4uug

The (R)-selective amine transaminase from Aspergillus fumigatus with inhibitor bound

spinqualitylabelsall models 4uug, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4uug is a 2 chain structure with sequence from Aspergillus fumigatus Af293. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.6Å Ligands: FMT, MPD, MRD, NA, PXG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q4WH08_ASPFU Publication Abstract from PubMed Chirale amines are important precursors for the pharmaceutical and fine-chemical industry. Due to this, the demand for enantiopure amines is currently increasing. Amine transaminases (ATA) can produce a large spectrum of chiral amines in (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 amine donor producing pyruvate as alpha-keto acid product. In order to guide protein engineering of transaminases to improve substrate specificity and enantioselectivity, we carried out a crystal structure analysis at 1.6 A resolution of the (R)-ATA from Aspergillus fumigatus with the bound inhibitor gabaculine. This revealed that Arg126 plays an important role for the dual substrate recognition of this enzyme as mutating this residue to alanine reduced substantially the ability of the enzyme to use pyruvate as amino acceptor. This article is protected by copyright. All rights reserved. Structural and biochemical characterization of the dual substrate recognition of the (R)-selective amine transaminase from Aspergillus fumigatus.,Skalden L, Thomsen M, Hohne M, Bornscheuer UT, Hinrichs W FEBS J. 2014 Nov 15. doi: 10.1111/febs.13149. PMID:25400251 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Aminotransferase 3D structures

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