来自 的一种新型的低浓度木葡聚糖寡糖作用的异头酶。
A novel isoprimeverose-producing enzyme from is active with low concentrations of xyloglucan oligosaccharides.
机构信息
Bioproduction Research Institute National Institute of Advanced Industrial Science and Technology (AIST) Tsukuba Ibaraki Japan.
Biotechnology Research Institute for Drug Discovery National Institute of Advanced Industrial Science and Technology (AIST) Tsukuba Ibaraki Japan.
出版信息
FEBS Open Bio. 2018 Dec 11;9(1):92-100. doi: 10.1002/2211-5463.12549. eCollection 2019 Jan.
Xyloglucan is one of the major polysaccharides found in the plant cell wall and seeds. Owing to its complex branched structure, several different hydrolases are required to degrade it. Isoprimeverose-producing enzymes (IPase) are unique among the glycoside hydrolase 3 family in that they recognize and release a disaccharide from the nonreducing end of xyloglucan oligosaccharides. Only two IPases have been previously isolated and characterized. A novel IPase from (PmIPase) was expressed and characterized. The xylopyranosyl residue at the nonreducing end of xyloglucan oligosaccharides was essential for hydrolytic activity, and PmIPase was unable to hydrolyze cellobiose into d-glucose. PmIPase had a for xyloglucan oligosaccharide substrate that was much lower than that of the reported IPase isolated from . This indicates that PmIPase was able to produce isoprimeverose efficiently from low concentrations of xyloglucan oligosaccharides. PmIPase also exhibited transglycosylation activity and was able to transfer isoprimeverose units to its substrates.
木葡聚糖是植物细胞壁和种子中主要的多糖之一。由于其复杂的分支结构，需要几种不同的水解酶来降解它。异头糖基转移酶（IPase）在糖苷水解酶 3 家族中是独特的，因为它们能够识别并从木葡聚糖寡糖的非还原端释放出二糖。以前已经分离并鉴定了两种 IPase。从 （PmIPase）表达并鉴定了一种新型的 IPase。木葡聚糖寡糖非还原端的木吡喃糖基残基对于水解活性是必需的，PmIPase不能将纤维二糖水解成 d-葡萄糖。PmIPase 对木葡聚糖寡糖底物的 远低于从 分离出的报道的 IPase。这表明 PmIPase能够从低浓度的木葡聚糖寡糖中有效地产生异头糖基转移酶。PmIPase 还表现出转糖基化活性，能够将异头糖基转移酶单元转移到其底物上。
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