Structural and functional diversity of lysyl oxidase and the LOX-like proteins.
Lysyl oxidase (LOX) and four lysyl oxidase-like proteins, LOXL, LOXL2, LOXL3 and LOXL4, each contain a copper binding site, conserved lysyl and tyrosyl residues that may contribute to quinone co-factor formation, and a cytokine receptor-like domain. Each protein differs mainly in their N-terminal sequence, which may confer individual functions. Processing of the LOX proteins by BMP-1 and possibly other mechanisms may result in multiple functional forms. Splicing, reported for LOXL3, may also generate additional variants with unique functions. Each LOX, with its individual, developmentally regulated tissue and cell-specific expression and localization, results in a complex structural and functional variation for the LOX amine oxidases. The presence of only two LOX-like proteins in Drosophila, each with distinct spatial and temporal expression, allows for the assignment of individual function to one of these amine oxidases. Comparative expression analysis of each LOX protein is presented to help determine their functional significance.
Molnar
J
J
Department of Allied Medical Sciences, John A. Burns School of Medicine, University of Hawaii, 1993 East West Road, Biomed T415, Honolulu, HI 96822, USA.
Fong
K S K
KS
He
Q P
QP
Hayashi
K
K
Kim
Y
Y
Fong
S F T
SF
Fogelgren
B
B
Szauter
K Molnarne
KM
Mink
M
M
Csiszar
K
K
D000594:Amino Acid Oxidoreductases / Q000737:chemistry* / Q000235:genetics / Q000502:physiology; D000818:Animals; D004330:Drosophila / Q000201:enzymology; D018507:Gene Expression Regulation, Developmental; D051379:Mice; D009206:Myocardium / Q000201:enzymology; D008249:Protein-Lysine 6-Oxidase / Q000737:chemistry* / Q000235:genetics / Q000502:physiology
D000594:Amino Acid Oxidoreductases; C435668:LOXL3 protein, human; C445682:LOXL4 protein, human; C485601:Loxl2 protein, mouse; D008249:Protein-Lysine 6-Oxidase