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

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 t...

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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 1996-08, Vol.273 (5278), p.1078-1084
Main Authors: 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.
Format: Article
Language:English
Subjects:
Active sites
Amines
Amino Acid Sequence
Amino acids
Analytical, structural and metabolic biochemistry
Animals
Aorta - enzymology
Average linear density
Binding Sites
Biological and medical sciences
Cattle
Cellular biology
Chromatography, High Pressure Liquid
Crosslinking
Enzymes and enzyme inhibitors
Fractions
Fundamental and applied biological sciences. Psychology
Ions
Lysine - analogs & derivatives
Lysine - chemistry
Lysine - metabolism
Mammals
Mass spectrometers
Mass Spectrometry
Molecular Sequence Data
Molecular Weight
Mutagenesis, Site-Directed
Oxidases
Oxidation-Reduction
Oxidation-reduction reaction
Oxidation-reduction reactions
Oxidoreductases
Phenylhydrazines
Protein crosslinking
Protein-Lysine 6-Oxidase - chemistry
Protein-Lysine 6-Oxidase - genetics
Protein-Lysine 6-Oxidase - isolation & purification
Protein-Lysine 6-Oxidase - metabolism
Proteins
Quinones
Quinones - chemistry
Quinones - metabolism
Sequencing
Spectrophotometry, Ultraviolet
Spectrum Analysis, Raman
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Summary: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.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.273.5278.1078