Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Andreotti, G.; Cubellis, M.V.; Nitti, G.; Sannia, G.; Mai, X.; Marino, G.; Adams, M.W.W.
    Characterization of aromatic aminotransferases from the hyperthermophilic archaeon Thermococcus litoralis (1994), Eur. J. Biochem., 220, 543-549.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.6.1.57 0.23
-
2-oxoglutarate
-
Thermococcus litoralis
2.6.1.57 0.44
-
2-oxoglutarate pH 7.6, 78°C, isoenzyme ArAT-I Thermococcus litoralis
2.6.1.57 0.49
-
2-oxoglutarate pH 7.6, 78°C, isoenzyme ArAT-II Thermococcus litoralis
2.6.1.57 0.55
-
L-phenylalanine pH 7.6, 78°C, isoenzyme ArAT-I Thermococcus litoralis
2.6.1.57 0.76
-
2-oxoglutarate pH 7.6, 80°C Pyrococcus furiosus
2.6.1.57 1.15
-
L-phenylalanine pH 7.6, 80°C, cosubstrate 2-oxoglutarate Pyrococcus furiosus
2.6.1.57 1.31
-
L-tryptophan pH 7.6, 80°C, cosubstrate 2-oxoglutarate Pyrococcus furiosus
2.6.1.57 1.47
-
L-tryptophan pH 7.6, 78°C, isoenzyme ArAT-I Thermococcus litoralis
2.6.1.57 1.55
-
L-phenylalanine pH 7.6, 78°C, isoenzyme ArAT-II Thermococcus litoralis
2.6.1.57 2.1
-
L-tyrosine pH 7.6, 80°C, cosubstrate 2-oxoglutarate Pyrococcus furiosus
2.6.1.57 2.37
-
L-tyrosine pH 7.6, 78°C, isoenzyme ArAT-II Thermococcus litoralis
2.6.1.57 2.39
-
L-tyrosine pH 7.6, 78°C, isoenzyme ArAT-I Thermococcus litoralis
2.6.1.57 4.62
-
L-tryptophan pH 7.6, 78°C, isoenzyme ArAT-II Thermococcus litoralis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.6.1.57 44000
-
2 * 44000, SDS-PAGE Pyrococcus furiosus
2.6.1.57 45000
-
2 * 45000, ArAT-II, SDS-PAGE Thermococcus litoralis
2.6.1.57 47000
-
2 * 47000, ArAT-I, SDS-PAGE Thermococcus litoralis
2.6.1.57 92000
-
gel filtration Pyrococcus furiosus
2.6.1.57 92000
-
isoenzyme ArAT-II, gel filtration Thermococcus litoralis
2.6.1.57 110000
-
isoenzyme ArAT-I, gel filtration Thermococcus litoralis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.6.1.57 L-phenylalanine + 2-oxoglutarate Pyrococcus furiosus
-
phenylpyruvate + L-glutamate
-
?
2.6.1.57 L-phenylalanine + 2-oxoglutarate Thermococcus litoralis may play a catabolic role in proteolysis, generation of glutamate phenylpyruvate + L-glutamate
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.6.1.57 Methanococcus aeolicus
-
-
-
2.6.1.57 Pyrococcus furiosus
-
-
-
2.6.1.57 Thermococcus litoralis
-
aromatic aminotransferases I and II
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.6.1.57 isoenzymes ArAT-I and ArAT-II, Q-Sepharose, DEAE-Sepharose, phenyl-Sepharose, Superdex-200, Mono Q Thermococcus litoralis
2.6.1.57 Q-Sepharose, ammonium sulfate, phenyl-Sepharose, S-Sepharose Pyrococcus furiosus

Reaction

EC Number Reaction Comment Organism Reaction ID
2.6.1.57 an aromatic amino acid + 2-oxoglutarate = an aromatic oxo acid + L-glutamate two-step mechanism with a pyridoxamine intermediate Thermococcus litoralis

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.6.1.57 110
-
isoenzyme ArAT-I Thermococcus litoralis
2.6.1.57 181.8
-
-
Pyrococcus furiosus
2.6.1.57 424
-
isoenzyme ArAT-II Thermococcus litoralis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.6.1.57 L-phenylalanine + 2-oxoglutarate
-
Pyrococcus furiosus phenylpyruvate + L-glutamate
-
?
2.6.1.57 L-phenylalanine + 2-oxoglutarate
-
Pyrococcus furiosus phenylpyruvate + L-glutamate
-
r
2.6.1.57 L-phenylalanine + 2-oxoglutarate
-
Methanococcus aeolicus phenylpyruvate + L-glutamate
-
?
2.6.1.57 L-phenylalanine + 2-oxoglutarate
-
Thermococcus litoralis phenylpyruvate + L-glutamate
-
?
2.6.1.57 L-phenylalanine + 2-oxoglutarate may play a catabolic role in proteolysis, generation of glutamate Thermococcus litoralis phenylpyruvate + L-glutamate
-
?
2.6.1.57 L-tryptophan + 2-oxoglutarate
-
Pyrococcus furiosus 3-indole-2-oxopropanoate + L-glutamate
-
r
2.6.1.57 L-tryptophan + 2-oxoglutarate
-
Methanococcus aeolicus 3-indole-2-oxopropanoate + L-glutamate
-
?
2.6.1.57 L-tryptophan + 2-oxoglutarate
-
Thermococcus litoralis 3-indole-2-oxopropanoate + L-glutamate
-
?
2.6.1.57 L-tyrosine + 2-oxoglutarate
-
Pyrococcus furiosus p-hydroxyphenylpyruvate + L-glutamate
-
r
2.6.1.57 L-tyrosine + 2-oxoglutarate
-
Methanococcus aeolicus p-hydroxyphenylpyruvate + L-glutamate
-
?
2.6.1.57 L-tyrosine + 2-oxoglutarate
-
Thermococcus litoralis p-hydroxyphenylpyruvate + L-glutamate
-
?

Subunits

EC Number Subunits Comment Organism
2.6.1.57 dimer 2 * 44000, SDS-PAGE Pyrococcus furiosus
2.6.1.57 dimer 2 * 47000, ArAT-I, SDS-PAGE Thermococcus litoralis
2.6.1.57 dimer 2 * 45000, ArAT-II, SDS-PAGE Thermococcus litoralis

Synonyms

EC Number Synonyms Comment Organism
2.6.1.57 ArAT-ITL i.e. aromatic aminotransferase II from Thermococcus litoralis Thermococcus litoralis
2.6.1.57 ArATPf
-
Pyrococcus furiosus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.6.1.57 additional information
-
temperature optimum seems to be above 95°C Pyrococcus furiosus
2.6.1.57 95 100
-
Thermococcus litoralis

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
2.6.1.57 30 95 extremely thermostable aromatic aminotransferase from hyperthermophilic archaeon, very low activity at 30°C, approx. 50% of maximal activity at 65°C Pyrococcus furiosus
2.6.1.57 30 105 virtually inactive at 30°C, approx. 50% of maximal ArAT-I activity at 70°C, approx. 50% of ArAT-II activity at 80°C, isoenzymes ArAT-I and II Thermococcus litoralis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.6.1.57 80
-
holoenzyme, i.e. enzyme in its pyridoxal form, approx. 20% loss of phenylalanine transaminase activity after 6 h, apoenzyme, 70% loss of activity, complete protection of holoenzyme in the presence of pyridoxamine 5'-phosphate and 2-oxoglutarate Pyrococcus furiosus
2.6.1.57 95
-
59% and 27% loss of activity after 13 h in the presence of pyridoxamine 5'-phosphate or 2-oxoglutarate Pyrococcus furiosus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.6.1.57 62
-
L-tryptophan pH 7.6, 80°C, cosubstrate 2-oxoglutarate Pyrococcus furiosus
2.6.1.57 72
-
L-tyrosine pH 7.6, 80°C, cosubstrate 2-oxoglutarate Pyrococcus furiosus
2.6.1.57 225
-
2-oxoglutarate pH 7.6, 80°C Pyrococcus furiosus
2.6.1.57 253
-
L-phenylalanine pH 7.6, 80°C, cosubstrate 2-oxoglutarate Pyrococcus furiosus

Cofactor

EC Number Cofactor Comment Organism Structure
2.6.1.57 pyridoxal 5'-phosphate
-
Pyrococcus furiosus
2.6.1.57 pyridoxal 5'-phosphate a pyridoxal phosphate protein Thermococcus litoralis