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
Department of Chemistry, University of California, Berkeley, CA 94720, USA.
Science. 1996 Aug 23;273(5278):1078-84. doi: 10.1126/science.273.5278.1078.
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.
在牛主动脉赖氨酰氧化酶的活性位点发现了一种此前未知的氧化还原辅因子。艾德曼测序、质谱分析、紫外可见光谱和共振拉曼研究表明，这种辅因子是一种醌。其结构源自肽基赖氨酸的ε-氨基与酪氨酸残基修饰侧链的交联，已被命名为赖氨酸-酪氨酸醌。这种醌似乎是由两个氨基酸侧链交联形成的哺乳动物辅因子的唯一实例。这一发现扩展了已知醌辅因子结构的范围，并对其生物合成机制具有重要意义。
