Amiri Mahdi, Naim Hassan Y
Department of Physiological Chemistry, University of Veterinary Medicine Hannover, Hannover, Germany.
J Pediatr Gastroenterol Nutr. 2018 Jun;66 Suppl 3:S18-S23. doi: 10.1097/MPG.0000000000001826.
The final step of carbohydrate digestion in the intestine is performed by 2 major α-glucosidases of the intestinal mucosa, sucrase-isomaltase (SI) and maltase-glucoamylase. Both of these enzymes are type II membrane glycoproteins, which share a significant level of homology in gene and protein structures and yet have differences in the posttranslational processing, substrate specificity and functional capacity. Insufficient activity of these disaccharidases particularly SI as a result of genetic mutations or secondary intestinal pathologies is associated with carbohydrate maldigestion and gastrointestinal intolerances. This review will discuss the maturation profiles of SI and maltase-glucoamylase relative to their functional capacities and deficiencies.
肠道中碳水化合物消化的最后一步由肠黏膜的两种主要α-葡萄糖苷酶——蔗糖酶-异麦芽糖酶（SI）和麦芽糖酶-葡糖淀粉酶完成。这两种酶都是II型膜糖蛋白，在基因和蛋白质结构上有显著的同源性，但在翻译后加工、底物特异性和功能能力方面存在差异。由于基因突变或继发性肠道疾病导致这些双糖酶，尤其是SI活性不足，与碳水化合物消化不良和胃肠道不耐受有关。本综述将讨论SI和麦芽糖酶-葡糖淀粉酶相对于其功能能力和缺陷的成熟情况。
