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Literature summary for 2.6.1.55 extracted from

  • Toyama, S.; Misono, H.; Soda, K.
    Properties of taurine: alpha-ketoglutarate aminotransferase of Achromobacter superficialis. Inactivation and reactivation of enzyme (1978), Biochim. Biophys. Acta, 523, 75-81.
    View publication on PubMed
Search for more literature for 2.6.1.55

Inhibitors

Inhibitors Comment Organism Structure
3-Methyl-2-benzothiazolone hydrazone hydrochloride weak inhibition Achromobacter superficialis
D-cycloserine 0.5 mM; 20% inhibition Achromobacter superficialis
HgCl2 0.1 mM, 98% inhibition Achromobacter superficialis
hydroxylamine 0.5 mM, complete inhibition Achromobacter superficialis
L-Cycloserine 0.5 mM, 97% inhibition Achromobacter superficialis
additional information not inhibited by p-chloromercuribenzoate, monoiodoacetic acid, D-penicillamine, L-penicillamine and EDTA Achromobacter superficialis
phenylhydrazine 0.5 mM, 17% inhibition Achromobacter superficialis
Semicarbazide 0.5 mM, 21% inhibition Achromobacter superficialis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
11
-
 2-oxoglutarate pH 8.0, 37°C, cosubstrate DL-3-aminoisobutyrate Achromobacter superficialis
12
-
 taurine
-
 Achromobacter superficialis
16
-
 Hypotaurine
-
 Achromobacter superficialis
17
-
 beta-Alanine
-
 Achromobacter superficialis

Organism

Organism UniProt Comment Textmining
Achromobacter superficialis
-
-
-

Storage Stability

Storage Stability Organism
0-5°C, crystalline enzyme in 10 mM potassium phosphate buffer, pH 7.0, 60% saturation of ammonium sulfate, 100 mM pyridoxal 5'-phosphate, 0.01% 2-mercaptoethanol, several months, no loss of activity Achromobacter superficialis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-aminopropanesulfonate + 2-oxoglutarate 43% of the activity with taurine Achromobacter superficialis 2-oxopropanesulfonate + L-glutamate
-
 ?
4-aminobutyrate + 2-oxoglutarate 60% of the activity with taurine Achromobacter superficialis L-glutamate + acetaldehyde + sulfite
-
 ?
beta-alanine + 2-oxoglutarate
-
 Achromobacter superficialis 3-oxopropanoate + L-glutamate
-
 ?
DL-3-aminobutyrate + 2-oxoglutarate 14% of the activity with taurine Achromobacter superficialis 3-oxobutyrate + L-glutamate
-
 ?
DL-3-aminoisobutyrate + 2-oxoglutarate
-
 Achromobacter superficialis 2-methyl-3-oxopropanoate + L-glutamate
-
 ?
hypotaurine + 2-oxoglutarate 601% of the activity with taurine Achromobacter superficialis 2-oxoethanesulfinic acid + L-glutamate
-
 ?
taurine + 2-oxoglutarate no activity with pyruvate, phenylpyruvate, oxaloacetate Achromobacter superficialis sulfoacetaldehyde + L-glutamate
-
 ?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
60
-
 pH 6.0-9.0, 10 min, stable Achromobacter superficialis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.8 8
-
 Achromobacter superficialis

pH Stability

pH Stability pH Stability Maximum Comment Organism
6 9 60°C, 10 min, stable Achromobacter superficialis

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate Km: 0.005 mM Achromobacter superficialis
pyridoxal 5'-phosphate 4 mol of pyridoxal phosphate per mol of enzyme Achromobacter superficialis
pyridoxal 5'-phosphate enzyme inactivated by treatment with ammonium sulfate is activated by incubation with pyridoxal 5'-phosphate at 45-60°C for about 10 min Achromobacter superficialis