Indolyl-3-acetaldoxime dehydratase from the phytopathogenic fungus Sclerotinia sclerotiorum: Purification, characterization, and substrate specificity
作者:M. Soledade C. Pedras、Zoran Minic、Premila D. Thongbam、Vangala Bhaskar、Sabine Montaut
DOI:10.1016/j.phytochem.2010.10.002
日期:2010.12
acid sequence of IAD, determined using LC-ESI-MS/MS, identified it as the protein SS1G_01653 from S. sclerotiorum. IADSs was highly homologous (84% amino acid identity) to the hypothetical protein BC1G_14775 from Botryotinia fuckeliana B05.10. In addition, similarity to the phenylacetaldoxime dehydratases from Gibberella zeae (33% amino acid identity) and Bacillus sp. (20% amino acid identity) was noted
描述了由植物真菌病原体核盘菌产生的吲哚基-3-乙醛肟脱水酶的纯化和表征。底物特异性表明它是一种吲哚基-3-乙醛肟脱水酶(IAD,EC 4.99.1.6),可催化吲哚基-3-乙醛肟转化为吲哚基-3-乙腈。该酶显示出 Michaelis-Menten 动力学,表观分子量为 44 kDa。使用 LC-ESI-MS/MS 确定 IAD 的氨基酸序列,将其鉴定为来自核盘菌的蛋白质 SS1G_01653。IADS 与来自 Botryotinia fuckeliana B05.10 的假设蛋白 BC1G_14775 高度同源(84% 氨基酸同一性)。此外,与来自玉米赤霉(33% 氨基酸同一性)和芽孢杆菌的苯乙醛肟脱水酶相似。注意到(20% 氨基酸同一性)。在厌氧条件下加入 Na(2)S(2)O(4) 后,IADSs 的比活性增加了约 17 倍,但在没有 Na(2)S(2)O(4) 的情况下没有显着变化观