Kagan H M
Department of Biochemistry, Boston University School of Medicine, Massachusetts.
Pathol Res Pract. 1994 Oct;190(9-10):910-9. doi: 10.1016/S0344-0338(11)80995-7.
Lysyl oxidase oxidizes peptidyl lysine in collagen and elastin substrates to residues of alpha-aminoadipic-delta-semialdehyde. The peptidyl aldehydes can then undergo spontaneous condensations with unreacted epsilon-amino groups and with neighboring aldehyde functions, thus forming the covalent crosslinkages which convert elastin and collagen into insoluble fibers. The unique role of lysyl oxidase in the post-translational modification of these proteins qualifies this enzymatic reaction as a potentially pivotal site of biological and/or chemotherapeutic control of collagen fiber deposition. Recent advances in the study of the catalytic mechanism, in the development of active site inhibitors, and in the biosynthesis and regulation of this unusual catalyst are reviewed as are studies on the response of lysyl oxidase in fibrotic liver.
赖氨酰氧化酶将胶原蛋白和弹性蛋白底物中的肽基赖氨酸氧化为α-氨基己二酸-δ-半醛残基。然后，肽基醛可以与未反应的ε-氨基以及相邻的醛基发生自发缩合，从而形成共价交联，将弹性蛋白和胶原蛋白转化为不溶性纤维。赖氨酰氧化酶在这些蛋白质翻译后修饰中的独特作用，使这种酶促反应成为胶原蛋白纤维沉积的生物学和/或化学治疗控制的潜在关键位点。本文综述了在催化机制研究、活性位点抑制剂开发、这种特殊催化剂的生物合成和调节方面的最新进展，以及对纤维化肝脏中赖氨酰氧化酶反应的研究。
