4UUG
The (R)-selective amine transaminase from Aspergillus fumigatus with inhibitor bound
Summary for 4UUG
| Entry DOI | 10.2210/pdb4uug/pdb |
| Descriptor | AMINE TRANSAMINASE, 3-[O-PHOSPHONOPYRIDOXYL]--AMINO-BENZOIC ACID, (4R)-2-METHYLPENTANE-2,4-DIOL, ... (7 entities in total) |
| Functional Keywords | transferase, gabaculine |
| Biological source | ASPERGILLUS FUMIGATUS |
| Total number of polymer chains | 2 |
| Total formula weight | 75656.73 |
| Authors | Thomsen, M.,Hinrichs, W. (deposition date: 2014-07-28, release date: 2014-11-26, Last modification date: 2024-01-10) |
| Primary citation | Skalden, L.,Thomsen, M.,Hohne, M.,Bornscheuer, U.T.,Hinrichs, W. Structural and Biochemical Characterization of the Dual Substrate Recognition of the (R)-Selective Amine Transaminase from Aspergillus Fumigatus FEBS J., 282:407-, 2015 Cited by PubMed Abstract: Chiral amines are important precursors for the pharmaceutical and fine-chemical industries. Because of this, the demand for enantiopure amines is currently increasing. Amine transaminases can produce a large spectrum of chiral amines in the (R)- or (S)-configuration, depending on their substrate scope and stereo-preference, by converting a prochiral ketone into the chiral amine while using alanine as the amine donor producing pyruvate as an α-keto acid product. In order to guide the protein engineering of transaminases to improve substrate specificity and enantioselectivity, we carried out a crystal structure analysis at 1.6 Å resolution of the (R)-amine transaminase from Aspergillus fumigatus with the bound inhibitor gabaculine. This revealed that Arg126 has an important role in the dual substrate recognition of this enzyme because mutating this residue to alanine reduced substantially the ability of the enzyme to use pyruvate as an amino acceptor. PubMed: 25400251DOI: 10.1111/FEBS.13149 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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