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本文引用的文献

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Complex pectin metabolism by gut bacteria reveals novel catalytic functions.肠道细菌复杂的果胶代谢揭示了新的催化功能。
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MEGA7: Molecular Evolutionary Genetics Analysis Version 7.0 for Bigger Datasets.MEGA7：适用于更大数据集的分子进化遗传学分析版本7.0
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Enzymatic Synthesis of Rhamnose Containing Chemicals by Reverse Hydrolysis.通过逆水解酶促合成含鼠李糖的化合物。
PLoS One. 2015 Oct 27;10(10):e0140531. doi: 10.1371/journal.pone.0140531. eCollection 2015.
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Crystal structure of a novel two domain GH78 family α-rhamnosidase from Klebsiella oxytoca with rhamnose bound.来自产酸克雷伯菌的一种新型双结构域GH78家族α-鼠李糖苷酶与鼠李糖结合的晶体结构。
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Differential Metabolism of Exopolysaccharides from Probiotic Lactobacilli by the Human Gut Symbiont Bacteroides thetaiotaomicron.人肠道共生菌嗜热栖粪杆菌对益生菌乳酸杆菌胞外多糖的差异代谢
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Biotransformation of rutin to isoquercitrin using recombinant α-L-rhamnosidase from Bifidobacterium breve.利用来自短双歧杆菌的重组α-L-鼠李糖苷酶将芦丁生物转化为异槲皮苷。
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Human gut Bacteroidetes can utilize yeast mannan through a selfish mechanism.人类肠道拟杆菌可通过一种自私机制利用酵母甘露聚糖。
Nature. 2015 Jan 8;517(7533):165-169. doi: 10.1038/nature13995.
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Automatic prediction of polysaccharide utilization loci in Bacteroidetes species.自动预测拟杆菌门物种中的多糖利用基因座。
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Metabolism of rutin and poncirin by human intestinal microbiota and cloning of their metabolizing α-L-rhamnosidase from Bifidobacterium dentium.人肠道微生物群对芦丁和枳属苷的代谢及其代谢型α-L-鼠李糖苷酶的克隆，该酶来自龋齿双歧杆菌。
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10
The metagenome-derived enzyme RhaB opens a new subclass of bacterial B type α-L-rhamnosidases.宏基因组来源的酶RhaB开创了细菌B型α-L-鼠李糖苷酶的一个新亚类。
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来自VPI-5482的糖苷水解酶家族78 α-L-鼠李糖苷酶的特性及功能残基的鉴定

Characterization of a glycoside hydrolase family 78 α-l-rhamnosidase from VPI-5482 and identification of functional residues.

作者信息

Li Binchun, Ji Yaru, Li Yanqin, Ding Guobin

机构信息

Key Laboratory of Chemical Biology and Molecular Engineering of Ministry of Education, Institute of Biotechnology, Shanxi University, Taiyuan, 030006 China.

出版信息

3 Biotech. 2018 Feb;8(2):120. doi: 10.1007/s13205-018-1139-9. Epub 2018 Feb 8.

DOI:10.1007/s13205-018-1139-9
PMID:29430381
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC5805665/
Abstract

A putative glycoside hydrolase family 78 α-l-rhamnosidase BtRha78A from VPI-5482 was heterologously over-expressed in . Enzymatic properties of recombinant BtRha78A were characterized in detail. Recombinant BtRha78A might efficiently hydrolyze -nitrophenyl α-l-rhamnopyranoside. BtRha78A displayed the highest activity at 60 °C in pH 6.5. BtRha78A exhibited a good pH stability and relatively high thermostability. BtRha78A could be tolerant of a low concentration of alcohols. These attractive advantages made it a promising alternative biocatalyst for industrial applications. The catalytic general acid Asp335 and general base Glu595 of BtRha78A were confirmed by site-directed mutagenesis. Alanine scanning mutagenesis based on sequence alignment and structural analysis revealed that the conserved residues Asp330, Arg334, Trp339, Asp342, Tyr383, Trp440, and His620 were crucial for enzyme catalysis. Most functional residues located at the conserved general acid motif (Asp330-Asp342) and were completely conserved in the subfamily I Rha78s.

摘要

来自VPI-5482的一种假定的糖苷水解酶家族78α-L-鼠李糖苷酶BtRha78A在[具体表达宿主未给出]中进行了异源过表达。对重组BtRha78A的酶学性质进行了详细表征。重组BtRha78A可能有效地水解对硝基苯基α-L-鼠李糖苷。BtRha78A在60℃、pH 6.5时表现出最高活性。BtRha78A表现出良好的pH稳定性和相对较高的热稳定性。BtRha78A能够耐受低浓度的醇类。这些吸引人的优点使其成为工业应用中一种有前景的替代生物催化剂。通过定点诱变证实了BtRha78A的催化通用酸Asp335和通用碱Glu595。基于序列比对和结构分析的丙氨酸扫描诱变表明，保守残基Asp330、Arg334、Trp339、Asp342、Tyr383、Trp440和His620对酶催化至关重要。大多数功能残基位于保守的通用酸基序（Asp330-Asp342），并且在亚家族I Rha78中完全保守。