Functional characterization of a novel “ulvan utilization loci” found in Alteromonas sp. LOR genome

Foran, Elizabeth; Buravenkov, Vitaliy; Kopel, Moran; Mizrahi, Naama; Shoshani, Sivan; Helbert, William; Banin, Ehud

doi:10.1016/j.algal.2017.04.036

Cited by 42 publications

(47 citation statements)

References 22 publications

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“…LOR encode ulvan-degradation enzymes, such as β-glucuronyl hydrolase and rhamnosidase. 26) Many proteins are involved in the complete degradation of ulvan and there is still a need to elucidate the entire degradation pathway.…”

Section: Discussionmentioning

confidence: 99%

Characterization of an Alteromonas long-type ulvan lyase involved in the degradation of ulvan extracted from Ulva ohnoi

Muramatsu

Kato

et al. 2017

Bioscience, Biotechnology, and Biochemistry

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Ulvan is a sulfated polysaccharide found in the cell wall of the green algae Ulva. We first isolated several ulvan-utilizing Alteromonas sp. from the feces of small marine animals. The strain with the highest ulvan-degrading activity, KUL17, was analyzed further. We identified a 55-kDa ulvan-degrading protein secreted by this strain and cloned the gene encoding for it. The deduced amino acid sequence indicated that the enzyme belongs to polysaccharide lyase family 24 and thus the protein was named ulvan lyase. The predicted molecular mass of this enzyme is 110 kDa, which is different from that of the identified protein. By deletion analysis, the catalytic domain was proven to be located on the N-terminal half of the protein. KUL17 contains two ulvan lyases, one long and one short, but the secreted and cleaved long ulvan lyase was demonstrated to be the major enzyme for ulvan degradation.

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Section: Discussionmentioning

confidence: 99%

Characterization of an Alteromonas long-type ulvan lyase involved in the degradation of ulvan extracted from Ulva ohnoi

Muramatsu

Kato

et al. 2017

Bioscience, Biotechnology, and Biochemistry

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“…While PL28 and GH105 degrade ulvan, the other enzymes that were produced in Escherichia coli did not show activity 15 . This result suggested that a complex cascade of sequential enzymatic reactions is required for complete ulvan degradation 15,17 .…”

Section: Introductionmentioning

confidence: 97%

A marine bacterial enzymatic cascade degrades the algal polysaccharide ulvan

et al. 2019

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HAL is a multidisciplinary open access archive for the deposit and dissemination of scientific research documents, whether they are published or not. The documents may come from teaching and research institutions in France or abroad, or from public or private research centers. L'archive ouverte pluridisciplinaire HAL, est destinée au dépôt et à la diffusion de documents scientifiques de niveau recherche, publiés ou non, émanant des établissements d'enseignement et de recherche français ou étrangers, des laboratoires publics ou privés.

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“…Ulvan is made of two main repetitive disaccharide units. Type A ulvanobiourinic 3-sulfate has [34)-␤-D-GlcA-(134)-␣-L-Rha3S- (13] 2 and type B ulvanobiouronic 3-sulfate has [34)-␣-L-IdoA-(134)-␣-L-Rha3S (13] disaccharide units (Scheme 1) (7). The occurrence of a sulfate group in ulvan resembles the glycosaminoglycans present in vertebrates, and the presence of uronic acid makes it subject to depolymerization by a lytic mechanism.…”

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confidence: 99%

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

Ulaganathan

Banin

Helbert

et al. 2018

Journal of Biological Chemistry

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Ulvan is a complex sulfated polysaccharide present in the cell wall of green algae of the genus (Chlorophyta). The first ulvan-degrading polysaccharide lyases were identified several years ago, and more were discovered through genome sequencing of marine bacteria. Ulvan lyases are now grouped in three polysaccharide lyase (PL) families in the CAZy database, PL24, PL25, and PL28. The recently determined structures of the representative lyases from families PL24 and PL25 show that they adopt a seven-bladed β-propeller fold and utilize the His/Tyr catalytic mechanism. No structural information is yet available for PL28 ulvan lyases. NLR48 from belongs to PL28 together with its close paralog, NLR42. Biochemical studies of NLR42 have revealed that it can cleave ulvan next to both uronic acid epimers. We report the crystal structure of ulvan lyase NLR48 at 1.9-Å resolution. It has a β-jelly roll fold with an extended, deep, and positively charged substrate-binding cleft. Putative active-site residues were identified from the sequence conservation pattern, and their role was confirmed by site-directed mutagenesis. The structure of an inactive K162M mutant with a tetrasaccharide substrate showed the substrate occupying the "-" subsites. Comparison with lyases from other PL families with β-jelly roll folds supported assignment of the active site and explained its ability to degrade ulvan next to either epimer of uronic acid. NLR48 contains the His/Tyr catalytic machinery with Lys and Tyr playing the catalytic base/acid roles.

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Functional characterization of a novel “ulvan utilization loci” found in Alteromonas sp. LOR genome

Cited by 42 publications

References 22 publications

Characterization of an Alteromonas long-type ulvan lyase involved in the degradation of ulvan extracted from Ulva ohnoi

Characterization of an Alteromonas long-type ulvan lyase involved in the degradation of ulvan extracted from Ulva ohnoi

A marine bacterial enzymatic cascade degrades the algal polysaccharide ulvan

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

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