Structural and functional characterization of PL28 family ulvan lyase NLR48 from Nonlabens ulvanivorans

Ulaganathan, ThirumalaiSelvi; Banin, Ehud; Helbert, William; Cygler, Mirosław

doi:10.1074/jbc.ra118.003659

Cited by 28 publications

(36 citation statements)

References 32 publications

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“…Furthermore, Rha3S can be modified by β-1,2-linked GlcA side chains and the GlcA-Rha3S or IdoA-Rha3S pattern can be interrupted by consecutive GlcA residues [7][8][9] . Increased interest in the enzymatic degradation of ulvan recently led to the description of several ulvan-active enzymes [10][11][12][13][14][15] . So far, and to the best of our knowledge, only two types of enzymes from different carbohydrate-active enzyme (CAZyme) families showed activity on ulvan.…”

Section: Introductionmentioning

confidence: 99%

A marine bacterial enzymatic cascade degrades the algal polysaccharide ulvan

et al. 2019

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Section: Introductionmentioning

confidence: 99%

A marine bacterial enzymatic cascade degrades the algal polysaccharide ulvan

et al. 2019

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“…Thus far, three ulvan lyase families have been established (), including PL24, PL25, and PL28. Structural characterizations of representative enzymes from these three families have also been reported [17,18,19]. As the primary ulvan-degrading enzyme [16], ulvan lyase catalyzes β-elimination at the internal bond between uronic acid and Rha3S, producing oligosaccharides with unsaturated uronic acid (∆GlcA) [14,15].…”

Section: Introductionmentioning

confidence: 99%

Cloning, Expression, and Characterization of a New PL25 Family Ulvan Lyase from Marine Bacterium Alteromonas sp. A321

Gao

Chi

et al. 2019

Marine Drugs

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Ulvan lyases can degrade ulvan to oligosaccharides with potent biological activity. A new ulvan lyase gene, ALT3695, was identified in Alteromonas sp. A321. Soluble expression of ALT3695 was achieved in Escherichia coli BL21 (DE3). The 1314-bp gene encoded a protein with 437 amino acid residues. The amino acid sequence of ALT3695 exhibited low sequence identity with polysaccharide lyase family 25 (PL25) ulvan lyases from Pseudoalteromonas sp. PLSV (64.14% identity), Alteromonas sp. LOR (62.68% identity), and Nonlabens ulvanivorans PLR (57.37% identity). Recombinant ALT3695 was purified and the apparent molecular weight was about 53 kDa, which is different from that of other polysaccharide-degrading enzymes identified in Alteromonas sp. A321. ALT3695 exhibited maximal activity in 50 mM Tris-HCl buffer at pH 8.0 and 50 °C. ALT3695 was relatively thermostable, as 90% activity was observed after incubation at 40 °C for 3 h. The Km and Vmax values of ALT3695 towards ulvan were 0.43 mg·mL−1 and 0.11 μmol·min−1·mL−1, respectively. ESI-MS analysis showed that enzymatic products were mainly disaccharides and tetrasaccharides. This study reports a new PL25 family ulvan lyase, ALT3695, with properties that suggest its great potential for the preparation of ulvan oligosaccharides.

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“…Ulvan lyases classified into 5 families, PL24, PL25, PL28, PL 37, and PL40, in the CAZy database ( Li et al, 2020 ) were isolated from several marine bacteria, such as genera, Alteromonas , Pseudoalteromonas, Formosa , and Nonlabens ( Kopel et al, 2016 ; Qin et al, 2018 ; Ulaganathan et al, 2018a ; Ulaganathan et al, 2018b ; Reisky et al, 2019 ). Ulvan lyases cleave between L-rhamnose 3-sulfate (Rha3S) and D-glucuronic acid (GlcA) or L-iduronic acid (IdoA).…”

Section: Resultsmentioning

confidence: 99%

Genes for degradation and utilization of uronic acid-containing polysaccharides of a marine bacteriumCatenovulumsp. CCB-QB4

Furusawa

Azami

Teh

2021

PeerJ

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Background Oligosaccharides from polysaccharides containing uronic acids are known to have many useful bioactivities. Thus, polysaccharide lyases (PLs) and glycoside hydrolases (GHs) involved in producing the oligosaccharides have attracted interest in both medical and industrial settings. The numerous polysaccharide lyases and glycoside hydrolases involved in producing the oligosaccharides were isolated from soil and marine microorganisms. Our previous report demonstrated that an agar-degrading bacterium, Catenovulum sp. CCB-QB4, isolated from a coastal area of Penang, Malaysia, possessed 183 glycoside hydrolases and 43 polysaccharide lyases in the genome. We expected that the strain might degrade and use uronic acid-containing polysaccharides as a carbon source, indicating that the strain has a potential for a source of novel genes for degrading the polysaccharides. Methods To confirm the expectation, the QB4 cells were cultured in artificial seawater media with uronic acid-containing polysaccharides, namely alginate, pectin (and saturated galacturonate), ulvan, and gellan gum, and the growth was observed. The genes involved in degradation and utilization of uronic acid-containing polysaccharides were explored in the QB4 genome using CAZy analysis and BlastP analysis. Results The QB4 cells were capable of using these polysaccharides as a carbon source, and especially, the cells exhibited a robust growth in the presence of alginate. 28 PLs and 22 GHs related to the degradation of these polysaccharides were found in the QB4 genome based on the CAZy database. Eleven polysaccharide lyases and 16 glycoside hydrolases contained lipobox motif, indicating that these enzymes play an important role in degrading the polysaccharides. Fourteen of 28 polysaccharide lyases were classified into ulvan lyase, and the QB4 genome possessed the most abundant ulvan lyase genes in the CAZy database. Besides, genes involved in uronic acid metabolisms were also present in the genome. These results were consistent with the cell growth. In the pectin metabolic pathway, the strain had genes for three different pathways. However, the growth experiment using saturated galacturonate exhibited that the strain can only use the pathway related to unsaturated galacturonate.

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Structural and functional characterization of PL28 family ulvan lyase NLR48 from Nonlabens ulvanivorans

Cited by 28 publications

References 32 publications

A marine bacterial enzymatic cascade degrades the algal polysaccharide ulvan

A marine bacterial enzymatic cascade degrades the algal polysaccharide ulvan

Cloning, Expression, and Characterization of a New PL25 Family Ulvan Lyase from Marine Bacterium Alteromonas sp. A321

Genes for degradation and utilization of uronic acid-containing polysaccharides of a marine bacteriumCatenovulumsp. CCB-QB4

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