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

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 铜胺氧化酶是一种普遍存在的酶，存在于从细菌到哺乳动物的各种生物体中。它们扮演着各种各样的角色，包括分解小的单胺和双胺。许多具有广泛的特异性，而另一些只氧化特定的胺。我们已经开始研究(1)能够氧化多肽中赖氨酸残基的末端氨基的胺氧化酶，(2)旨在探索从分子表面到活性部位的途径的衍生物，以及(3)酶抑制复合体。我们还在继续对电子转移的长期研究，通过确定几个新表征的1型或蓝铜蛋白的结构。

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.