| Literature DB >> 8688089 |
S X Wang1, M Mure, K F Medzihradszky, A L Burlingame, D E Brown, D M Dooley, A J Smith, H M Kagan, J P Klinman.
Abstract
A 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.Entities:
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Year: 1996 PMID： 8688089 DOI： 10.1126/science.273.5278.1078
Source DB: PubMed Journal: Science ISSN： 0036-8075 Impact factor: 47.728