9BFO
BCAT mutant 36E
Summary for 9BFO
| Entry DOI | 10.2210/pdb9bfo/pdb |
| Related | 9BFA |
| Descriptor | Branched-chain-amino-acid aminotransferase, cytosolic (2 entities in total) |
| Functional Keywords | aminotransferase, mutant, transferase |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 2 |
| Total formula weight | 82542.04 |
| Authors | |
| Primary citation | Dare, E.S.,Newman, R.H.,Conway, M.E.,Dong, M. Crystal structures of the phosphorylation mimics of human cytosolic branched chain aminotransferase. Arch.Biochem.Biophys., 770:110479-110479, 2025 Cited by PubMed Abstract: The phosphorylation sites of the human cytosolic Branched Chain Aminotransferase (hBCATc) mediated by mitogen-activated protein kinase (MAPK)/extracellular-signal-regulated-kinase 2 (ERK2, also known as MAPK1) were mapped. The crystal structures of the phosphorylation mimics at T33 and T36 were determined. The modified transaminase activity of these variants was analyzed. Although there were no major conformational changes in the phosphorylation mimics of hBCAT, a regional conformational change at the interdomain loop was observed mainly in mutant T33E. Consistently, when the catalytic turnovers of the T33E and T36E mutants were comparable to the wild type of hBCATc, the K dropped significantly compared to the wild type, indicating a shift of the substrate binding affinity in the mutants. Taken together, this indicated the phosphorylation of hBCATc by ERK2 is affecting the hBCATc's transaminase activity. PubMed: 40414328DOI: 10.1016/j.abb.2025.110479 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.663 Å) |
Structure validation
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