Strukturelle Charakterisierung der L-Aminosäureoxidase aus Rhodococcus opacus und zufällige/strukturbasierte Mutagenese zur Aufklärung des Reaktionsmechanismus

• Applicant: Professor Dr. Dietmar Schomburg
• Subject Area: Biochemistry
• Term: from 2003 to 2008
• Project identifier: Deutsche Forschungsgemeinschaft (DFG) - Project number 5387022

• Final Report Year: 2008

Final Report Abstract

In conclusion, the present results from the substrate and inhibitor, favour the hydride mechanism in its classical formulation as the first step in the reaction catalysed by L-amino acid oxidases. The chemical transformation can proceed effectively without the involvement of functional groups of amino acid residues. The groups present in the active site are involved in substrate recognition, binding and exact orientation of the substrate for an efficiently hydride transfer by directing the trajectory of the interacting orbitals.

Publications

• (2006): Crystallization and preliminary X-ray analysis of a bacterial L-amino-acid oxidase from Rhodococcus opacus. Acta Crystallogr F 62, 279-81
  Faust A, Geueke B, Niefind K, Hummel W, Schomburg D
  
• (2007): The structure of a bacterial L-amino acid oxidase from Rhodococcus opacus gives new evidence for the hydride mechanism for dehydrogenation. J Mol Biol. 367, 234-48
  Faust A, Niefind K, Hummel W, Schomburg D