Cloned (Comment) | Organism |
---|---|
recombinant enzyme expression in Escherichia coli strain BL21(DE3) | Streptococcus mutans |
Crystallization (Comment) | Organism |
---|---|
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 | UniProt | Comment | Textmining |
---|---|---|---|
Streptococcus mutans | - |
- |
- |
Streptococcus mutans ATCC 700610 | - |
- |
- |
Streptococcus mutans UA159 | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant enzyme from Escherichia coli strain BL21(DE3) | Streptococcus mutans |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
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 |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
an aromatic amino acid + 2-oxoglutarate | - |
Streptococcus mutans | an aromatic oxo acid + L-glutamate | - |
? | |
an aromatic amino acid + 2-oxoglutarate | - |
Streptococcus mutans ATCC 700610 | an aromatic oxo acid + L-glutamate | - |
? | |
an aromatic amino acid + 2-oxoglutarate | - |
Streptococcus mutans UA159 | an aromatic oxo acid + L-glutamate | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | enzyme structure analysis, overall and substrate-binding pocket structures comparisons, overview | Streptococcus mutans |
Synonyms | Comment | Organism |
---|---|---|
AroAT | - |
Streptococcus mutans |
aromatic-amino-acid aminotransferase | - |
Streptococcus mutans |
SmAroAT | - |
Streptococcus mutans |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
pyridoxal 5'-phosphate | PLP | Streptococcus mutans |
General Information | Comment | Organism |
---|---|---|
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 |