Properties and function of lysyl oxidase.
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.
Department of Biochemistry, Boston University School of Medicine, Massachusetts.
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D000818:Animals; D003238:Connective Tissue / Q000201:enzymology*; D005109:Extracellular Matrix / Q000201:enzymology*; D006801:Humans; D008171:Lung Diseases / Q000201:enzymology; D008970:Molecular Weight; D008249:Protein-Lysine 6-Oxidase / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000502:physiology*
D008249:Protein-Lysine 6-Oxidase