A crosslinked cofactor in lysyl oxidase: Redox function for amino acid side chains

被引:305
作者
Wang, SX
Mure, M
Medzihradszky, KF
Burlingame, AL
Brown, DE
Dooley, DM
Smith, AJ
Kagan, HM
Klinman, JP
机构
[1] UNIV CALIF BERKELEY,DEPT CHEM,BERKELEY,CA 94720
[2] UNIV CALIF BERKELEY,DEPT MOL & CELL BIOL,BERKELEY,CA 94720
[3] UNIV CALIF SAN FRANCISCO,DEPT PHARMACEUT CHEM,SAN FRANCISCO,CA 94143
[4] UNIV CALIF SAN FRANCISCO,CTR LIVER,SAN FRANCISCO,CA 94143
[5] MONTANA STATE UNIV,DEPT CHEM & BIOCHEM,BOZEMAN,MT 59717
[6] STANFORD UNIV,MED CTR,BECKMAN CTR,STANFORD,CA 94305
[7] BOSTON UNIV,SCH MED,DEPT BIOCHEM,BOSTON,MA 02118
关键词
D O I
10.1126/science.273.5278.1078
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
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.
引用
收藏
页码:1078 / 1084
页数:7
相关论文
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