来自海洋软体动物马蹄蛤的内切-1→3-β-D-葡聚糖酶的催化特性和氨基酸序列。
Catalytic properties and amino acid sequence of endo-1→3-β-D-glucanase from the marine mollusk Tapes literata.
机构信息
Pacific Institute of Bioorganic Chemistry, Far East Branch of the Russian Academy of Sciences, pr. 100 let Vladivostoku 159, 690022 Vladivostok, Russia.
出版信息
Biochemistry (Mosc). 2012 Aug;77(8):878-88. doi: 10.1134/S0006297912080081.
A specific 1→3-β-D-glucanase with molecular mass 37 kDa was isolated in homogeneous state from crystalline style of the commercial marine mollusk Tapes literata. It exhibits maximal activity within the pH range from 4.5 to 7.5 at 45°C. The 1→3-β-D-glucanase catalyzes hydrolysis of β-1→3 bonds in glucans as an endoenzyme with retention of bond configuration, and it has transglycosylating activity. The K(m) for hydrolysis of laminaran is 0.25 mg/ml. The enzyme is classified as a glucan endo-(1→3)-β-D-glucosidase (EC 3.2.1.39). The cDNA encoding this 1→3-β-D-glucanase from T. literata was sequenced, and the amino acid sequence of the enzyme was determined. The endo-1→3-β-D-glucanase from T. literata was assigned to the 16th structural family (GHF 16) of O-glycoside hydrolases.
从商业性海洋贝类帘蛤科文蛤(Tapes literata)的晶状型中分离出一种特定的 1→3-β-D-葡聚糖酶，其相对分子质量为 37 kDa，呈均一状态。该酶在 45°C 时 pH4.5-7.5 范围内具有最大活性。1→3-β-D-葡聚糖酶作为一种保留键构象的内切酶，以酶的形式作用于葡聚糖，催化β-1→3 键水解，同时具有转糖苷活性。其对昆布多糖的水解的 K(m)值为 0.25mg/ml。该酶被归类为葡聚糖内切-(1→3)-β-D-葡糖苷酶（EC 3.2.1.39）。测序了来自 T. literata 的编码这种 1→3-β-D-葡聚糖酶的 cDNA，并测定了酶的氨基酸序列。来自 T. literata 的内切 1→3-β-D-葡聚糖酶被分配到 O-糖基水解酶的第 16 个结构家族（GHF 16）。
Zotero 插件