8fts | pdb_00008fts

SgvM methyltransferase with SAH and alpha-ketoleucine

spinqualitylabelsall models 8fts, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8fts is a 1 chain structure with sequence from Streptomyces griseoviridis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.2Å Ligands: COI, SAH, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function R9UTR3_STRGD Publication Abstract from PubMed Catalytic asymmetric alpha-alkylation of carbonyl compounds represents a long-standing challenge in synthetic organic chemistry. Herein, we advance a dual biocatalytic platform for the efficient asymmetric alkylation of alpha-keto acids. First, guided by our recently obtained crystal structures, we develop SgvM(VAV) as a general biocatalyst for the enantioselective methylation, ethylation, allylation and propargylation of a range of alpha-keto acids with total turnover numbers (TTNs) up to 4,600. Second, we mine a family of bacterial HMTs from Pseudomonas species sharing less than 50% sequence identities with known HMTs and evaluated their activities in SAM regeneration. Our best performing HMT from P. aeruginosa, PaHMT, displays the highest SAM regeneration efficiencies (TTN up to 7,700) among HMTs characterized to date. Together, the synergistic use of SgvM(VAV) and PaHMT affords a fully biocatalytic protocol for asymmetric methylation featuring a record turnover efficiency, providing a solution to the notorious problem of asymmetric alkylation. A biocatalytic platform for asymmetric alkylation of alpha-keto acids by mining and engineering of methyltransferases.,Ju S, Kuzelka KP, Guo R, Krohn-Hansen B, Wu J, Nair SK, Yang Y Nat Commun. 2023 Sep 14;14(1):5704. doi: 10.1038/s41467-023-40980-w. PMID:37709735 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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