The proteolytic processing site of the precursor of lysyl oxidase.
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.
Cronshaw
A D
AD
Department of Biochemistry, University of Edinburgh, U.K.
Fothergill-Gilmore
L A
LA
Hulmes
D J
DJ
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
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