The Enzyme Database

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EC 1.4.3.13     
Accepted name: protein-lysine 6-oxidase
Reaction: peptidyl-L-lysyl-peptide + O2 + H2O = peptidyl-allysyl-peptide + NH3 + H2O2
Other name(s): lysyl oxidase
Systematic name: protein-L-lysine:oxygen 6-oxidoreductase (deaminating)
Comments: Also acts on protein 5-hydroxylysine. This enzyme catalyses the final known enzymic step required for collagen and elastin cross-linking in the biosynthesis of normal mature extracellular matrices [4]. These reactions play an important role for the development, elasticity and extensibility of connective tissue. The enzyme is also active on free amines, such as cadaverine or benzylamine [4,5].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 99676-44-5
References:
1.  Harris, E.D., Gonnerman, W.A., Savage, J.E. and O'Dell, B.L. Connective tissue amine oxidase. II. Purification and partial characterization of lysyl oxidase from chick aorta. Biochim. Biophys. Acta 341 (1974) 332–344. [PMID: 4838158]
2.  Rayton, J.K. and Harris, E.D. Induction of lysyl oxidase with copper. Properties of an in vitro system. J. Biol. Chem. 254 (1979) 621–626. [PMID: 33171]
3.  Stassen, F.L.H. Properties of highly purified lysyl oxidase from embryonic chick cartilage. Biochim. Biophys. Acta 438 (1976) 49–60. [PMID: 7318]
4.  Palamakumbura, A.H. and Trackman, P.C. A fluorometric assay for detection of lysyl oxidase enzyme activity in biological samples. Anal. Biochem. 300 (2002) 245–251. [PMID: 11779117]
5.  Kagan, H.M., Williams, M.A., Williamson, P.R. and Anderson, J.M. Influence of sequence and charge on the specificity of lysyl oxidase toward protein and synthetic peptide substrates. J. Biol. Chem. 259 (1984) 11203–11207. [PMID: 6147351]
[EC 1.4.3.13 created 1980, modified 1983]
 
 


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