Abstract:Abstract: As the key enzyme for N-glycan modification of proteins in eukaryotes, α-mannosidases (α-Mans) could remove the mannose reside of glycan, complicate the N-glycans of a glycoprotein, and play a decisive role in protein folding. According to their functional specificity, α-Man is divided into two families: glycosyl hydrolase families 38 (GH38) and 47 (GH47). Through bioinformatics analysis, predictions were made on the relations between GH38 and GH47 in evolution, amino acid sequence conservation of GH38 and GH47, the physico-chemical properties, structural and functional characteristics of endoplasmic reticulum Man I (ERMan I) from different species. It was found that GH47 is more conserved than GH38, and is also prior to GH38 in the evolutionary process. There were significant differences in the length of α-Man genes in different species. It showed that the higher degree one species evolves to, the longer the average length of the gene. Eukaryotic ERMan I is one of unstable proteins, and it is hydrophilic, with a transmembrane domain and a signal peptide. It has a barrel-like spatial structure and a Ca2+-binding domain. The analysis results provide important messages for further studies on function of α-Man in life processes.
引用本文:
王 铎, 孙春玉, 陈 静, 王 义. 真核生物α-甘露糖苷酶生物信息学分析[J]. 生命科学研究, 2018, 22(3): 173-183.
WANG Duo, SUN Chun-yu, CHEN Jing, WANG Yi. Bioinformatics Analysis of α-Mannosidase in Eukaryotes. Life Science Research, 2018, 22(3): 173-183.