 758 min(-1) for leucine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate) (PubMed:15556614). kcat is 345 min(-1) for serine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate) (PubMed:15556614). kcat is 1540 min(-1) for alanine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate) (PubMed:15556614). kcat is 317 min(-1) for amino-butyrate (at 45 degrees Celsius, at pH 8.5 and with pyruvate as cosubstrate) (PubMed:15556614). {ECO:0000269|PubMed:15556614}; pH dependence: Optimum pH is 8.5 and 10 (with pyruvate as cosubstrate). {ECO:0000269|PubMed:12110301}; Temperature dependence: Optimum temperature is 60 degrees Celsius (at pH 8.5 and with pyruvate as cosubstrate). {ECO:0000269|PubMed:12110301};

Pathway: Amino-acid degradation; L-kynurenine degradation; kynurenate from L-kynurenine: step 1/2. {ECO:0000269|PubMed:12110301, ECO:0000269|PubMed:15556614}.

Subunit: Homodimer. {ECO:0000305|PubMed:12110301, ECO:0000305|PubMed:15853804, ECO:0000305|PubMed:18186649}.

Subcellular location: Mitochondrion {ECO:0000255}.

Tissue specificity: Expressed in developing ovaries (PubMed:12110301). Expressed at high levels in the head (PubMed:12110301). {ECO:0000269|PubMed:12110301}.

Developmental stage: Expressed in larvae, pupae and adults (PubMed:12110301). Expressed at low levels in larvae, then expression increases at the beginning of pupal development to reach high expression levels in adults (PubMed:12110301). {ECO:0000269|PubMed:12110301}.

Similarity: Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
Taxonomy:		Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae; Culicinae; Aedini; Aedes; Stegomyia.



Function:		Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA) (PubMed:12110301, PubMed:15556614). Also catalyzes the irreversible transamination of several amino acids including cysteine, tyrosine, glutamine, methionine, histidine and phenylalanine (PubMed:15556614). Can use various keto-acids as the amino group acceptor (PubMed:15556614, PubMed:12110301). {ECO:0000269\|PubMed:12110301, ECO:0000269\|PubMed:15556614}.


Catalytic activity:		Reaction=L-kynurenine + pyruvate = H2O + kynurenate + L-alanine; Xref=Rhea:RHEA:65916, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, ChEBI:CHEBI:57959, ChEBI:CHEBI:57972, ChEBI:CHEBI:58454; Evidence={ECO:0000269\|PubMed:12110301, ECO:0000269\|PubMed:15556614};
Catalytic activity:		Reaction=2-oxoglutarate + L-kynurenine = H2O + kynurenate + L- glutamate; Xref=Rhea:RHEA:65560, ChEBI:CHEBI:15377, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57959, ChEBI:CHEBI:58454; EC=2.6.1.7; Evidence={ECO:0000269\|PubMed:12110301, ECO:0000269\|PubMed:15556614};
Catalytic activity:		Reaction=glyoxylate + L-kynurenine = glycine + H2O + kynurenate; Xref=Rhea:RHEA:65896, ChEBI:CHEBI:15377, ChEBI:CHEBI:36655, ChEBI:CHEBI:57305, ChEBI:CHEBI:57959, ChEBI:CHEBI:58454; EC=2.6.1.63; Evidence={ECO:0000269\|PubMed:15556614};
Catalytic activity:		Reaction=2-oxobutanoate + L-kynurenine = (2S)-2-aminobutanoate + H2O + kynurenate; Xref=Rhea:RHEA:66044, ChEBI:CHEBI:15377, ChEBI:CHEBI:16763, ChEBI:CHEBI:57959, ChEBI:CHEBI:58454, ChEBI:CHEBI:74359; Evidence={ECO:0000269\|PubMed:15556614};
Catalytic activity:		Reaction=2-oxobutanoate + L-cysteine = (2S)-2-aminobutanoate + 2-oxo-3- sulfanylpropanoate; Xref=Rhea:RHEA:66108, ChEBI:CHEBI:16763, ChEBI:CHEBI:35235, ChEBI:CHEBI:57678, ChEBI:CHEBI:74359; Evidence={ECO:0000269\|PubMed:15556614};
Catalytic activity:		Reaction=2-oxobutanoate + L-tyrosine = (2S)-2-aminobutanoate + 3-(4- hydroxyphenyl)pyruvate; Xref=Rhea:RHEA:66112, ChEBI:CHEBI:16763, ChEBI:CHEBI:36242, ChEBI:CHEBI:58315, ChEBI:CHEBI:74359; Evidence={ECO:0000269\|PubMed:15556614};
Catalytic activity:		Reaction=2-oxobutanoate + L-glutamine = (2S)-2-aminobutanoate + 2- oxoglutaramate; Xref=Rhea:RHEA:66116, ChEBI:CHEBI:16763, ChEBI:CHEBI:16769, ChEBI:CHEBI:58359, ChEBI:CHEBI:74359; Evidence={ECO:0000269\|PubMed:15556614};
Catalytic activity:		Reaction=2-oxobutanoate + L-methionine = (2S)-2-aminobutanoate + 4- methylsulfanyl-2-oxobutanoate; Xref=Rhea:RHEA:66120, ChEBI:CHEBI:16723, ChEBI:CHEBI:16763, ChEBI:CHEBI:57844, ChEBI:CHEBI:74359; Evidence={ECO:0000269\|PubMed:15556614};
Catalytic activity:		Reaction=2-oxobutanoate + L-histidine = (2S)-2-aminobutanoate + 3- (imidazol-5-yl)pyruvate; Xref=Rhea:RHEA:66124, ChEBI:CHEBI:16763, ChEBI:CHEBI:57595, ChEBI:CHEBI:58133, ChEBI:CHEBI:74359; Evidence={ECO:0000269\|PubMed:15556614};
Catalytic activity:		Reaction=2-oxobutanoate + L-phenylalanine = (2S)-2-aminobutanoate + 3- phenylpyruvate; Xref=Rhea:RHEA:66128, ChEBI:CHEBI:16763, ChEBI:CHEBI:18005, ChEBI:CHEBI:58095, ChEBI:CHEBI:74359; Evidence={ECO:0000269\|PubMed:15556614};
Catalytic activity:		Reaction=indole-3-pyruvate + L-kynurenine = H2O + kynurenate + L- tryptophan; Xref=Rhea:RHEA:66052, ChEBI:CHEBI:15377, ChEBI:CHEBI:17640, ChEBI:CHEBI:57912, ChEBI:CHEBI:57959, ChEBI:CHEBI:58454; Evidence={ECO:0000269\|PubMed:15556614};
Catalytic activity:		Reaction=2-oxohexanoate + L-kynurenine = H2O + kynurenate + L-2- aminohexanoate; Xref=Rhea:RHEA:66060, ChEBI:CHEBI:15377, ChEBI:CHEBI:35177, ChEBI:CHEBI:57959, ChEBI:CHEBI:58454, ChEBI:CHEBI:58455; Evidence={ECO:0000269\|PubMed:15556614};
Catalytic activity:		Reaction=4-methyl-2-oxopentanoate + L-kynurenine = H2O + kynurenate + L-leucine; Xref=Rhea:RHEA:66068, ChEBI:CHEBI:15377, ChEBI:CHEBI:17865, ChEBI:CHEBI:57427, ChEBI:CHEBI:57959, ChEBI:CHEBI:58454; Evidence={ECO:0000269\|PubMed:15556614};
Catalytic activity:		Reaction=2-oxopentanoate + L-kynurenine = H2O + kynurenate + L-2- aminopentanoate; Xref=Rhea:RHEA:66076, ChEBI:CHEBI:15377, ChEBI:CHEBI:28644, ChEBI:CHEBI:57959, ChEBI:CHEBI:58441, ChEBI:CHEBI:58454; Evidence={ECO:0000269\|PubMed:15556614};
Catalytic activity:		Reaction=L-kynurenine + oxaloacetate = H2O + kynurenate + L-aspartate; Xref=Rhea:RHEA:66084, ChEBI:CHEBI:15377, ChEBI:CHEBI:16452, ChEBI:CHEBI:29991, ChEBI:CHEBI:57959, ChEBI:CHEBI:58454; Evidence={ECO:0000269\|PubMed:15556614};
Catalytic activity:		Reaction=3-phenylpyruvate + L-kynurenine = H2O + kynurenate + L- phenylalanine; Xref=Rhea:RHEA:66092, ChEBI:CHEBI:15377, ChEBI:CHEBI:18005, ChEBI:CHEBI:57959, ChEBI:CHEBI:58095, ChEBI:CHEBI:58454; Evidence={ECO:0000269\|PubMed:15556614};
Catalytic activity:		Reaction=3-(4-hydroxyphenyl)pyruvate + L-kynurenine = H2O + kynurenate + L-tyrosine; Xref=Rhea:RHEA:66100, ChEBI:CHEBI:15377, ChEBI:CHEBI:36242, ChEBI:CHEBI:57959, ChEBI:CHEBI:58315, ChEBI:CHEBI:58454; Evidence={ECO:0000269\|PubMed:15556614};
Cofactor:		Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269\|PubMed:15853804, ECO:0000269\|PubMed:18186649};
Activity regulation:		Competitive inhibition of L-kynurenine transamination by glutamine, methionine and histidine but not by tyrosine and phenylalanine (PubMed:15556614). Cysteine concentration between 0.31-2.5 mM increases L-kynurenine transamination while concentration above 2.5 mM inhibits L-kynurenine transamination (PubMed:15556614). Keto-acids as amino acceptors modulate the transamination activity toward L-kynurenine (PubMed:15556614). {ECO:0000269\|PubMed:15556614}.
Biophysicochemical properties:		Kinetic parameters: KM=1.3 mM for cysteine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate) {ECO:0000269\|PubMed:15556614}; KM=0.9 mM for tyrosine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate) {ECO:0000269\|PubMed:15556614}; KM=3.8 mM for glutamine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate) {ECO:0000269\|PubMed:15556614}; KM=1.4 mM for methionine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate) {ECO:0000269\|PubMed:15556614}; KM=1.5 mM for histidine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate) {ECO:0000269\|PubMed:15556614}; KM=3.5 mM for phenylalanine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate) {ECO:0000269\|PubMed:15556614}; KM=4.3 mM for kynurenine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate) {ECO:0000269\|PubMed:15556614}; KM=6.1 mM for asparagine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate) {ECO:0000269\|PubMed:15556614}; KM=12.9 mM for tryptophan (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate) {ECO:0000269\|PubMed:15556614}; KM=34.5 mM for leucine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate) {ECO:0000269\|PubMed:15556614}; KM=32.7 mM for serine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate) {ECO:0000269\|PubMed:15556614}; KM=246 mM for alanine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate) {ECO:0000269\|PubMed:15556614}; KM=92.7 mM for amino-butyrate (at 45 degrees Celsius, at pH 8.5 and with pyruvate as cosubstrate) {ECO:0000269\|PubMed:15556614}; Note=kcat is 206 min(-1) for cysteine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate) (PubMed:15556614). kcat is 139 min(-1) for tyrosine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate) (PubMed:15556614). kcat is 561 min(-1) for glutamine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate) (PubMed:15556614). kcat is 163 min(-1) for methionine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate) (PubMed:15556614). kcat is 168 min(-1) for histidine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate) (PubMed:15556614). kcat is 283 min(-1) for cysteine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate) (PubMed:15556614). kcat is 172 min(-1) for kynurenine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate) (PubMed:15556614). kcat is 230 min(-1) for asparagine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate) (PubMed:15556614). kcat is 283 min(-1) for tryptophan (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate) (PubMed:15556614). kcat is 758 min(-1) for leucine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate) (PubMed:15556614). kcat is 345 min(-1) for serine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate) (PubMed:15556614). kcat is 1540 min(-1) for alanine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate) (PubMed:15556614). kcat is 317 min(-1) for amino-butyrate (at 45 degrees Celsius, at pH 8.5 and with pyruvate as cosubstrate) (PubMed:15556614). {ECO:0000269\|PubMed:15556614}; pH dependence: Optimum pH is 8.5 and 10 (with pyruvate as cosubstrate). {ECO:0000269\|PubMed:12110301}; Temperature dependence: Optimum temperature is 60 degrees Celsius (at pH 8.5 and with pyruvate as cosubstrate). {ECO:0000269\|PubMed:12110301};
Pathway:		Amino-acid degradation; L-kynurenine degradation; kynurenate from L-kynurenine: step 1/2. {ECO:0000269\|PubMed:12110301, ECO:0000269\|PubMed:15556614}.
Subunit:		Homodimer. {ECO:0000305\|PubMed:12110301, ECO:0000305\|PubMed:15853804, ECO:0000305\|PubMed:18186649}.
Subcellular location:		Mitochondrion {ECO:0000255}.
Tissue specificity:		Expressed in developing ovaries (PubMed:12110301). Expressed at high levels in the head (PubMed:12110301). {ECO:0000269\|PubMed:12110301}.
Developmental stage:		Expressed in larvae, pupae and adults (PubMed:12110301). Expressed at low levels in larvae, then expression increases at the beginning of pupal development to reach high expression levels in adults (PubMed:12110301). {ECO:0000269\|PubMed:12110301}.
Similarity:		Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. {ECO:0000305}.