4wxf
From Proteopedia
Crystal structure of L-Serine Hydroxymethyltransferase in complex with glycine
Structural highlights
FunctionGLYA_STRT1 Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. Publication Abstract from PubMedalpha,alpha-Disubstituted alpha-amino acids are central to biotechnological and biomedical chemical processes for their own sake and as substructures of biologically active molecules for diverse biomedical applications. Structurally, these compounds contain a quaternary stereocenter, which is particularly challenging for stereoselective synthesis. The pyridoxal-5'-phosphate (PLP)-dependent L-serine hydroxymethyltransferase from Streptococcus thermophilus (SHMTSth ; EC 2.1.2.1) was engineered to achieve the stereoselective synthesis of a broad structural variety of alpha,alpha-dialkyl-alpha-amino acids. This was accomplished by the formation of quaternary stereocenters through aldol addition of the amino acids D-Ala and D-Ser to a wide acceptor scope catalyzed by the minimalist SHMTSth Y55T variant overcoming the limitation of the native enzyme for Gly. The SHMTSth Y55T variant tolerates aromatic and aliphatic aldehydes as well as hydroxy- and nitrogen-containing aldehydes as acceptors. Engineered L-Serine Hydroxymethyltransferase from Streptococcus thermophilus for the Synthesis of alpha,alpha-Dialkyl-alpha-Amino Acids.,Hernandez K, Zelen I, Petrillo G, Uson I, Wandtke CM, Bujons J, Joglar J, Parella T, Clapes P Angew Chem Int Ed Engl. 2015 Jan 21. doi: 10.1002/anie.201411484. PMID:25611820[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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