A chondroitin sulfate and hyaluronic acid lyase with poor activity to glucuronyl 4,6-O-disulfated N-acetylgalactosamine (E-type)–containing structures

Peng, Chune; Wang, Qingbin; Wang, Shumin; Wang, Wenshuang; Jiao, Runmiao; Han, Wenyuan; Li, Fuchuan

doi:10.1074/jbc.ra117.001238

Cited by 15 publications

(13 citation statements)

References 55 publications

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“…Although HCLase can digest the β-1,4-glycosidic bond between GalNAc and most disaccharide units, it is unable to act on the galactosaminidic linkage between GalNAc and the D unit, suggesting that the 2-O-sulfation of GlcA inhibits the action of HCLase, which is similar to the case of CSase AC I (Han et al, 2014). In contrast, HCLase Er from the same strain is the first identified CS lyase that is specifically inhibited by both 4-O-and 6-O-sulfation of GalNAc, which is very useful for selectively preparing E unit-rich oligosaccharides from CS polysaccharides (Peng et al, 2018). HCDLase is a novel exotype lyase from the same bacterial strain, which can degrade HA, CS and DS from their reducing end by sequentially releasing unsaturated disaccharides.…”

Section: Newly Identified Cs/ds Lyasesmentioning

confidence: 74%

Research and Application of Chondroitin Sulfate/Dermatan Sulfate-Degrading Enzymes

Wang

Shi

Qin

et al. 2020

Front. Cell Dev. Biol.

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Chondroitin sulfate (CS) and dermatan sulfate (DS) are widely distributed on the cell surface and in the extracellular matrix in the form of proteoglycan, where they participate in various biological processes. The diverse functions of CS/DS can be mainly attributed to their high structural variability. However, their structural complexity creates a big challenge for structural and functional studies of CS/DS. CS/DS-degrading enzymes with different specific activities are irreplaceable tools that could be used to solve this problem. Depending on the site of action, CS/DS-degrading enzymes can be classified as glycosidic bond-cleaving enzymes and sulfatases from animals and microorganisms. As discussed in this review, a few of the identified enzymes, particularly those from bacteria, have wildly applied to the basic studies and applications of CS/DS, such as disaccharide composition analysis, the preparation of bioactive oligosaccharides, oligosaccharide sequencing, and potential medical application, but these do not fulfill all of the needs in terms of the structural complexity of CS/DS.

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Section: Newly Identified Cs/ds Lyasesmentioning

confidence: 74%

Research and Application of Chondroitin Sulfate/Dermatan Sulfate-Degrading Enzymes

Wang

Shi

Qin

et al. 2020

Front. Cell Dev. Biol.

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“…Hence for example, a lyase from the marine bacterium Vibrio sp. FC509 has been used to isolate several CS-E oligosaccharides and their interaction with herpes simplex virus receptors has been analyzed [115]. As such, the bioactive domain in the binding to the virus has been established [115], opening the door to the development of new antiviral drugs (Figure 9).…”

Section: Oligosaccharide Mappingmentioning

confidence: 99%

“…FC509 has been used to isolate several CS-E oligosaccharides and their interaction with herpes simplex virus receptors has been analyzed [115]. As such, the bioactive domain in the binding to the virus has been established [115], opening the door to the development of new antiviral drugs (Figure 9). Knowledge of the oligosaccharide sequences that contain GAGs is an important prerequisite for a better understanding of their biological roles and the development of pharmaceuticals based on them.…”

Section: Oligosaccharide Mappingmentioning

confidence: 99%

“…FC509 has been used to isolate several CS-E oligosaccharides and their interaction with herpes simplex virus receptors has been analyzed [115]. As such, the bioactive domain in the binding to the virus has been established [115], opening the door to the development of new antiviral drugs (Figure 9). In a similar way, CS from shark fin cartilage has been digested with chondroitinase AC-I from Flavobacterium heparinum, an enzyme which cannot act on the galactosaminidic linkages bound to GlcA(2-O-sulfate)-GalNAc(6-O-sulfate) disaccharides (CS-D units) ( Figure 10A) [116].…”

Section: Oligosaccharide Mappingmentioning

confidence: 99%

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Chondroitin Sulfate-Degrading Enzymes as Tools for the Development of New Pharmaceuticals

et al. 2019

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Chondroitin sulfates are linear anionic sulfated polysaccharides found in biological tissues, mainly within the extracellular matrix, which are degraded and altered by specific lyases depending on specific time points. These polysaccharides have recently acquired relevance in the pharmaceutical industry due to their interesting therapeutic applications. As a consequence, chondroitin sulfate (CS) lyases have been widely investigated as tools for the development of new pharmaceuticals based on these polysaccharides. This review focuses on the major breakthrough represented by chondroitin sulfate-degrading enzymes and their structures and mechanisms of function in addition to their major applications.

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“…The purification, cloning, and sequencing of PCR products were completed at the Sangon Biotech (Shanghai) Co., Ltd. The sequencing products were listed on the Ezbiocloud website for homologous comparison [17] and the phylogenetic tree was constructed using MEGA7.0.26 software. Spore staining [18], capsule staining [19], flagellum staining [20] and gram staining [21] were carried out on high activity lyase strains and the specific morphologies of the strains were observed by scanning electron microscope [22].…”

Section: Physiological and Biochemical Identification Of Gellan-degramentioning

confidence: 99%

Screening and enzymatic activity of high-efficiency gellan lyase producing bacteria Pseudoalteromonas hodoensis PE1

Luo

et al. 2019

Bioengineered

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2019) Screening and enzymatic activity of high-efficiency gellan lyase producing bacteria Pseudoalteromonashodoensis PE1, Bioengineered, 10:1, 240-249, ABSTRACTGellan is a widely used microbial polysaccharide and one of the more effective ways to expand its application value would be to investigate the mechanism of gellan lyase and to produce gellan oligosaccharide. In this study, efficient gellan degrading bacteria were screened. One of the strains with high efficient gellan degradation capacity was labeled PE1. Through physiological and biochemical analysis of 16S rDNA, the species was identified as Pseudoalteromonas hodoensis. The optimum conditions for enzymatic activity and how it was affected by metal ions were determined, and the results showed that the lyase activities were much higher than those of previously reported (about 20 times). The gellan degradation products were determined by thinlayer chromatography and the oligosaccharides were determined by high-efficiency liquid chromatography to analyze the action site of lyase. This study laid a solid foundation which elucidates the production and application of gellan oligosaccharides. Research highlights• High efficiency gellan lyase producing bacteria • Optimization of reaction conditions for gellan degradation • Oligosaccharides were detected by TLC and HPLC to speculate the lyase action sites. ARTICLE HISTORY

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A chondroitin sulfate and hyaluronic acid lyase with poor activity to glucuronyl 4,6-O-disulfated N-acetylgalactosamine (E-type)–containing structures

Cited by 15 publications

References 55 publications

Research and Application of Chondroitin Sulfate/Dermatan Sulfate-Degrading Enzymes

Research and Application of Chondroitin Sulfate/Dermatan Sulfate-Degrading Enzymes

Chondroitin Sulfate-Degrading Enzymes as Tools for the Development of New Pharmaceuticals

Screening and enzymatic activity of high-efficiency gellan lyase producing bacteria Pseudoalteromonas hodoensis PE1

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