7nea | pdb_00007nea

Crystal structure of branched-chain amino acid aminotransferase from Thermobaculum terrenum (M3 mutant).

spinqualitylabelsall models 7nea, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7nea is a 1 chain structure with sequence from Thet1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CL, GOL, NA, PLP Gene: ilvE, Tter_1720 (THET1) Activity: Branched-chain-amino-acid transaminase, with EC number 2.6.1.42 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [D1CCW1_THET1] Acts on leucine, isoleucine and valine.[RuleBase:RU364094] Publication Abstract from PubMed Creating biocatalysts for (R)-selective amination effectively is highly desirable in organic synthesis. Despite noticeable progress in the engineering of (R)-amine activity in pyridoxal-5'-phosphate-dependent transaminases of fold type IV, the specialization of the activity is still an intuitive task, as there is poor understanding of sequence-structure-function relationships. In this study, we analyzed this relationship in transaminase from Thermobaculum terrenum, distinguished by expanded substrate specificity and activity in reactions with L-amino acids and (R)-(+)-1-phenylethylamine using alpha-ketoglutarate and pyruvate as amino acceptors. We performed site-directed mutagenesis to create a panel of the enzyme variants, which differ in the active site residues from the parent enzyme to a putative transaminase specific to (R)-primary amines. The variants were examined in the overall transamination reactions and half-reaction with (R)-(+)-1-phenylethylamine. A structural analysis of the most prominent variants revealed a spatial reorganization in the active sites, which caused changes in activity. Although the specialization to (R)-amine transaminase was not implemented, we succeeded in understanding the role of the particular active site residues in expanding substrate specificity of the enzyme. We showed that the specificity for (R)-(+)-1-phenylethylamine in transaminase from T. terrenum arises without sacrificing the specificity for L-amino acids and alpha-ketoglutarate and in consensus with it. Probing the role of the residues in the active site of the transaminase from Thermobaculum terrenum.,Bezsudnova EY, Nikolaeva AY, Bakunova AK, Rakitina TV, Suplatov DA, Popov VO, Boyko KM PLoS One. 2021 Jul 29;16(7):e0255098. doi: 10.1371/journal.pone.0255098., eCollection 2021. PMID:34324538 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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