EzCatDB: T00208

DB codeT00208
RLCP classification1.31.36210.99
CATH domainDomain 12.60.120.200
Domain 22.120.10.10Catalytic domain
Domain 32.60.120.200
E.C.3.2.1.18

CATH domainRelated DB codes (homologues)
2.120.10.10D00173,M00310,T00064,T00065
2.60.120.200S00148,D00535,D00666,M00185,S00511,T00064

Enzyme Name
Swiss-protKEGG

P0C6E9
Protein nameSialidaseexo-alpha-sialidase
neuraminidase
sialidase
alpha-neuraminidase
acetylneuraminidase
SynonymsEC 3.2.1.18
Neuraminidase
NANase

KEGG pathways
MAP codePathways
MAP00511N-Glycan degradation
MAP00600Sphingolipid metabolism
MAP01032Glycan structures - degradation

Swiss-prot:Accession NumberP0C6E9
Entry nameNANH_VIBCH
ActivityHydrolysis 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.
SubunitMonomer (Probable).
Subcellular locationSecreted.
CofactorCalcium.


CofactorsSubstratesProductsintermediates
KEGG-idC00076C04730C06128C04884C04927C06139C06140C00001C00270C01290C02686C06135C04911C06140C06141
CompoundCalciumGM3N-Acetylneuraminyl-galactosylceramideN-Acetyl-D-galactosaminyl-(N-acetylneuraminyl)-D-galactosyl-D-glucosylceramideN-Acetylneuraminyl-D-galactosyl-N-acetyl-D-galactosaminyl-(N- acetylneuraminyl)-D-galactosyl-D-glucosylceramideGQ1GT1bH2ON-Acetylneuraminatebeta-D-Galactosyl-1,4-beta-D-glucosylceramideGalactosylceramideGA2D-Galactosyl-N-acetyl-D-galactosaminyl-(N-acetylneuraminyl)-D-galactosyl-D-glucosylceramideGT1bGD1b
Typedivalent metal (Ca2+, Mg2+)amide group,carbohydrate,carboxyl group,lipid,polysaccharideamide group,carbohydrate,carboxyl group,lipid,polysaccharideamide group,carbohydrate,carboxyl group,lipid,polysaccharideamide group,carbohydrate,carboxyl group,lipid,polysaccharideamide group,carbohydrate,carboxyl group,lipid,polysaccharideamide group,carbohydrate,carboxyl group,lipid,polysaccharideH2Oamide group,carbohydrate,carboxyl groupamide group,carbohydrate,lipid,polysaccharideamide group,carbohydrate,lipidamide group,carbohydrate,lipid,polysaccharideamide group,carbohydrate,carboxyl group,lipid,polysaccharideamide group,carbohydrate,carboxyl group,lipid,polysaccharideamide group,carbohydrate,carboxyl group,lipid,polysaccharide
1kitA01UnboundUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1w0oA01UnboundUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1w0pA01UnboundUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1kitA02Bound:2x_CAUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1w0oA02Bound:2x_CAUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundTransition-state-analogue:DAN
1w0pA02Bound:2x_CAUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1kitA03UnboundUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1w0oA03UnboundUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1w0pA03UnboundUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound

Active-site residues
resource
See T00065
pdbCatalytic residuesCofactor-binding residues
1kitA01

1w0oA01

1w0pA01

1kitA02ASP 250;GLU 619;TYR 740
ALA 253;ASN 256;ASP 289;THR 313(Calcium-1);PRO 548;ASP 621;ASP 682;ALA 683(Calcium-2)
1w0oA02ASP 250;GLU 619;TYR 740
ALA 253;ASN 256;ASP 289;THR 313(Calcium-1);PRO 548;ASP 621;ASP 682;ALA 683(Calcium-2)
1w0pA02ASP 250;GLU 619;TYR 740
ALA 253;ASN 256;ASP 289;THR 313(Calcium-1);PRO 548;ASP 621;ASP 682;ALA 683(Calcium-2)
1kitA03

1w0oA03

1w0pA03


References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[4]p.539-541
[9]Scheme 1, p.348

references
[1]
PubMed ID1797392
JournalCarbohydr Res
Year1991
Volume216
Pages61-6
AuthorsSchreiner E, Zbiral E, Kleineidam RG, Schauer R
Title2,3-Didehydro-2-deoxysialic acids structurally varied at C-5 and their behaviour towards the sialidase from Vibrio cholerae.
[2]
CommentsCHARACTERIZATION, AND X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
Medline ID92389334
PubMed ID1518058
JournalJ Mol Biol
Year1992
Volume226
Pages1287-90
AuthorsTaylor G, Vimr E, Garman E, Laver G
TitlePurification, crystallization and preliminary crystallographic study of neuraminidase from Vibrio cholerae and Salmonella typhimurium LT2.
Related Swiss-protP37060
[3]
PubMed ID8379920
JournalBiochem J
Year1993
Volume294
Pages653-6
AuthorsGuo X, Sinnott ML
TitleA kinetic-isotope-effect study of catalysis by Vibrio cholerae neuraminidase.
[4]
CommentsX-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
Medline ID95006320
PubMed ID7922030
JournalStructure
Year1994
Volume2
Pages535-44
AuthorsCrennell S, Garman E, Laver G, Vimr E, Taylor G
TitleCrystal structure of Vibrio cholerae neuraminidase reveals dual lectin-like domains in addition to the catalytic domain.
Related PDB1kit
Related Swiss-protP37060
[5]
PubMed ID8994884
JournalCurr Opin Struct Biol
Year1996
Volume6
Pages830-7
AuthorsTaylor G
TitleSialidases: structures, biological significance and therapeutic potential.
[6]
PubMed ID10822584
JournalOrg Lett
Year1999
Volume1
Pages443-6
AuthorsWilson JC, Kiefel MJ, Angus DI, von Itzstein M
TitleInvestigation of the stability of thiosialosides toward hydrolysis by sialidases using NMR spectroscopy.
[7]
PubMed ID12797770
JournalJ Am Chem Soc
Year2003
Volume125
Pages7154-5
AuthorsThobhani S, Ember B, Siriwardena A, Boons GJ
TitleMultivalency and the mode of action of bacterial sialidases.
[8]
CommentsX-ray crystallography
PubMed ID15226294
JournalJ Biol Chem
Year2004
Volume279
Pages40819-26
AuthorsMoustafa I, Connaris H, Taylor M, Zaitsev V, Wilson JC, Kiefel MJ, von Itzstein M, Taylor G
TitleSialic acid recognition by Vibrio cholerae neuraminidase.
Related PDB1w0o,1w0p
[9]
PubMed ID15211517
JournalProteins
Year2004
Volume56
Pages346-53
AuthorsHaselhorst T, Wilson JC, Thomson RJ, McAtamney S, Menting JG, Coppel RL, von Itzstein M
TitleSaturation 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.
[10]
PubMed ID16128567
JournalBiochemistry
Year2005
Volume44
Pages11669-75
AuthorsHinou H, Kurogochi M, Shimizu H, Nishimura S
TitleCharacterization of Vibrio cholerae neuraminidase by a novel mechanism-based fluorescent labeling reagent.

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.

createdupdated
2006-12-062009-02-26
Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2010)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)

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