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Lysyl Oxidase as a Potential Therapeutic Target
Drug News & Perspectives, 2008Lysyl oxidase (LOX) is a copper-dependent amine oxidase that catalyzes the covalent cross-link of collagens and elastin in the extracellular environment, thereby determining the mechanical properties of extracellular matrix (ECM) and connective tissues. ECM remodeling is a common feature of diverse pathologic processes.
Cristina, Rodríguez +2 more
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Identification of the disulfide bonds of lysyl oxidase
Journal of Neural Transmission, 2010Proteolytic digestion of bovine aortic lysyl oxidase followed by tandem mass spectrometry has enabled assignment of all five disulfide bonds. The results indicate that the enzyme has a very stable central core containing three disulfide bonds, the lysyl tyrosyl quinone cross-link and the copper.
Xi, Chen, Frederick T, Greenaway
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Simplified assay for lysyl oxidase activity
Analytical Biochemistry, 1977Abstract A simplified method for the assay of lysyl oxidase activity was developed. The method is based on the measurement of tritiated water released by enzyme action from labeled protein-bound lysine and hydroxylysine. Trichloroacetic acid (TCA) supernates of the incubation mixtures are passed through small Dowex 50 (H+) columns and the effluents ...
J, Melet, G D, Vianden, B N, Bachra
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Lysyl Oxidase Isoforms in Gastric Cancer
Biomarkers in Medicine, 2016Gastric cancer (GC) is the fifth most frequent cancer in the world and shows the highest incidence in Latin America and Asia. An increasing amount of evidence demonstrates that lysyl oxidase isoforms, a group of extracellular matrix crosslinking enzymes, should be considered as potential biomarkers and therapeutic targets in GC.
Carolina, Añazco +7 more
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1989
The pH dependency of steady-state kinetic parameters and the results of chemical modification of lysyl oxidase by diethylpyrocarbonate has identified an enzyme residue with a pKa of 7.0 ± 0.1 and an enthalpy of ionization of 6.1 kcal mole-1, consistent with an active site histidine residue.
Herbert M. Kagan +4 more
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The pH dependency of steady-state kinetic parameters and the results of chemical modification of lysyl oxidase by diethylpyrocarbonate has identified an enzyme residue with a pKa of 7.0 ± 0.1 and an enthalpy of ionization of 6.1 kcal mole-1, consistent with an active site histidine residue.
Herbert M. Kagan +4 more
openaire +1 more source