Ontology highlight
ABSTRACT:
SUBMITTER: Kataoka M
PROVIDER: S-EPMC3004256 | biostudies-literature | 2011 Jan
REPOSITORIES: biostudies-literature
Kataoka Misumi M Oya Hiroko H Tominaga Ayuko A Otsu Masayuki M Okajima Toshihide T Tanizawa Katsuyuki K Yamaguchi Hiroshi H
Journal of synchrotron radiation 20101105 1
To reveal the chemical changes and geometry changes of active-site residues that cooperate with a reaction is important for understanding the functional mechanism of proteins. Consecutive temporal analyses of enzyme structures have been performed during reactions to clarify structure-based reaction mechanisms. Phenylethylamine oxidase from Arthrobacter globiformis (AGAO) contains a copper ion and topaquinone (TPQ(ox)). The catalytic reaction of AGAO catalyzes oxidative deaminations of phenylethy ...[more]