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来自海洋细菌QA16的两种硫酸软骨素硫酸酯酶的鉴定及作用模式

Identification and Action Patterns of Two Chondroitin Sulfate Sulfatases From a Marine Bacterium sp. QA16.

作者信息

Wei Lin, Zhang Qingdong, Lu Danrong, Du Min, Xu Xiangyu, Wang Wenshuang, Zhang Yu-Zhong, Yuan Xunyi, Li Fuchuan

机构信息

National Glycoengineering Research Center, Shandong Key Laboratory of Carbohydrate Chemistry and Glycobiology, NMPA Key Laboratory for Quality Research and Evaluation of Carbohydrate-Based Medicine, Shandong University, Qingdao, China.

School of Life Sciences and Technology, Weifang Medical University, Weifang, China.

出版信息

Front Microbiol. 2022 Jan 24;12:775124. doi: 10.3389/fmicb.2021.775124. eCollection 2021.

DOI:10.3389/fmicb.2021.775124
PMID:35140691
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC8819143/
Abstract

Chondroitin sulfate (CS)/dermatan sulfate (DS) is a kind of sulfated polyanionic, linear polysaccharide belonging to glycosaminoglycan. CS/DS sulfatases, which specifically hydrolyze sulfate groups from CS/DS oligo-/polysaccharides, are potential tools for structural and functional studies of CD/DS. However, only a few sulfatases have been reported and characterized in detail to date. In this study, two CS/DS sulfatases, PB_3262 and PB_3285, were identified from the marine bacterium sp. QA16 and their action patterns were studied in detail. PB_3262 was characterized as a novel 4--endosulfatase that can effectively and specifically hydrolyze the 4--sulfate group of disaccharide GlcUAβ1-3GalNAc(4--sulfate) but not GlcUAβ1-3GalNAc(4,6--sulfate) and IdoUAα1-3GalNAc(4--sulfate) in CS/DS oligo-/polysaccharides, which is very different from the identified 4--endosulfatases in the substrate profile. In contrast, PB_3285 specifically hydrolyzes the 6--sulfate groups of GalNAc(6--sulfate) residues located at the reducing ends of the CS chains and is the first recombinantly expressed 6--exosulfatase to effectively act on CS oligosaccharides.

摘要

硫酸软骨素（CS）/硫酸皮肤素（DS）是一种硫酸化的聚阴离子线性多糖，属于糖胺聚糖。CS/DS硫酸酯酶能特异性地从CS/DS寡糖/多糖中水解硫酸基团，是研究CS/DS结构和功能的潜在工具。然而，迄今为止，仅有少数硫酸酯酶被报道并得到详细表征。在本研究中，从海洋细菌QA16中鉴定出两种CS/DS硫酸酯酶PB_3262和PB_3285，并对其作用模式进行了详细研究。PB_3262被鉴定为一种新型的4-硫酸酯酶，它能够有效且特异性地水解CS/DS寡糖/多糖中双糖GlcUAβ1-3GalNAc(4-硫酸酯)的4-硫酸基团，但不能水解GlcUAβ1-3GalNAc(4,6-硫酸酯)和IdoUAα1-3GalNAc(4-硫酸酯)，这在底物谱方面与已鉴定的4-硫酸酯酶有很大不同。相比之下，PB_3285特异性水解位于CS链还原端的GalNAc(6-硫酸酯)残基的6-硫酸基团，并且是第一个重组表达的能有效作用于CS寡糖的6-外硫酸酯酶。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ba1f/8819143/37117be89b12/fmicb-12-775124-g008.jpg
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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ba1f/8819143/f425fe59de03/fmicb-12-775124-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ba1f/8819143/2f0613f0b8e2/fmicb-12-775124-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ba1f/8819143/1090693531e0/fmicb-12-775124-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ba1f/8819143/37117be89b12/fmicb-12-775124-g008.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ba1f/8819143/4283452460f0/fmicb-12-775124-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ba1f/8819143/7f3ea87d04ad/fmicb-12-775124-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ba1f/8819143/f2227721df92/fmicb-12-775124-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ba1f/8819143/3eeb61181e31/fmicb-12-775124-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ba1f/8819143/f425fe59de03/fmicb-12-775124-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ba1f/8819143/2f0613f0b8e2/fmicb-12-775124-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ba1f/8819143/1090693531e0/fmicb-12-775124-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ba1f/8819143/37117be89b12/fmicb-12-775124-g008.jpg

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