Department of Biology, Washington University in St. Louis, One Brookings Drive, Campus Box 1137, St. Louis, MO 63130, USA.
Curr Opin Struct Biol. 2013 Apr;23(2):302-10. doi: 10.1016/j.sbi.2013.02.011. Epub 2013 Mar 17.
The physical organization of enzymes in metabolism is an old concept being revisited by new experimental approaches. In plants and microbes, the enzymes of cysteine biosynthesis-serine acetyltransferase (SAT) and O-acetylserine sulfhydrylase (OASS)-form a bi-enzyme complex called the cysteine regulatory complex (CRC), which likely plays a role in modulating cysteine biosynthesis in response to sulfur nutrient state. Structural and biochemical studies of SAT and OASS as individual enzymes and recent advances in structural, biophysical, and in vivo analysis of the CRC provide new insights on the function of this macromolecular assembly in plants and microbes and opens biotechnology and pharmaceutical opportunities for future exploration.
酶在新陈代谢中的物理组织是一个被新的实验方法重新审视的旧概念。在植物和微生物中,半胱氨酸生物合成的酶——丝氨酸乙酰转移酶(SAT)和 O-乙酰丝氨酸硫羟化酶(OASS)——形成一个被称为半胱氨酸调节复合物(CRC)的双酶复合物,该复合物可能在调节半胱氨酸生物合成以响应硫营养状态方面发挥作用。SAT 和 OASS 作为单个酶的结构和生化研究以及 CRC 的结构、生物物理和体内分析的最新进展为该大分子组装在植物和微生物中的功能提供了新的见解,并为未来的生物技术和药物探索开辟了机会。