EC Number   |
General Information |
Reference |
|---|
   2.6.1.B21 | evolution |
(R)-selective omega-aminotransferases (R-omegaATs) are variants of aminotransferase group III |
-, 759127 |
| 2.6.1.B21 | evolution |
the ATA enzyme from Ruegeria sp. TM1040 (Rsp-ATA, PDB ID 3FCR) belongs to the ATAs of fold class I |
759050 |
| 2.6.1.B21 | evolution |
the enzyme belongs to the PLP fold type IV transaminases |
-, 759531 |
| 2.6.1.B21 | evolution |
the enzyme belongs to the PLP fold type IV transaminases. PLP fold type IV transaminases include branched-chain amino acid transaminases (BCATs), D-amino acid transaminases, and (R)-amine:pyruvate transaminases |
-, 758848 |
| 2.6.1.B21 | evolution |
the enzyme belongs to the PLP fold type IV transaminases. PLP fold type IV transaminases include branched-chain amino acid transaminases (BCATs), D-amino acid transaminases, and (R)-amine:pyruvate transaminases. It is generally accepted that R-omegaATs are variants of aminotransferase group III. Library screening, phylogenetic analysis. R-omegaAT enzyme secondary structure and structural motifs comparisons, overview. V238I variation is observed among residues in PLP binding site. Val62 and Thr274 are changed to glycine in Bacillus cellulosilyticus R-omegaAT_Bcel and Bacillus thuringiensis R-omegaAT_Bthu among residues in the small binding pocket. H55Y, Y60F, F115Y, E117R, and W184Y variations and deletion of R128 are observed among residues in the large binding pocket. Noticeable variation include the deletion of Arg128 and variation of V62G and T274G |
-, 759127 |
| 2.6.1.B21 | evolution |
the enzyme is a PLP fold type IV transaminase. PLP fold type IV transaminases include branched-chain amino acid transaminases (BCATs), D-amino acid transaminases, and (R)-amine:pyruvate transaminases. Enzyme Hoch3033 is a transaminases with mixed type of activity. The mixed type of activity of Hoch3033 is implemented within the BCAT-like active site, but in the active site of Hoch3033, substitutions of specificity-determining residues, that are important for substrate binding in canonical BCATs, are observed |
758848 |
| 2.6.1.B21 | evolution |
the enzyme is a PLP fold type IV transaminase. Transaminases of PLP fold type IV are characterized by (R)- or (S)-stereoselective transfer of amino groups, depending on the substrate profile of the enzyme. PLP fold type IV transaminases include branched-chain amino acid transaminases (BCATs), D-amino acid transaminases, and (R)-amine:pyruvate transaminases. A small substrate binding pocket which is a general property for all the omega-TAs known to date |
759007 |
| 2.6.1.B21 | more |
enzyme Hoch3033 active site structure and substrate binding. Hoch3033 has changes in the specificity determining key residues, which constitute characteristic sequence motifs, overview |
758848 |
| 2.6.1.B21 | more |
the mixed type of activity of the enzyme is implemented within the BCAT-like active site. In the active site of the enzyme, substitutions of specificity-determining residues, that are important for substrate binding in canonical BCATs, are observed. These changes result in the loss of activity towards 2-oxoglutarate and increase the affinity towards (R)-alpha-methylbenzylamine. Active structure analysis |
-, 758848 |
| 2.6.1.B21 | physiological function |
enzyme Hoch3033 is a transaminases with mixed type of activity. The mixed type of activity of Hoch3033 is implemented within the BCAT-like active site, but in the active site of Hoch3033, substitutions of specificity-determining residues, that are important for substrate binding in canonical BCATs, are observed. These changes (H106Y/Y108R) result in the loss of activity towards 2-oxoglutarate and increase the affinity towards (R)-alpha-methylbenzylamine |
758848 |
