2yii

Manipulating the regioselectivity of phenylalanine aminomutase: new insights into the reaction mechanism of MIO-dependent enzymes from structure-guided directed evolution

spinqualitylabelsall models 2yii, resolution 2.18Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2yii is a 4 chain structure with sequence from Taxus chinensis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.18Å Ligands: BME, FMT, GOL, MDO Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PAM_TAXCH Phenylalanine aminomutase that catalyzes the rearrangement of L-phenylalanine to R-beta-phenylalanine. Catalyzes the first committed step in the biosynthesis of the side chain of the alkaloid taxol (paclitaxel), a widely-used compound with antitumor activity. Has also low phenylalanine ammonia-lyase activity and can catalyze the amination of trans-cinnamate. Publication Abstract from PubMed Turn to switch: A mutant of phenylalanine aminomutase was engineered that can catalyze the regioselective amination of cinnamate derivatives (see scheme, red) to, for example, beta-amino acids. This regioselectivity, along with the X-ray crystal structures, suggests two distinct carboxylate binding modes differentiated by C(beta)-C(ipso) bond rotation, which determines if beta- (see scheme) or alpha-addition takes place. Mechanism-inspired engineering of phenylalanine aminomutase for enhanced beta-regioselective asymmetric amination of cinnamates.,Wu B, Szymanski W, Wybenga GG, Heberling MM, Bartsch S, de Wildeman S, Poelarends GJ, Feringa BL, Dijkstra BW, Janssen DB Angew Chem Int Ed Engl. 2012 Jan 9;51(2):482-6. doi: 10.1002/anie.201106372. Epub, 2011 Nov 23. PMID:22113970 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Aminomutase 3D structures

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