| Description | Lysyl oxidase ( ) (LOX) [ ] is an extracellular copper-dependent enzyme that catalyses the oxidative deamination of peptidyl lysine residues in precursors of various collagens and elastins, yielding alpha-aminoadipic-delta-semialdehyde. The deaminated lysines are then able to form semialdehyde cross-links, resulting in the formation of insoluble collagen and elastin fibres in the extracellular matrix [].LOX binds a single copper atom which seems to reside within an octahedral coordination complex which includes at least three histidine ligands. Four histidine residues are clustered in a central region of the enzyme. This region is thought to be involved in cooper-binding and is called the 'copper-talon' [ ]. The signature pattern for this entry covers the four histidines that make up the putative 'copper-binding-talon'. | Name | Lysyl oxidase, conserved site |
| Short Name | Lysyl_oxidase_CS | Type | Conserved_site |
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