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29 March 2024
 
  » pubmed » pmid8688089

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A crosslinked cofactor in lysyl oxidase: redox function for amino acid side chains
S X Wang ; M Mure ; K F Medzihradszky ; A L Burlingame ; D E Brown ; D M Dooley ; A J Smith ; H M Kagan ; J P Klinman ;
Date 23 Aug 1996
Journal Science, 273 (5278), 1078-84
AbstractA previously unknown redox cofactor has been identified in the active site of lysyl oxidase from the bovine aorta. Edman sequencing, mass spectrometry, ultraviolet-visible spectra, and resonance Raman studies showed that this cofactor is a quinone. Its structure is derived from the crosslinking of the epsilon-amino group of a peptidyl lysine with the modified side chain of a tyrosyl residue, and it has been designated lysine tyrosylquinone. This quinone appears to be the only example of a mammalian cofactor formed from the crosslinking of two amino acid side chains. This discovery expands the range of known quino-cofactor structures and has implications for the mechanism of their biogenesis.
Source PubMed, pmid8688089
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