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海洋细菌粘沙赤壳菌 CZ1127 中的岩藻聚糖硫酸酯酶

Fucoidan Sulfatases from Marine Bacterium Wenyingzhuangia fucanilytica CZ1127.

机构信息

Laboratory of Enzyme Chemistry, G.B. Elyakov Pacific Institute of Bioorganic Chemistry, Far-Eastern Branch of the Russian Academy of Sciences, 159, Prospect 100-let Vladivostoku, 690022 Vladivostok, Russia.

School of Natural Sciences, Far-Eastern Federal University, 8, Sukhanova, st., 690091 Vladivostok, Russia.

出版信息

Biomolecules. 2018 Sep 21;8(4):98. doi: 10.3390/biom8040098.

DOI:10.3390/biom8040098
PMID:30248971
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC6315715/
Abstract

Fucoidans belong to a structurally heterogeneous class of sulfated polysaccharides isolated from brown algae. They have a wide spectrum of biological activities. The complex structures of these polysaccharides hinder structure-activity relationships determination. Fucoidan sulfatases can make useful tools for the determination of the fine chemical structure of fucoidans. In this study, identification and preparation of two recombinant sulfatases able to catalyze the cleavage of sulfate groups from fragments of fucoidan molecules is described for the first time. Two genes of sulfatases and of the marine bacterium CZ1127 were cloned and the proteins were produced in cells. Sulfatases SWF1 and SWF4 are assigned to S1_17 and S1_25 subfamilies of formylglycine-dependent enzymes of S1 family (SulfAtlas). Some molecular and biochemical characteristics of recombinant fucoidan sulfatases have been studied. Detailed specificity and catalytic features of sulfatases were determined using various sulfated fucooligosaccharides. Structures of products produced by SWF1 and SWF4 were established by nuclear magnetic resonance (NMR) spectroscopy. Based on the obtained data, the enzymes are classified as fucoidan -2-sulfatase (SWF1) and fucoidan -3-sulfatase (SWF4). In addition, we demonstrated the sequential action of sulfatases on 2,3-di--sulfated fucooligosacchrides, which indicates an exolitic degradation pathway of fucoidan by a marine bacterium CZ1127.

摘要

岩藻聚糖属于从褐藻中分离得到的结构多样的硫酸化多糖类。它们具有广泛的生物活性。这些多糖的复杂结构阻碍了结构-活性关系的确定。岩藻聚糖硫酸酯酶可以作为确定岩藻聚糖精细化学结构的有用工具。本研究首次描述了两种能够催化岩藻聚糖分子片段硫酸基团裂解的重组硫酸酯酶的鉴定和制备。从海洋细菌 CZ1127 中克隆了两种硫酸酯酶 和 的基因，并在 细胞中表达了这些蛋白质。SWF1 和 SWF4 硫酸酯酶被分配到 S1_17 和 S1_25 亚家族的依赖于甲酰甘氨酸的 S1 家族酶（SulfAtlas）。研究了重组岩藻聚糖硫酸酯酶的一些分子和生化特性。使用各种硫酸化岩藻寡糖详细确定了硫酸酯酶的特异性和催化特征。通过核磁共振（NMR）光谱法确定了 SWF1 和 SWF4 产生的产物的结构。基于获得的数据，将这些酶分类为岩藻聚糖-2-硫酸酯酶（SWF1）和岩藻聚糖-3-硫酸酯酶（SWF4）。此外，我们证明了硫酸酯酶对 2,3-二--硫酸化岩藻寡糖的顺序作用，这表明海洋细菌 CZ1127 对岩藻聚糖的降解途径是外切酶途径。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/de85/6315715/a3238cddac48/biomolecules-08-00098-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/de85/6315715/64abb07d9b38/biomolecules-08-00098-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/de85/6315715/18b2cf78441b/biomolecules-08-00098-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/de85/6315715/23d77976f1f5/biomolecules-08-00098-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/de85/6315715/adfb2630ffa6/biomolecules-08-00098-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/de85/6315715/b3c25f0f3092/biomolecules-08-00098-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/de85/6315715/c557b6127528/biomolecules-08-00098-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/de85/6315715/a3238cddac48/biomolecules-08-00098-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/de85/6315715/64abb07d9b38/biomolecules-08-00098-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/de85/6315715/18b2cf78441b/biomolecules-08-00098-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/de85/6315715/23d77976f1f5/biomolecules-08-00098-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/de85/6315715/adfb2630ffa6/biomolecules-08-00098-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/de85/6315715/b3c25f0f3092/biomolecules-08-00098-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/de85/6315715/c557b6127528/biomolecules-08-00098-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/de85/6315715/a3238cddac48/biomolecules-08-00098-g007.jpg

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