1AHZ

STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE IN COMPLEX WITH 4-(1-HEPTENYL)PHENOL

Summary for 1AHZ

• Entry DOI: 10.2210/pdb1ahz/pdb
• Descriptor: VANILLYL-ALCOHOL OXIDASE, CHLORIDE ION, FLAVIN-ADENINE DINUCLEOTIDE, ... (4 entities in total)
• Functional Keywords: flavoenzyme, oxidase, catalysis
• Biological source: Penicillium simplicissimum
• Cellular location: Peroxisome: P56216
• Total number of polymer chains: 2
• Total formula weight: 128048.55

Authors

Mattevi, A. (deposition date: 1997-04-10, release date: 1997-10-15, Last modification date: 2024-12-25)

Primary citation

Mattevi, A.,Fraaije, M.W.,Mozzarelli, A.,Olivi, L.,Coda, A.,van Berkel, W.J.
Crystal structures and inhibitor binding in the octameric flavoenzyme vanillyl-alcohol oxidase: the shape of the active-site cavity controls substrate specificity.
Structure, 5:907-920, 1997

PubMed Abstract: Lignin degradation leads to the formation of a broad spectrum of aromatic molecules that can be used by various fungal micro-organisms as their sole source of carbon. When grown on phenolic compounds, Penicillium simplicissimum induces the strong impression of a flavin-containing vanillyl-alcohol oxidase (VAO). The enzyme catalyses the oxidation of a vast array of substrates, ranging from aromatic amines to 4-alkyphenols. VAO is a member of a novel class of widely distributed oxidoreductases, which use flavin adenine dinucleotide (FAD) as a cofactor covalently bound to the protein. We have carried out the determination of the structure of VAO in order to shed light on the most interesting features of these novel oxidoreductases, such as the functional significance of covalent flavinylation and the mechanism of catalysis.

PubMed: 9261083
DOI: 10.1016/S0969-2126(97)00245-1

Experimental method

X-RAY DIFFRACTION (3.3 Å)