7P3T
Transaminase of gamma-proteobacterium
Summary for 7P3T
| Entry DOI | 10.2210/pdb7p3t/pdb |
| Descriptor | Branched-chain amino acid aminotransferase, PYRIDOXAL-5'-PHOSPHATE, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | transaminase, pyridoxal-phosphate, transferase |
| Biological source | Luminiphilus syltensis NOR5-1B |
| Total number of polymer chains | 6 |
| Total formula weight | 205022.38 |
| Authors | Ermler, U. (deposition date: 2021-07-08, release date: 2021-12-15, Last modification date: 2024-01-31) |
| Primary citation | Konia, E.,Chatzicharalampous, K.,Drakonaki, A.,Muenke, C.,Ermler, U.,Tsiotis, G.,Pavlidis, I.V. Rational engineering of Luminiphilus syltensis ( R )-selective amine transaminase for the acceptance of bulky substrates. Chem.Commun.(Camb.), 57:12948-12951, 2021 Cited by PubMed Abstract: Despite the plethora of information on ()-selective amine transaminases, the ()-selective ones are still not well-studied; only a few structures are known to date, and their substrate scope is limited, apart from a few stellar works in the field. Herein, the structure of ()-selective amine transaminase is elucidated to facilitate engineering towards variants active on bulkier substrates. The V37A variant exhibited increased activity towards 1-phenylpropylamine and to activity against 1-butylamine. In contrast, the S248 and T249 positions, located on the β-turn in the P-pocket, seem crucial for maintaining the activity of the enzyme. PubMed: 34806715DOI: 10.1039/d1cc04664k PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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