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Literature summary for 2.6.1.88 extracted from

  • Heilbronn, J.; Wilson, J.; Berger, B.J.
    Tyrosine aminotransferase catalyzes the final step of methionine recycling in Klebsiella pneumonia (1999), J. Bacteriol., 181, 1739-1747.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.6.1.88

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Klebsiella pneumoniae

Inhibitors

Inhibitors Comment Organism Structure
3-nitrotyrosine approximately 20% inhibition at 1 mM Klebsiella pneumoniae
Canaline approximately 40% inhibition at 1 mM Klebsiella pneumoniae
carboxymethoxylamine complete inhibition at 1 mM Klebsiella pneumoniae
malate approximately 20% inhibition at 1 mM Klebsiella pneumoniae
additional information serine-O-sulfate and nitrophenylalanine have no inhibitory activity at 0.1 or 1 mM Klebsiella pneumoniae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.42
-
 L-tryptophan recombinant enzyme, in 10 mM phosphate buffer (pH 7.4), 50 mM pyridoxal 5'-phosphate, at 37°C Klebsiella pneumoniae
2.01
-
 L-phenylalanine recombinant enzyme, in 10 mM phosphate buffer (pH 7.4), 50 mM pyridoxal 5'-phosphate, at 37°C Klebsiella pneumoniae
2.01
-
 L-tyrosine recombinant enzyme, in 10 mM phosphate buffer (pH 7.4), 50 mM pyridoxal 5'-phosphate, at 37°C Klebsiella pneumoniae
2.46
-
 2-oxo-4-methylthiobutanoate recombinant enzyme, with L-tyrosine as cosubstrate, in 10 mM phosphate buffer (pH 7.4), 50 mM pyridoxal 5'-phosphate, at 37°C Klebsiella pneumoniae
11.93
-
 L-glutamate recombinant enzyme, in 10 mM phosphate buffer (pH 7.4), 50 mM pyridoxal 5'-phosphate, at 37°C Klebsiella pneumoniae

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
45000
-
 2 * 45000, SDS-PAGE Klebsiella pneumoniae
90000
-
 gel filtration Klebsiella pneumoniae

Organism

Organism UniProt Comment Textmining
Klebsiella pneumoniae
-
-
-
Klebsiella pneumoniae ATCC 13883
-
-
-

Purification (Commentary)

Purification (Comment) Organism
DEAE-Sepharose column chromatography, Red-120 Sepharose column chromatography, Mono-Q column chromatography, S200-Sephacryl gel filtration, and phenylethyl column chromatography Klebsiella pneumoniae

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.00314
-
 crude recombinant enzyme, after incubation with 2 mM each amino acid (ADEFGHIKLNQRSTWY) and 1 mM 2-oxo-4-methylthiobutanoate in 10 mM phosphate buffer (pH 7.4), 50 mM pyridoxal 5'-phosphate, at 37°C Klebsiella pneumoniae
0.7227
-
 recombinant enzyme after 722.7fold purification, after incubation with 2 mM each amino acid (ADEFGHIKLNQRSTWY) and 1 mM 2-oxo-4-methylthiobutanoate in 10 mM phosphate buffer (pH 7.4), 50 mM pyridoxal 5'-phosphate, at 37°C Klebsiella pneumoniae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-oxo-4-methylthiobutanoate + an L-amino acid a wide range of L-amino acids are effective donors, with Asp, Glu, Phe, His, Ile, Leu, Asn, Gln, Trp, and Tyr all producing more than 0.5 nM of L-methionine/min/mg of protein. Glu, Phe, Trp, and Tyr are the preferred amino donors, catalyzing the formation of above 1100 nM L-methionine/min/mg of protein Klebsiella pneumoniae L-methionine + a 2-oxo acid
-
 ?
2-oxo-4-methylthiobutanoate + an L-amino acid a wide range of L-amino acids are effective donors, with Asp, Glu, Phe, His, Ile, Leu, Asn, Gln, Trp, and Tyr all producing more than 0.5 nM of L-methionine/min/mg of protein. Glu, Phe, Trp, and Tyr are the preferred amino donors, catalyzing the formation of above 1100 nM L-methionine/min/mg of protein Klebsiella pneumoniae ATCC 13883 L-methionine + a 2-oxo acid
-
 ?
2-oxo-4-methylthiobutanoate + L-glutamate while L-glutamate is capable of producing the highest maximum initial velocity for L-methionine production from 2-oxo-4-methylthiobutanoate, it is 5-10fold poorer in terms of substrate specificity when compared with L-tyrosine, L-tryptophan, and L-phenylalanine Klebsiella pneumoniae L-methionine + 2-oxoglutarate
-
 ?
2-oxo-4-methylthiobutanoate + L-glutamate while L-glutamate is capable of producing the highest maximum initial velocity for L-methionine production from 2-oxo-4-methylthiobutanoate, it is 5-10fold poorer in terms of substrate specificity when compared with L-tyrosine, L-tryptophan, and L-phenylalanine Klebsiella pneumoniae ATCC 13883 L-methionine + 2-oxoglutarate
-
 ?
2-oxo-4-methylthiobutanoate + L-phenylalanine
-
 Klebsiella pneumoniae L-methionine + 2-oxo-3-phenylpropanoate
-
 ?
2-oxo-4-methylthiobutanoate + L-phenylalanine
-
 Klebsiella pneumoniae ATCC 13883 L-methionine + 2-oxo-3-phenylpropanoate
-
 ?
2-oxo-4-methylthiobutanoate + L-tryptophan
-
 Klebsiella pneumoniae L-methionine + 3-(1H-indol-3-yl)-2-oxopropanoate
-
 ?
2-oxo-4-methylthiobutanoate + L-tryptophan
-
 Klebsiella pneumoniae ATCC 13883 L-methionine + 3-(1H-indol-3-yl)-2-oxopropanoate
-
 ?
2-oxo-4-methylthiobutanoate + L-tyrosine
-
 Klebsiella pneumoniae L-methionine + 4-hydroxyhenylpyruvate
-
 r
L-methionine + 2-oxoglutarate
-
 Klebsiella pneumoniae 2-oxo-4-methylthiobutanoate + L-glutamate
-
 r
additional information the purified enzyme is unable to effectively utilize systems containing L-glutamate and oxaloacetate, L-glutamate and pyruvate, or L-alanine and 2-oxoglutarate Klebsiella pneumoniae ?
-
 ?
additional information the purified enzyme is unable to effectively utilize systems containing L-glutamate and oxaloacetate, L-glutamate and pyruvate, or L-alanine and 2-oxoglutarate Klebsiella pneumoniae ATCC 13883 ?
-
 ?

Subunits

Subunits Comment Organism
homodimer 2 * 45000, SDS-PAGE Klebsiella pneumoniae

Synonyms

Synonyms Comment Organism
KMAT
-
 Klebsiella pneumoniae
TyrAT
-
 Klebsiella pneumoniae
tyrosine aminotransferase
-
 Klebsiella pneumoniae

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
-
 Klebsiella pneumoniae