Structural highlights
Publication Abstract from PubMedThe importance of amine transaminases for producing optically pure chiral precursors for pharmaceuticals and chemicals has substantially increased in recent years. The X-ray crystal structure of the (R)-selective amine transaminase from the fungus Aspergillus fumigatus was solved by S-SAD phasing to 1.84 A resolution. The refined structure at 1.27 A resolution provides detailed knowledge about the molecular basis of substrate recognition and conversion to facilitate protein-engineering approaches. The protein forms a homodimer and belongs to fold class IV of the pyridoxal-5'-phosphate-dependent enzymes. Both subunits contribute residues to form two active sites. The structure of the holoenzyme shows the catalytically important cofactor pyridoxal-5'-phosphate bound as an internal aldimine with the catalytically responsible amino-acid residue Lys179, as well as in its free form. A long N-terminal helix is an important feature for the stability of this fungal (R)-selective amine transaminase, but is missing in branched-chain amino-acid aminotransferases and D-amino-acid aminotransferases. Crystallographic characterization of the (R)-selective amine transaminase from Aspergillus fumigatus.,Thomsen M, Skalden L, Palm GJ, Hohne M, Bornscheuer UT, Hinrichs W Acta Crystallogr D Biol Crystallogr. 2014 Apr 1;70(Pt 4):1086-93. doi:, 10.1107/S1399004714001084. Epub 2014 Mar 20. PMID:24699652[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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