<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Wang XH</submitter><funding>National Science Foundation of China</funding><pagination>e0155922</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC9746311</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>88(23)</volume><pubmed_abstract>Alginate lyases play a vital role in the degradation of alginate, an important marine carbon source. Alginate is a complex macromolecular substrate, and the synergy of alginate lyases is important for the alginate utilization by microbes and the application of alginate lyases in biotechnology. Although many studies have focused on the synergy between different alginate lyases, the synergy between two alginate lyase domains of one alginate lyase has not been reported. Here, we report the synergism between the two catalytic domains of a novel alginate lyase, AlyC6', from the marine alginate-degrading bacterium &lt;i>Vibrio&lt;/i> sp. NC2. AlyC6' contains two PL7 catalytic domains (CD1 and CD2) that have no sequence similarity. While both CD1 and CD2 are endo-lyases with the highest activity at 30°</pubmed_abstract><journal>Applied and environmental microbiology</journal><pubmed_title>Synergy of the Two Alginate Lyase Domains of a Novel Alginate Lyase from &lt;i>Vibrio&lt;/i> sp. NC2 in Alginate Degradation.</pubmed_title><pmcid>PMC9746311</pmcid><funding_grant_id>31870052</funding_grant_id><funding_grant_id>32270047</funding_grant_id><funding_grant_id>42176229</funding_grant_id><funding_grant_id>U2006205</funding_grant_id><pubmed_authors>Sun XH</pubmed_authors><pubmed_authors>Li PY</pubmed_authors><pubmed_authors>Qin QL</pubmed_authors><pubmed_authors>Zhang YQ</pubmed_authors><pubmed_authors>Xu F</pubmed_authors><pubmed_authors>Wang XH</pubmed_authors><pubmed_authors>Chen XL</pubmed_authors></additional><is_claimable>false</is_claimable><name>Synergy of the Two Alginate Lyase Domains of a Novel Alginate Lyase from &lt;i>Vibrio&lt;/i> sp. NC2 in Alginate Degradation.</name><description>Alginate lyases play a vital role in the degradation of alginate, an important marine carbon source. Alginate is a complex macromolecular substrate, and the synergy of alginate lyases is important for the alginate utilization by microbes and the application of alginate lyases in biotechnology. Although many studies have focused on the synergy between different alginate lyases, the synergy between two alginate lyase domains of one alginate lyase has not been reported. Here, we report the synergism between the two catalytic domains of a novel alginate lyase, AlyC6', from the marine alginate-degrading bacterium &lt;i>Vibrio&lt;/i> sp. NC2. AlyC6' contains two PL7 catalytic domains (CD1 and CD2) that have no sequence similarity. While both CD1 and CD2 are endo-lyases with the highest activity at 30°</description><dates><release>2022-01-01T00:00:00Z</release><publication>2022 Dec</publication><modification>2025-04-19T10:24:29.761Z</modification><creation>2025-02-19T02:37:54.949Z</creation></dates><accession>S-EPMC9746311</accession><cross_references><pubmed>36394323</pubmed><doi>10.1128/aem.01559-22</doi></cross_references></HashMap>