作者: Xavier Grau-Bové , Iñaki Ruiz-Trillo , Fernando Rodriguez-Pascual
DOI: 10.1038/SREP10568
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摘要: Lysyl oxidases (LOX) are copper-dependent enzymes that oxidize primary amine substrates to reactive aldehydes. The best-studied role of LOX is the remodeling extracellular matrix (ECM) in animals by cross-linking collagens and elastin, although intracellular functions have been reported as well. Five different identified mammals, LOX-like (LOXL) 1 4, showing a highly conserved catalytic carboxy terminal domain more divergence rest sequence. Here we surveyed wide selection genomes order infer evolutionary history LOX. We proteins not only animals, but also many other eukaryotes, well bacteria archaea – which reveals pre-metazoan origin for this gene family. genes expanded during metazoan evolution resulting two superfamilies, LOXL2/L3/L4 LOX/L1/L5. Considering current knowledge on function mammalian isoforms ECM remodeling, propose members might preferentially involved making cross-linked collagen IV-based basement membrane, whereas diversification LOX/L1/L5 forms contributed chordate/vertebrate-specific innovations, such elastin fibronectin. Our work provides novel view family enzymes.