| Annotation | X-ray crystal structure analysis supported by site-directed mutagenesis, modeling, and molecular dynamics simulations identified a molecular determinant of prephenate aminotransferase activity in the flexible N-terminal loop of 1beta AAT. A Lys/Arg/Gln residue in position 12 in the sequence present only in PAT-competent enzymes could interact with the 4-hydroxyl group of the prephenate substrate. | Organism | A. thaliana |
| Gene | AAT | PubMed Id | 30771275 |
| last updated | 2020-05-09 |
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