2YII

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

Summary for 2YII

• Entry DOI: 10.2210/pdb2yii/pdb
• Descriptor: PHENYLALANINE AMMONIA-LYASE, BETA-MERCAPTOETHANOL, FORMIC ACID, ... (5 entities in total)
• Functional Keywords: lyase
• Biological source: TAXUS WALLICHIANA VAR. CHINENSIS (CHINESE YEW)
• Total number of polymer chains: 4
• Total formula weight: 311115.79

Authors

Wu, B.,Szymanski, W.,Wybenga, G.G.,Heberling, M.M.,Bartsch, S.,Wildeman, S.,Poelarends, G.J.,Feringa, B.L.,Dijkstra, B.W.,Janssen, D.B. (deposition date: 2011-05-13, release date: 2011-11-09, Last modification date: 2023-12-20)

Primary citation

Wu, B.,Szymanski, W.,Wybenga, G.G.,Heberling, M.M.,Bartsch, S.,De Wildeman, S.,Poelarends, G.J.,Feringa, B.L.,Dijkstra, B.W.,Janssen, D.B.
Mechanism-Inspired Engineering of Phenylalanine Aminomutase for Enhanced Beta-Regioselective Asymmetric Amination of Cinnamates.
Angew.Chem.Int.Ed.Engl., 51:482-, 2012

PubMed Abstract: 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, β-amino acids. This regioselectivity, along with the X-ray crystal structures, suggests two distinct carboxylate binding modes differentiated by C(β)-C(ipso) bond rotation, which determines if β- (see scheme) or α-addition takes place.

PubMed: 22113970
DOI: 10.1002/ANIE.201106372

Experimental method

X-RAY DIFFRACTION (2.18 Å)