<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>291(30)</volume><submitter>Inoue A</submitter><pubmed_abstract>Extremophiles are expected to represent a source of enzymes having unique functional properties. The hypothetical protein NIS_0185, termed NitAly in this study, was identified as an alginate lyase-homolog protein in the genomic database of ϵ-Proteobacteria Nitratiruptor sp. SB155-2, which was isolated from deep-sea hydrothermal vents at a water depth of 1,000 m. Among the characterized alginate lyases in the polysaccharide lyase family 7 (PL-7), the amino acid sequence of NitAly showed the highest identity (39%) with that of red alga Pyropia yezoensis alginate lyase PyAly. Recombinant NitAly (rNitAly) was successfully expressed in Escherichia coli Purified rNitAly degraded alginate in an endolytic manner. Among alginate block types, polyM was preferable to polyG and polyMG as a substrate, </pubmed_abstract><journal>The Journal of biological chemistry</journal><pagination>15551-63</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC4957041</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Discovery of a Novel Alginate Lyase from Nitratiruptor sp. SB155-2 Thriving at Deep-sea Hydrothermal Vents and Identification of the Residues Responsible for Its Heat Stability.</pubmed_title><pmcid>PMC4957041</pmcid><pubmed_authors>Inoue A</pubmed_authors><pubmed_authors>Anraku M</pubmed_authors><pubmed_authors>Nakagawa S</pubmed_authors><pubmed_authors>Ojima T</pubmed_authors></additional><is_claimable>false</is_claimable><name>Discovery of a Novel Alginate Lyase from Nitratiruptor sp. SB155-2 Thriving at Deep-sea Hydrothermal Vents and Identification of the Residues Responsible for Its Heat Stability.</name><description>Extremophiles are expected to represent a source of enzymes having unique functional properties. The hypothetical protein NIS_0185, termed NitAly in this study, was identified as an alginate lyase-homolog protein in the genomic database of ϵ-Proteobacteria Nitratiruptor sp. SB155-2, which was isolated from deep-sea hydrothermal vents at a water depth of 1,000 m. Among the characterized alginate lyases in the polysaccharide lyase family 7 (PL-7), the amino acid sequence of NitAly showed the highest identity (39%) with that of red alga Pyropia yezoensis alginate lyase PyAly. Recombinant NitAly (rNitAly) was successfully expressed in Escherichia coli Purified rNitAly degraded alginate in an endolytic manner. Among alginate block types, polyM was preferable to polyG and polyMG as a substrate, </description><dates><release>2016-01-01T00:00:00Z</release><publication>2016 Jul</publication><modification>2025-04-22T18:42:49.93Z</modification><creation>2019-03-27T02:18:56Z</creation></dates><accession>S-EPMC4957041</accession><cross_references><pubmed>27231344</pubmed><doi>10.1074/jbc.M115.713230</doi><doi>10.1074/jbc.m115.713230</doi></cross_references></HashMap>