Discovery of a new type of sialidase, "KDNase," which specifically hydrolyzes deaminoneuraminyl (3-deoxy-D-glycero-D-galacto-2-nonulosonic acid) but not N-acylneuraminyl linkages
The release of 3-deoxy-D-glycero-D-galacto-2-nonulosonic acid (KDN, deaminoneuraminic acid) residues from their alpha-ketosidic linkage is required to determine the structural and functional role of KDN-glycoconjugates in sources as disparate as trout egg polysialoglycoproteins and human cancers. We...
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| Veröffentlicht in: | The Journal of biological chemistry 1994-08, Vol.269 (34), p.21415-21419 |
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| creator | K Kitajima H Kuroyanagi S Inoue J Ye F A Troy, 2nd Y Inoue |
| description | The release of 3-deoxy-D-glycero-D-galacto-2-nonulosonic acid (KDN, deaminoneuraminic acid) residues from their alpha-ketosidic
linkage is required to determine the structural and functional role of KDN-glycoconjugates in sources as disparate as trout
egg polysialoglycoproteins and human cancers. We report for the first time the isolation and characterization of a novel type
of sialidase (KDNase), which specifically hydrolyzes KDN ketosidic but not N-acylneuraminyl linkages. KDNase activity was
assayed using 4-methylumbelliferyl KDN (4-MU-KDN). A KDNase-producing microorganism was identified as Sphingobacterium multivorum.
The affinity-purified enzyme was designated KDNase SM to denote its origin and that it was free of N-acylneuraminidase, proteolytic,
and other glycosidase activities. KDNase SM activity toward 4-MU-KDN was not inhibited by the N-acylneuraminidase inhibitor,
2,3-dehydro-2-deoxy-N-acetylneuraminic acid. KDNase SM released free KDN from naturally occurring substrates, including (KDN)GM3,
KDN-glycoprotein, which bears a number of O-linked chains of KDN alpha 2-->3Gal beta 1-->3GalNAc alpha 1-->3 (KDN alpha 2-->(-->8KDN
alpha 2-->)n-->6)GalNAc alpha 1-->, and the biantennary complex-type of N-glycan, KDN alpha 2-->3Gal beta 1-->4GlcNAc beta
1-->2Man alpha 1-->6(KDN alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4GlcNAc beta 1-->4GlcNAc.
KDNase SM thus exhibited a broad linkage specificity and was able to hydrolyze the KDN residues ketosidically linked alpha
2-->3, alpha 2-->6, and alpha 2-->8. The enzyme did not release Neu5Ac or Neu5Gc from 4-MU-Neu5Ac, N-acetyl-neuraminyllactose,
colominic acid, or other Sia(Neu5Ac or Neu5Gc)-containing glycoconjugates. |
| doi_str_mv | 10.1016/S0021-9258(17)31819-7 |
| format | Article |
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linkage is required to determine the structural and functional role of KDN-glycoconjugates in sources as disparate as trout
egg polysialoglycoproteins and human cancers. We report for the first time the isolation and characterization of a novel type
of sialidase (KDNase), which specifically hydrolyzes KDN ketosidic but not N-acylneuraminyl linkages. KDNase activity was
assayed using 4-methylumbelliferyl KDN (4-MU-KDN). A KDNase-producing microorganism was identified as Sphingobacterium multivorum.
The affinity-purified enzyme was designated KDNase SM to denote its origin and that it was free of N-acylneuraminidase, proteolytic,
and other glycosidase activities. KDNase SM activity toward 4-MU-KDN was not inhibited by the N-acylneuraminidase inhibitor,
2,3-dehydro-2-deoxy-N-acetylneuraminic acid. KDNase SM released free KDN from naturally occurring substrates, including (KDN)GM3,
KDN-glycoprotein, which bears a number of O-linked chains of KDN alpha 2-->3Gal beta 1-->3GalNAc alpha 1-->3 (KDN alpha 2-->(-->8KDN
alpha 2-->)n-->6)GalNAc alpha 1-->, and the biantennary complex-type of N-glycan, KDN alpha 2-->3Gal beta 1-->4GlcNAc beta
1-->2Man alpha 1-->6(KDN alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4GlcNAc beta 1-->4GlcNAc.
KDNase SM thus exhibited a broad linkage specificity and was able to hydrolyze the KDN residues ketosidically linked alpha
2-->3, alpha 2-->6, and alpha 2-->8. The enzyme did not release Neu5Ac or Neu5Gc from 4-MU-Neu5Ac, N-acetyl-neuraminyllactose,
colominic acid, or other Sia(Neu5Ac or Neu5Gc)-containing glycoconjugates.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(17)31819-7</identifier><identifier>PMID: 8063773</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Bacteria - enzymology ; Carbohydrate Sequence ; Cations, Divalent - pharmacology ; Chromatography, Affinity ; Glycoconjugates - metabolism ; Glycosides - metabolism ; Hydrogen-Ion Concentration ; Molecular Sequence Data ; N-Acetylneuraminic Acid ; Neuraminidase - antagonists & inhibitors ; Neuraminidase - metabolism ; Sialic Acids - metabolism ; Sphingobacterium multivorum ; Substrate Specificity ; Sugar Acids - metabolism</subject><ispartof>The Journal of biological chemistry, 1994-08, Vol.269 (34), p.21415-21419</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c411t-c3180a3d99ac9ca9c54dc9731d62aef3bccd2c4ce06b47a54c283a5e578f675a3</citedby><cites>FETCH-LOGICAL-c411t-c3180a3d99ac9ca9c54dc9731d62aef3bccd2c4ce06b47a54c283a5e578f675a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8063773$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>K Kitajima</creatorcontrib><creatorcontrib>H Kuroyanagi</creatorcontrib><creatorcontrib>S Inoue</creatorcontrib><creatorcontrib>J Ye</creatorcontrib><creatorcontrib>F A Troy, 2nd</creatorcontrib><creatorcontrib>Y Inoue</creatorcontrib><title>Discovery of a new type of sialidase, "KDNase," which specifically hydrolyzes deaminoneuraminyl (3-deoxy-D-glycero-D-galacto-2-nonulosonic acid) but not N-acylneuraminyl linkages</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>The release of 3-deoxy-D-glycero-D-galacto-2-nonulosonic acid (KDN, deaminoneuraminic acid) residues from their alpha-ketosidic
linkage is required to determine the structural and functional role of KDN-glycoconjugates in sources as disparate as trout
egg polysialoglycoproteins and human cancers. We report for the first time the isolation and characterization of a novel type
of sialidase (KDNase), which specifically hydrolyzes KDN ketosidic but not N-acylneuraminyl linkages. KDNase activity was
assayed using 4-methylumbelliferyl KDN (4-MU-KDN). A KDNase-producing microorganism was identified as Sphingobacterium multivorum.
The affinity-purified enzyme was designated KDNase SM to denote its origin and that it was free of N-acylneuraminidase, proteolytic,
and other glycosidase activities. KDNase SM activity toward 4-MU-KDN was not inhibited by the N-acylneuraminidase inhibitor,
2,3-dehydro-2-deoxy-N-acetylneuraminic acid. KDNase SM released free KDN from naturally occurring substrates, including (KDN)GM3,
KDN-glycoprotein, which bears a number of O-linked chains of KDN alpha 2-->3Gal beta 1-->3GalNAc alpha 1-->3 (KDN alpha 2-->(-->8KDN
alpha 2-->)n-->6)GalNAc alpha 1-->, and the biantennary complex-type of N-glycan, KDN alpha 2-->3Gal beta 1-->4GlcNAc beta
1-->2Man alpha 1-->6(KDN alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4GlcNAc beta 1-->4GlcNAc.
KDNase SM thus exhibited a broad linkage specificity and was able to hydrolyze the KDN residues ketosidically linked alpha
2-->3, alpha 2-->6, and alpha 2-->8. The enzyme did not release Neu5Ac or Neu5Gc from 4-MU-Neu5Ac, N-acetyl-neuraminyllactose,
colominic acid, or other Sia(Neu5Ac or Neu5Gc)-containing glycoconjugates.</description><subject>Bacteria - enzymology</subject><subject>Carbohydrate Sequence</subject><subject>Cations, Divalent - pharmacology</subject><subject>Chromatography, Affinity</subject><subject>Glycoconjugates - metabolism</subject><subject>Glycosides - metabolism</subject><subject>Hydrogen-Ion Concentration</subject><subject>Molecular Sequence Data</subject><subject>N-Acetylneuraminic Acid</subject><subject>Neuraminidase - antagonists & inhibitors</subject><subject>Neuraminidase - metabolism</subject><subject>Sialic Acids - metabolism</subject><subject>Sphingobacterium multivorum</subject><subject>Substrate Specificity</subject><subject>Sugar Acids - metabolism</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc9u1DAQxiMEKkvhESpZFUKthMGOEzs5oi7_RFUOgMTNcsaTjcEbL3bCEh6LJyTpripuzGW-0XwzI80vy844e8EZly8_MZZzWudldcHVpeAVr6m6l604qwQVJf96P1vdWR5mj1L6xuYoan6SnVRMCqXEKvuzdgnCT4wTCS0xpMc9GaYdLlVyxjtrEj4n5x_WN4s4J_vOQUfSDsG1Doz3E-kmG4OffmMiFs3W9aHHMS5i8uRCUIvh10TXdOMnwBgWZbyBIdCczt7RhxR6B8SAs5ekGQfSh4HcUAOT_2eTd_13s8H0OHvQGp_wyTGfZl_evP589Y5ef3z7_urVNYWC84HC_BJmhK1rAzWYGsrCQq0EtzI32IoGwOZQADLZFMqUBeSVMCWWqmqlKo04zZ4d9u5i-DFiGvR2_hV6b3oMY9JKSllJlv_XyGUt58NqNpYHI8SQUsRW76LbmjhpzvQCVd9C1QsxzZW-haqXubPjgbHZor2bOlKc-08P_c5tur2LqBsXoMOtzmWtRaFzXvBS_AUMxawl</recordid><startdate>19940826</startdate><enddate>19940826</enddate><creator>K Kitajima</creator><creator>H Kuroyanagi</creator><creator>S Inoue</creator><creator>J Ye</creator><creator>F A Troy, 2nd</creator><creator>Y Inoue</creator><general>American Society for Biochemistry and Molecular Biology</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>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>19940826</creationdate><title>Discovery of a new type of sialidase, "KDNase," which specifically hydrolyzes deaminoneuraminyl (3-deoxy-D-glycero-D-galacto-2-nonulosonic acid) but not N-acylneuraminyl linkages</title><author>K Kitajima ; H Kuroyanagi ; S Inoue ; J Ye ; F A Troy, 2nd ; Y Inoue</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c411t-c3180a3d99ac9ca9c54dc9731d62aef3bccd2c4ce06b47a54c283a5e578f675a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Bacteria - enzymology</topic><topic>Carbohydrate Sequence</topic><topic>Cations, Divalent - pharmacology</topic><topic>Chromatography, Affinity</topic><topic>Glycoconjugates - metabolism</topic><topic>Glycosides - metabolism</topic><topic>Hydrogen-Ion Concentration</topic><topic>Molecular Sequence Data</topic><topic>N-Acetylneuraminic Acid</topic><topic>Neuraminidase - antagonists & inhibitors</topic><topic>Neuraminidase - metabolism</topic><topic>Sialic Acids - metabolism</topic><topic>Sphingobacterium multivorum</topic><topic>Substrate Specificity</topic><topic>Sugar Acids - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>K Kitajima</creatorcontrib><creatorcontrib>H Kuroyanagi</creatorcontrib><creatorcontrib>S Inoue</creatorcontrib><creatorcontrib>J Ye</creatorcontrib><creatorcontrib>F A Troy, 2nd</creatorcontrib><creatorcontrib>Y Inoue</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>K Kitajima</au><au>H Kuroyanagi</au><au>S Inoue</au><au>J Ye</au><au>F A Troy, 2nd</au><au>Y Inoue</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Discovery of a new type of sialidase, "KDNase," which specifically hydrolyzes deaminoneuraminyl (3-deoxy-D-glycero-D-galacto-2-nonulosonic acid) but not N-acylneuraminyl linkages</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1994-08-26</date><risdate>1994</risdate><volume>269</volume><issue>34</issue><spage>21415</spage><epage>21419</epage><pages>21415-21419</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>The release of 3-deoxy-D-glycero-D-galacto-2-nonulosonic acid (KDN, deaminoneuraminic acid) residues from their alpha-ketosidic
linkage is required to determine the structural and functional role of KDN-glycoconjugates in sources as disparate as trout
egg polysialoglycoproteins and human cancers. We report for the first time the isolation and characterization of a novel type
of sialidase (KDNase), which specifically hydrolyzes KDN ketosidic but not N-acylneuraminyl linkages. KDNase activity was
assayed using 4-methylumbelliferyl KDN (4-MU-KDN). A KDNase-producing microorganism was identified as Sphingobacterium multivorum.
The affinity-purified enzyme was designated KDNase SM to denote its origin and that it was free of N-acylneuraminidase, proteolytic,
and other glycosidase activities. KDNase SM activity toward 4-MU-KDN was not inhibited by the N-acylneuraminidase inhibitor,
2,3-dehydro-2-deoxy-N-acetylneuraminic acid. KDNase SM released free KDN from naturally occurring substrates, including (KDN)GM3,
KDN-glycoprotein, which bears a number of O-linked chains of KDN alpha 2-->3Gal beta 1-->3GalNAc alpha 1-->3 (KDN alpha 2-->(-->8KDN
alpha 2-->)n-->6)GalNAc alpha 1-->, and the biantennary complex-type of N-glycan, KDN alpha 2-->3Gal beta 1-->4GlcNAc beta
1-->2Man alpha 1-->6(KDN alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4GlcNAc beta 1-->4GlcNAc.
KDNase SM thus exhibited a broad linkage specificity and was able to hydrolyze the KDN residues ketosidically linked alpha
2-->3, alpha 2-->6, and alpha 2-->8. The enzyme did not release Neu5Ac or Neu5Gc from 4-MU-Neu5Ac, N-acetyl-neuraminyllactose,
colominic acid, or other Sia(Neu5Ac or Neu5Gc)-containing glycoconjugates.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>8063773</pmid><doi>10.1016/S0021-9258(17)31819-7</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0021-9258 |
| ispartof | The Journal of biological chemistry, 1994-08, Vol.269 (34), p.21415-21419 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_76668602 |
| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Bacteria - enzymology Carbohydrate Sequence Cations, Divalent - pharmacology Chromatography, Affinity Glycoconjugates - metabolism Glycosides - metabolism Hydrogen-Ion Concentration Molecular Sequence Data N-Acetylneuraminic Acid Neuraminidase - antagonists & inhibitors Neuraminidase - metabolism Sialic Acids - metabolism Sphingobacterium multivorum Substrate Specificity Sugar Acids - metabolism |
| title | Discovery of a new type of sialidase, "KDNase," which specifically hydrolyzes deaminoneuraminyl (3-deoxy-D-glycero-D-galacto-2-nonulosonic acid) but not N-acylneuraminyl linkages |
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