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

该子项目是利用NIH/NCRR资助的中心赠款提供的资源的许多研究子项目之一。子项目和研究者（PI）可能从另一个NIH来源获得主要资金，因此可以在其他CRISP条目中表示。所列机构为中心，不一定是研究者所在机构。含铜胺氧化酶是从细菌到哺乳动物的生物体中普遍存在的酶。它们具有广泛的作用，包括小分子单胺和二胺的催化剂。许多具有广泛的特异性，而其他仅氧化特定的胺。我们已经开始研究（1）具有氧化肽中赖氨酸残基的末端氨基的能力的胺氧化酶，（2）设计用于探测从分子表面到活性位点的途径的衍生物，以及（3）酶抑制剂复合物。我们还通过确定几种新表征的1型或蓝铜蛋白的结构，继续进行长期的电子转移研究。

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.