| | |
| | |
Stat |
Members: 3643 Articles: 2'487'895 Articles rated: 2609
29 March 2024 |
|
| | | |
|
Article overview
| |
|
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 | 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. | Source: | PubMed, pmid8688089 | Services: | Forum | Review | Favorites |
|
|
No review found.
Did you like this article?
Note: answers to reviews or questions about the article must be posted in the forum section.
Authors are not allowed to review their own article. They can use the forum section.
browser claudebot
|
| |
|
|
|
| News, job offers and information for researchers and scientists:
| |