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Literature summary extracted from

  • Cong, X.; Li, X.; Li, S.
    Crystal structure of the aromatic-amino-acid aminotransferase from Streptococcus mutans (2019), Acta Crystallogr. Sect. F, 75, 141-146 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.6.1.57 recombinant enzyme expression in Escherichia coli strain BL21(DE3) Streptococcus mutans

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.6.1.57 purified recombinant enzyme, hanging drop vapor diffusion method, mixing of 0.001 ml of 18.0 mg/ml protein in 25 mM Tris-HCl, pH 7.0, with 0.001 ml of reservoir solution containing 0.2 M potassium chloride, pH 7.0, and 20% w/v PEG 3550, and equilibration against 0.02 ml reservoir, X-ray diffraction structrue determination and analysis at 2.2 A resolution, molecular replacement method using the crystal structure of AroAT from Pyrococcus horikoshii strain OT3 (PDB ID 1dju) as initial search model, modeling Streptococcus mutans

Organism

EC Number Organism UniProt Comment Textmining
2.6.1.57 Streptococcus mutans
-
-
-
2.6.1.57 Streptococcus mutans ATCC 700610
-
-
-
2.6.1.57 Streptococcus mutans UA159
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.6.1.57 recombinant enzyme from Escherichia coli strain BL21(DE3) Streptococcus mutans

Reaction

EC Number Reaction Comment Organism Reaction ID
2.6.1.57 an aromatic amino acid + 2-oxoglutarate = an aromatic oxo acid + L-glutamate the mechanism of the transamination reaction of aminotransferases is a ping-pong bi-bi mechanism, in which two half-reactions are required to complete one catalytic cycle, consequently transferring the alpha-amino group from an amino acid to an 2-oxo acid Streptococcus mutans
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.6.1.57 an aromatic amino acid + 2-oxoglutarate
-
 Streptococcus mutans an aromatic oxo acid + L-glutamate
-
 ?
2.6.1.57 an aromatic amino acid + 2-oxoglutarate
-
 Streptococcus mutans ATCC 700610 an aromatic oxo acid + L-glutamate
-
 ?
2.6.1.57 an aromatic amino acid + 2-oxoglutarate
-
 Streptococcus mutans UA159 an aromatic oxo acid + L-glutamate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.6.1.57 More enzyme structure analysis, overall and substrate-binding pocket structures comparisons, overview Streptococcus mutans

Synonyms

EC Number Synonyms Comment Organism
2.6.1.57 AroAT
-
 Streptococcus mutans
2.6.1.57 aromatic-amino-acid aminotransferase
-
 Streptococcus mutans
2.6.1.57 SmAroAT
-
 Streptococcus mutans

Cofactor

EC Number Cofactor Comment Organism Structure
2.6.1.57 pyridoxal 5'-phosphate PLP Streptococcus mutans

General Information

EC Number General Information Comment Organism
2.6.1.57 evolution structural analysis indicates that proteins of the aromatic-amino-acid aminotransferase family have conserved structural elements that might play a role in substrate binding. Streptococcus mutans AroAT (SmAroAT) belongs to the type I folding group of PLP-dependent aminotransferases Streptococcus mutans