title: The proteolytic processing site of the precursor of lysyl oxidase.
abstract: The precise cleavage site of the N-terminal propeptide region of the precursor of lysyl oxidase has not yet been established, due to N-terminal blocking of the mature protein. Using a combination of peptide fragmentation, amino acid sequencing, time-of-flight m.s. and partial chemical unblocking procedures, it is shown that the mature form of lysyl oxidase begins at residue Asp-169 of the precursor protein (numbered according to the human sequence). The cleavage site is 28 residues to the C-terminal side of the site previously suggested on the basis of apparant molecular mass by SDS/PAGE, with the consequence that the two putative, N-linked glycosylation sites and the position of the Arg/Gln sequence polymorphism are now all in the precursor region.
authors.affiliation: Department of Biochemistry, University of Edinburgh, U.K.
authors.forename: A D
authors.initials: AD
authors.lastname: Cronshaw
authors.forename: L A
authors.initials: LA
authors.lastname: Fothergill-Gilmore
authors.forename: D J
authors.initials: DJ
authors.lastname: Hulmes
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001224:Aspartic Acid; D001665:Binding Sites; D002851:Chromatography, High Pressure Liquid; D003488:Cyanogen Bromide; D010450:Endopeptidases / Q000378:metabolism; D006031:Glycosylation; D008666:Metalloendopeptidases; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism; D011498:Protein Precursors / Q000737:chemistry* / Q000378:metabolism; D008249:Protein-Lysine 6-Oxidase / Q000737:chemistry* / Q000378:metabolism; D017421:Sequence Analysis; D013552:Swine
chemical_list: D010446:Peptide Fragments; D011498:Protein Precursors; D001224:Aspartic Acid; D008249:Protein-Lysine 6-Oxidase; D010450:Endopeptidases; D008666:Metalloendopeptidases; C058921:endoproteinase Asp-N; D003488:Cyanogen Bromide