X-ray structure analysis of rare sugar producible enzymes aiming for elucidation of novel isomerization mechanism

研究了不动杆菌（Acinetobacter sp., L-RI）一种新型异构酶l -核糖异构酶的x射线结构。L-RI可以催化l -核糖和l -核酮糖之间的可逆异构化，是一种可行的稀有糖生产酶。在结构分析中，L-RI显示二聚体的形成。L-RI的单体结构与大肠杆菌O157:H7的d -葡萄糖异构酶相似。L-RI在活性位点保留一个金属离子和三个组氨酸。两个谷氨酸是假定的催化残基。

X-ray structure of a novel isomerase, L-ribose isomerase from Acinetobacter sp. (L-RI) was determined. L-RI can catalyze reversible isomerization between L-ribose and L-ribulose, and is a plausible enzyme for rare sugar production. In the structure analysis, L-RI showed the dimer formation. The monomer structure of L-RI is similar to that of D-lyxose isomerase from Escherichia coli O157:H7. L-RI retains a metal ion in the active site with three histidines. Two glutamates are putative catalytic residues.