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KEGG pathways | MAP code | Pathways |
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MAP00511 | N-Glycan degradation | MAP00600 | Sphingolipid metabolism | MAP01032 | Glycan structures - degradation |
UniProtKB:Accession Number | P0C6E9 |
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Entry name | NANH_VIBCH |
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Activity | Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates. |
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Subunit | Monomer (Probable). |
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Subcellular location | Secreted. |
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Cofactor | Calcium. |
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Compound table: links to PDB-related databases & PoSSuM |
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| Cofactors | Substrates | Products | intermediates |
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KEGG-id | C00076 | C04730 | C06128 | C04884 | C04927 | C06139 | C06140 | C00001 | C00270 | C01290 | C02686 | C06135 | C04911 | C06140 | C06141 |
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Compound | Calcium | GM3 | N-Acetylneuraminyl-galactosylceramide | N-Acetyl-D-galactosaminyl-(N-acetylneuraminyl)-D-galactosyl-D-glucosylceramide | N-Acetylneuraminyl-D-galactosyl-N-acetyl-D-galactosaminyl-(N- acetylneuraminyl)-D-galactosyl-D-glucosylceramide | GQ1 | GT1b | H2O | N-Acetylneuraminate | beta-D-Galactosyl-1,4-beta-D-glucosylceramide | Galactosylceramide | GA2 | D-Galactosyl-N-acetyl-D-galactosaminyl-(N-acetylneuraminyl)-D-galactosyl-D-glucosylceramide | GT1b | GD1b |
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Type | divalent metal (Ca2+, Mg2+) | amide group,carbohydrate,carboxyl group,lipid,polysaccharide | amide group,carbohydrate,carboxyl group,lipid,polysaccharide | amide group,carbohydrate,carboxyl group,lipid,polysaccharide | amide group,carbohydrate,carboxyl group,lipid,polysaccharide | amide group,carbohydrate,carboxyl group,lipid,polysaccharide | amide group,carbohydrate,carboxyl group,lipid,polysaccharide | H2O | amide group,carbohydrate,carboxyl group | amide group,carbohydrate,lipid,polysaccharide | amide group,carbohydrate,lipid | amide group,carbohydrate,lipid,polysaccharide | amide group,carbohydrate,carboxyl group,lipid,polysaccharide | amide group,carbohydrate,carboxyl group,lipid,polysaccharide | amide group,carbohydrate,carboxyl group,lipid,polysaccharide |
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ChEBI | 29108
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PubChem | 271
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1kitA01 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
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1w0oA01 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
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1w0pA01 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
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1kitA02 |  |  |  |  |  |  |  | Bound:2x_CA | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
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1w0oA02 |  |  |  |  |  |  |  | Bound:2x_CA | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Transition-state-analogue:DAN |
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1w0pA02 |  |  |  |  |  |  |  | Bound:2x_CA | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
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1kitA03 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
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1w0oA03 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
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1w0pA03 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
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References for Catalytic Mechanism | References | Sections | No. of steps in catalysis |
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[4] | p.539-541 |
| [9] | Scheme 1, p.348 |
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references | [1] |
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PubMed ID | 1797392 |
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Journal | Carbohydr Res |
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Year | 1991 |
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Volume | 216 |
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Pages | 61-6 |
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Authors | Schreiner E, Zbiral E, Kleineidam RG, Schauer R |
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Title | 2,3-Didehydro-2-deoxysialic acids structurally varied at C-5 and their behaviour towards the sialidase from Vibrio cholerae. |
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[2] |
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Comments | CHARACTERIZATION, AND X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). |
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Medline ID | 92389334 |
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PubMed ID | 1518058 |
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Journal | J Mol Biol |
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Year | 1992 |
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Volume | 226 |
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Pages | 1287-90 |
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Authors | Taylor G, Vimr E, Garman E, Laver G |
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Title | Purification, crystallization and preliminary crystallographic study of neuraminidase from Vibrio cholerae and Salmonella typhimurium LT2. |
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Related UniProtKB | P37060 |
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[3] |
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PubMed ID | 8379920 |
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Journal | Biochem J |
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Year | 1993 |
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Volume | 294 |
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Pages | 653-6 |
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Authors | Guo X, Sinnott ML |
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Title | A kinetic-isotope-effect study of catalysis by Vibrio cholerae neuraminidase. |
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[4] |
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Comments | X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS). |
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Medline ID | 95006320 |
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PubMed ID | 7922030 |
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Journal | Structure |
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Year | 1994 |
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Volume | 2 |
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Pages | 535-44 |
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Authors | Crennell S, Garman E, Laver G, Vimr E, Taylor G |
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Title | Crystal structure of Vibrio cholerae neuraminidase reveals dual lectin-like domains in addition to the catalytic domain. |
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Related PDB | 1kit |
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Related UniProtKB | P37060 |
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[5] |
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PubMed ID | 8994884 |
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Journal | Curr Opin Struct Biol |
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Year | 1996 |
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Volume | 6 |
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Pages | 830-7 |
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Authors | Taylor G |
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Title | Sialidases: structures, biological significance and therapeutic potential. |
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[6] |
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PubMed ID | 10822584 |
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Journal | Org Lett |
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Year | 1999 |
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Volume | 1 |
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Pages | 443-6 |
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Authors | Wilson JC, Kiefel MJ, Angus DI, von Itzstein M |
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Title | Investigation of the stability of thiosialosides toward hydrolysis by sialidases using NMR spectroscopy. |
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[7] |
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PubMed ID | 12797770 |
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Journal | J Am Chem Soc |
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Year | 2003 |
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Volume | 125 |
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Pages | 7154-5 |
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Authors | Thobhani S, Ember B, Siriwardena A, Boons GJ |
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Title | Multivalency and the mode of action of bacterial sialidases. |
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[8] |
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Comments | X-ray crystallography |
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PubMed ID | 15226294 |
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Journal | J Biol Chem |
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Year | 2004 |
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Volume | 279 |
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Pages | 40819-26 |
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Authors | Moustafa I, Connaris H, Taylor M, Zaitsev V, Wilson JC, Kiefel MJ, von Itzstein M, Taylor G |
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Title | Sialic acid recognition by Vibrio cholerae neuraminidase. |
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Related PDB | 1w0o,1w0p |
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[9] |
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PubMed ID | 15211517 |
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Journal | Proteins |
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Year | 2004 |
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Volume | 56 |
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Pages | 346-53 |
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Authors | Haselhorst T, Wilson JC, Thomson RJ, McAtamney S, Menting JG, Coppel RL, von Itzstein M |
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Title | Saturation transfer difference (STD) 1H-NMR experiments and in silico docking experiments to probe the binding of N-acetylneuraminic acid and derivatives to Vibrio cholerae sialidase. |
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[10] |
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PubMed ID | 16128567 |
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Journal | Biochemistry |
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Year | 2005 |
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Volume | 44 |
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Pages | 11669-75 |
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Authors | Hinou H, Kurogochi M, Shimizu H, Nishimura S |
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Title | Characterization of Vibrio cholerae neuraminidase by a novel mechanism-based fluorescent labeling reagent. |
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comments | This enzyme belongs to the glycosidase family-33. This enzyme is composed of three domains. The central catalytic domain is flanked by two lectin-like domains. The catalytic domain of this enzyme is homologous to other glycosidase family-33 neuramidases (T00065 in EzCatDB). Although this enzyme binds two calcium ions, they are not involved in catalysis. Since the active site of this enzyme is conserved and the same as that of its homologous enzyme, sialidase from Micromonospora viridifaciens (T00065 in EzCatDB), the catalytic mechanism of this enzyme is the same as that of the homologous enzyme. Asp250 acts as a general acid-base, whilst Tyr740 acts as a nucleophile.
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created | updated |
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2006-12-06 | 2009-02-26 |
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