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赖氨酰氧化酶的特性与功能。

Properties and function of lysyl oxidase.

作者信息

Kagan H M, Trackman P C

机构信息

Department of Biochemistry, Boston University School of Medicine, Massachusetts.

出版信息

Am J Respir Cell Mol Biol. 1991 Sep;5(3):206-10. doi: 10.1165/ajrcmb/5.3.206.

Abstract

Lysyl oxidase catalyzes the oxidation of peptidyl lysine to alpha-aminoadipic-delta-semialdehyde, the precursor to the covalent crosslinkages that stabilize fibers of elastin and collagen. This enzyme contains both copper and a carbonyl cofactor consistent with an o-quinone. The proposed mechanism of action is derived from available kinetic and chemical data and also can account for mechanism-based inhibition of the enzyme by specific monoamines and diamines. Recent evidence for biosynthetic precursors and for the regulation of lysyl oxidase in fibrotic and malignant diseases is discussed.

摘要

赖氨酰氧化酶催化肽基赖氨酸氧化生成α-氨基己二酸-δ-半醛,后者是稳定弹性蛋白和胶原蛋白纤维共价交联的前体。该酶含有铜和与邻醌一致的羰基辅因子。提出的作用机制源自现有的动力学和化学数据,也能解释特定单胺和二胺对该酶的基于机制的抑制作用。本文还讨论了纤维化和恶性疾病中赖氨酰氧化酶生物合成前体及调节的最新证据。

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