Exploring molecular oxygen pathways in Hansenula polymorpha copper-containing amine oxidase.

ABSTRACT: The accessibility of large substrates to buried enzymatic active sites is dependent upon the utilization of proteinaceous channels. The necessity of these channels in the case of small substrates is questionable because diffusion through the protein matrix is often assumed. Copper amine oxidases contain a buried protein-derived quinone cofactor and a mononuclear copper center that catalyze the conversion of two substrates, primary amines and molecular oxygen, to aldehydes and hydrogen peroxide, respectively. The nature of molecular oxygen migration to the active site in the enzyme from Hansenula polymorpha is explored using a combination of kinetic, x-ray crystallographic, and computational approaches. A crystal structure of H. polymorpha amine oxidase in complex with xenon gas, which serv

SUBMITTER: Johnson BJ 

PROVIDER: S-EPMC3081669 | biostudies-literature | 2007 Jun

REPOSITORIES: biostudies-literature