Lysyl oxidase copper-talon complex: a model.
The translated primary amino-acid sequences from human genomic and human, rat and mouse lysyl oxidase cDNAs were subjected to computer comparison. This revealed a highly-conserved primary structure and similar computer-predicted secondary structures. A prototypical lysyl oxidase structural model was reconciled with the known physical, chemical and biological properties. Analysis of the post-translationally-modified and proteolytically-processed mature enzyme model revealed a copper coordination complex that may be contained as part of the active site. This integral copper coordination complex resembles a talon. The proposed model should facilitate the elucidation of these and other structural and functional relationships within the lysyl oxidase molecule.
Krebs
C J
CJ
Department of Molecular Biology and Genetics, Wayne State University School of Medicine, Detroit, MI 48201.
Krawetz
S A
SA
D015110:4-Hydroxycoumarins / Q000737:chemistry*; D000595:Amino Acid Sequence; D000818:Animals; D003300:Copper / Q000737:chemistry*; D006801:Humans; D051379:Mice; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D008249:Protein-Lysine 6-Oxidase / Q000737:chemistry* / Q000235:genetics; D051381:Rats; D016415:Sequence Alignment; D012984:Software
D015110:4-Hydroxycoumarins; D003300:Copper; C013418:bromfenacoum; D008249:Protein-Lysine 6-Oxidase