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 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.
Wang
S X
SX
Department of Chemistry, University of California, Berkeley, CA 94720, USA.
Mure
M
M
Medzihradszky
K F
KF
Burlingame
A L
AL
Brown
D E
DE
Dooley
D M
DM
Smith
A J
AJ
Kagan
H M
HM
Klinman
J P
JP
D000595:Amino Acid Sequence; D000818:Animals; D001011:Aorta / Q000201:enzymology; D001665:Binding Sites; D002417:Cattle; D002851:Chromatography, High Pressure Liquid; D008239:Lysine / Q000031:analogs & derivatives* / Q000737:chemistry / Q000378:metabolism; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D008970:Molecular Weight; D016297:Mutagenesis, Site-Directed; D010084:Oxidation-Reduction; D008249:Protein-Lysine 6-Oxidase / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D011809:Quinones / Q000737:chemistry* / Q000378:metabolism; D013056:Spectrophotometry, Ultraviolet; D013059:Spectrum Analysis, Raman
D011809:Quinones; C100796:lysine tyrosylquinone; D008249:Protein-Lysine 6-Oxidase; D008239:Lysine