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Cited by 339

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A Crosslinked Cofactor in Lysyl Oxidase: Redox Function for Amino Acid Side Chains

Wang, Sophie Xuefei, Mure, Minae, Medzihradszky, Katalin F., Burlingame, Alma L., Brown, Doreen E., Dooley, David M., Smith, Alan J., Kagan, Herbert M., Klinman, Judith P.·1996·Science

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 ε-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.

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Metadata

Authors
Wang, S. X., Mure, M., Medzihradszky, K. F., Burlingame, A. L., Brown, D. E., Dooley, D. M., Smith, A. J., Kagan, H. M., & Klinman, J. P.
Venue
Science
Published
1996-08-23
Volume
273
Issue
5278
Pages
1078-1084
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W1979098362
Cited by
339
References
0
FWCI
14.15
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: A Crosslinked Cofactor in Lysyl Oxidase: Redox Function for Amino Acid Side Chains. https://app.cochat.ai/papers/10.1126/science.273.5278.1078
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Wang, S. X., Mure, M., Medzihradszky, K. F., Burlingame, A. L., Brown, D. E., Dooley, D. M., Smith, A. J., Kagan, H. M., & Klinman, J. P. (1996). A Crosslinked Cofactor in Lysyl Oxidase: Redox Function for Amino Acid Side Chains. Science. https://doi.org/10.1126/science.273.5278.1078

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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