Properties and Function of Lysyl Oxidase

作者：Herbert M. Kagan, Philip C. Trackman · 发表于：American Journal of Respiratory Cell and Molecular Biology · 年份：1991 · DOI：10.1165/ajrcmb/5.3.206 · 被引用次数：330 · 研究领域：Microbial metabolism and enzyme function、Porphyrin Metabolism and Disorders、Biochemical Acid Research Studies

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.