STRUCTURE OF A LYSYL OXIDASE FROM PICHIA PASTORIS: A COPPER-CONTAINING AMINE OXI

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This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Copper-containing amine oxidases are ubiquitous enzymes occurring in organisms ranging from bacteria to mammals. They perform a wide variety of roles including the catabolism of small mono-amines and di-amines. Many have broad specificities whereas others oxidize only specific amines. We have embarked on studies of (1) an amine oxidase that has the ability to oxidise the terminal amino groups of lysine residues in peptides, (2) derivatives designed to probe the pathway from the molecular surface to the active site, and (3) enzyme-inhibitor complexes. We are also continuing a long-standing study of electron transfer by determining the structures of several newly characterized type 1 or blue copper proteins.