Alginate lyase: Review of major sources and classification, properties, structure-function analysis and applications
Alginate lyases catalyze the degradation of alginate, a complex copolymer of α-L-guluronate and its C5 epimer β-D-mannuronate. The enzymes have been isolated from various kinds of organisms with different substrate specificities, including algae, marine mollusks, marine and terrestrial bacteria, and...
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| Veröffentlicht in: | Bioengineered 2015, Vol.6 (3), p.125-131 |
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| creator | Zhu, Benwei Yin, Heng |
| description | Alginate lyases catalyze the degradation of alginate, a complex copolymer of α-L-guluronate and its C5 epimer β-D-mannuronate. The enzymes have been isolated from various kinds of organisms with different substrate specificities, including algae, marine mollusks, marine and terrestrial bacteria, and some viruses and fungi. With the progress of structural biology, many kinds of alginate lyases of different polysaccharide lyases families have been characterized by obtaining crystal structures, and the catalytic mechanism has also been elucidated. Combined with various studies, we summarized the source, classification and properties of the alginate lyases from different polysaccharide lyases families. The relationship between substrate specificity and protein sequence was also investigated. |
| doi_str_mv | 10.1080/21655979.2015.1030543 |
| format | Article |
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The relationship between substrate specificity and protein sequence was also investigated.</description><subject>alginate lyase</subject><subject>Alginates - chemistry</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>applications</subject><subject>Bacteria - enzymology</subject><subject>classification</subject><subject>Fungi - enzymology</subject><subject>Glucuronic Acid - chemistry</subject><subject>Hexuronic Acids - chemistry</subject><subject>Invited</subject><subject>Molecular Sequence Data</subject><subject>Mollusca - enzymology</subject><subject>Oligosaccharides - biosynthesis</subject><subject>Polysaccharide-Lyases - chemistry</subject><subject>Polysaccharide-Lyases - genetics</subject><subject>Protein Conformation</subject><subject>structure</subject><subject>Substrate Specificity</subject><subject>Viruses - enzymology</subject><issn>2165-5979</issn><issn>2165-5987</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kU1r3DAQhkVpacI2P6FFxx7iRLIsf_RQGkK_IFAo7VnMjqVUQZZcSU7Yfx-Z3SztJRdJzDzvOyNeQt5ydsFZzy5r3ko5dMNFzbgsJcFkI16Q07VeyaHvXh7f3XBCzlK6Y4wVrpFd_5qc1LIXvACnJF-5W-sha-p2kPQH-lPfW_1Ag6ET3IVIU1gi6kTBjxQdpGSNRcg2-HM6xzDrmK1O5zTluGBeoq7M4nHtFwm4XbJ7LcyzOwjTG_LKgEv67HBvyO8vn39df6tufnz9fn11U6EUTa6acm454z3vgGOL0mwRsdGGlW_UNWDptNhzhC3owbCuG0eQhslaS2C9EBvyce87L9tJj6h9juDUHO0EcacCWPV_x9s_6jbcq6ZlvC4OG_L-YBDD30WnrCabUDsHXoclKd72TSOYGFZU7lGMIaWozXEMZ2oNTT2FptbQ1CG0onv3745H1VNEBfi0B6w3IU7wEKIbVYadC9FE8GiTEs_PeAS8q6nU</recordid><startdate>2015</startdate><enddate>2015</enddate><creator>Zhu, Benwei</creator><creator>Yin, Heng</creator><general>Taylor & Francis</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>2015</creationdate><title>Alginate lyase: Review of major sources and classification, properties, structure-function analysis and applications</title><author>Zhu, Benwei ; Yin, Heng</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c534t-4534b101817a1c6c5fbccc4ef045722ac1816c81cabae9f077dda5f052e5a0833</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2015</creationdate><topic>alginate lyase</topic><topic>Alginates - chemistry</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>applications</topic><topic>Bacteria - enzymology</topic><topic>classification</topic><topic>Fungi - enzymology</topic><topic>Glucuronic Acid - chemistry</topic><topic>Hexuronic Acids - chemistry</topic><topic>Invited</topic><topic>Molecular Sequence Data</topic><topic>Mollusca - enzymology</topic><topic>Oligosaccharides - biosynthesis</topic><topic>Polysaccharide-Lyases - chemistry</topic><topic>Polysaccharide-Lyases - genetics</topic><topic>Protein Conformation</topic><topic>structure</topic><topic>Substrate Specificity</topic><topic>Viruses - enzymology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zhu, Benwei</creatorcontrib><creatorcontrib>Yin, Heng</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Bioengineered</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zhu, Benwei</au><au>Yin, Heng</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Alginate lyase: Review of major sources and classification, properties, structure-function analysis and applications</atitle><jtitle>Bioengineered</jtitle><addtitle>Bioengineered</addtitle><date>2015</date><risdate>2015</risdate><volume>6</volume><issue>3</issue><spage>125</spage><epage>131</epage><pages>125-131</pages><issn>2165-5979</issn><eissn>2165-5987</eissn><abstract>Alginate lyases catalyze the degradation of alginate, a complex copolymer of α-L-guluronate and its C5 epimer β-D-mannuronate. The enzymes have been isolated from various kinds of organisms with different substrate specificities, including algae, marine mollusks, marine and terrestrial bacteria, and some viruses and fungi. With the progress of structural biology, many kinds of alginate lyases of different polysaccharide lyases families have been characterized by obtaining crystal structures, and the catalytic mechanism has also been elucidated. Combined with various studies, we summarized the source, classification and properties of the alginate lyases from different polysaccharide lyases families. The relationship between substrate specificity and protein sequence was also investigated.</abstract><cop>United States</cop><pub>Taylor & Francis</pub><pmid>25831216</pmid><doi>10.1080/21655979.2015.1030543</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central |
| subjects | alginate lyase Alginates - chemistry Amino Acid Sequence Animals applications Bacteria - enzymology classification Fungi - enzymology Glucuronic Acid - chemistry Hexuronic Acids - chemistry Invited Molecular Sequence Data Mollusca - enzymology Oligosaccharides - biosynthesis Polysaccharide-Lyases - chemistry Polysaccharide-Lyases - genetics Protein Conformation structure Substrate Specificity Viruses - enzymology |
| title | Alginate lyase: Review of major sources and classification, properties, structure-function analysis and applications |
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