8ajp | pdb_00008ajp

Crystal structure of Halogen methyl transferase from Paraburkholderia xenovorans at 1.8 A in complex with SAH

spinqualitylabelsall models 8ajp, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8ajp is a 1 chain structure with sequence from Paraburkholderia xenovorans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CL, SAH Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [Q145N6_PARXL] Publication Abstract from PubMed Late-stage methylation is a key technology in the development of pharmaceutical compounds. Methyltransferase biocatalysis may provide powerful options to insert methyl groups into complex molecules with high regio- and chemo-selectivity. The challenge of a large-scale application of methyltransferases is their dependence on S-adenosylmethionine (SAM) as a stoichiometric, and thus exceedingly expensive co-substrate. As a solution to this problem, we and others have explored the use of methyl halides as reagents for in-situ regeneration of SAM. However, the need to handle volatile electrophiles such as methyl iodide (MeI) may also hamper applications at scale. As a more practical solution, we have now developed an enzyme-catalyzed process that affords regeneration of SAM with methyl toluene sulfonate. In this report we describe enzymes from the thiopurine methyltransferase family that accept sulfate- and sulfonate-based methyl donors to convert S-adenosylhomocysteine to SAM with efficiencies that rival MeI-based reactions. Synthetic reagents for enzyme-catalyzed methylation.,Wen X, Leisinger F, Leopold V, Seebeck FP Angew Chem Int Ed Engl. 2022 Aug 21. doi: 10.1002/anie.202208746. PMID:35989225 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA