Medical Research Council Mitochondrial Biology Unit, Wellcome Trust/MRC Building, Cambridge, UK.
Biochem J. 2011 Jul 15;437(2):e1-3. doi: 10.1042/BJ20110918.
The prokaryotic and eukaryotic homologues of complex I (proton-pumping NADH:quinone oxidoreductase) perform the same function in energy transduction, but the eukaryotic enzymes are twice as big as their prokaryotic cousins, and comprise three times as many subunits. Fourteen core subunits are conserved in all complexes I, and are sufficient for catalysis - so why are the eukaryotic enzymes embellished by so many supernumerary or accessory subunits? In this issue of the Biochemical Journal, Angerer et al. have provided new evidence to suggest that the supernumerary subunits are important for enzyme stability. This commentary aims to put this suggestion into context.
在能量转导中，原核和真核生物的 I 复合物（质子泵 NADH：醌氧化还原酶）执行相同的功能，但真核生物的酶比原核生物的酶大两倍，并且由三倍数量的亚基组成。所有 I 复合物中都保守有 14 个核心亚基，这些亚基足以进行催化 - 那么，为什么真核生物的酶会有这么多多余或附属的亚基呢？在本期《生物化学杂志》中，Angerer 等人提供了新的证据表明，多余的亚基对于酶的稳定性很重要。本文的目的是将这一观点置于适当的背景下进行讨论。
