Matsui H, Iwanami S, Ito H, Mori H, Honma M, Chiba S
Faculty of Agriculture, Hokkaido University, Sapporo, Japan.
Biosci Biotechnol Biochem. 1997 May;61(5):875-80. doi: 10.1271/bbb.61.875.
A cDNA encoding sugar beet alpha-glucosidase was cloned from a library constructed from mRNA of suspension-cultured cells. The cDNA, 3056 bp in length, had an open reading frame encoding a polypeptide of 913 amino acid residues with a molecular mass of 102,078 Da, included only one of four regions which were conserved in the alpha-amylase family of enzymes. The deduced amino acid sequence from the analysis of the cDNA contained the sequences of the proteolysis peptides and the active site region peptide of sugar beet alpha-glucosidase. The primary structure indicated relatively high homology in the range of 28.2 to 54.3% to those for other alpha-glucosidases. The highest homology was found in barley alpha-glucosidase.
从悬浮培养细胞的mRNA构建的文库中克隆出一个编码甜菜α-葡萄糖苷酶的cDNA。该cDNA长度为3056 bp,具有一个开放阅读框,编码一个由913个氨基酸残基组成的多肽,分子量为102,078 Da,在α-淀粉酶家族的四种保守区域中仅包含其中之一。对该cDNA分析推导的氨基酸序列包含甜菜α-葡萄糖苷酶的蛋白水解肽序列和活性位点区域肽序列。一级结构表明与其他α-葡萄糖苷酶的同源性在28.2%至54.3%之间相对较高。与大麦α-葡萄糖苷酶的同源性最高。