7ypm

Crystal structure of transaminase CC1012 complexed with PLP and L-alanine

spinqualitylabelsall models 7ypm, resolution 1.98Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7ypm is a 4 chain structure with sequence from Caulobacter sp. D5. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.984Å Ligands: ALA, EDO, PEG, PLP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A318BC23_9CAUL Publication Abstract from PubMed omega-Transaminases (omega-TAs) show considerable potential for the synthesis of chiral amines. However, their low catalytic efficiency towards bulky substrates limits their application, and complicated catalytic mechanisms prevent precise enzyme design. Herein, we address this challenge using a mechanism-guided computational enzyme design strategy by reprograming the transition and ground states in key reaction steps. The common features among the three high-energy-barrier steps responsible for the low catalytic efficiency were revealed using quantum mechanics (QM). Five key residues were simultaneously tailored to stabilize the rate-limiting transition state with the aid of the Rosetta design. The 14 top-ranked variants showed 16.9-143-fold improved catalytic activity. The catalytic efficiency of the best variant, M9 (Q25F/M60W/W64F/I266A), was significantly increased, with a 1660-fold increase in k(cat) /K(m) and a 1.5-26.8-fold increase in turnover number (TON) towards various indanone derivatives. Mechanism-Guided Computational Design of omega-Transaminase by Reprograming of High-Energy-Barrier Steps.,Yang L, Zhang K, Xu M, Xie Y, Meng X, Wang H, Wei D Angew Chem Int Ed Engl. 2022 Dec 23;61(52):e202212555. doi: , 10.1002/anie.202212555. Epub 2022 Nov 23. PMID:36300723 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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