3.2.1.129: endo-alpha-sialidase

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For detailed information about endo-alpha-sialidase, go to the full flat file.

Reaction

Synonyms

alpha-2,8-sialosylhydrolase, endo-N, endo-N 1588, endo-N-acetylneuraminidase, endo-sialidase, endoE, EndoN Trap, endoN92, endoneuraminidase, endoneuraminidase-N, endoNF, EndoNt, endosialidase, endosialidase E, endosialidase NF, endosialidaseNF, G102, gp47, neuraminidase, endo-, poly(alpha-2,8-sialoside) alpha-2,8-sialosylhydrolase, poly(alpha-2,8-sialosyl) endo-N-acetylneuraminidase, poly(sialoside) alpha-2,8-sialosylhydrolase

ECTree

     3 Hydrolases

         3.2 Glycosylases

             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds

                3.2.1.129 endo-alpha-sialidase

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Results	in table
21	AA Sequence
12	Application
1	CAS Registry Number
14	Cloned(Commentary)
5	Crystallization (Commentary)
34	Disease/ Diagnostics
4	General Information
1	Inhibitors
15	KM Value [mM]
13	Molecular Weight [Da]
23	Natural Substrates/ Products (Substrates)
1	Organic Solvent Stability
34	Organism
27	PDB ID
2	pH Optimum
1	Posttranslational Modification
56	Protein Variants
14	Purification (Commentary)
1	Reaction
6	Reaction Type
34	Reference
10	Source Tissue
9	Specific Activity [micromol/min/mg]
61	Substrates and Products (Substrate)
11	Subunits
55	Synonyms
1	Systematic Name
8	Turnover Number [1/s]

Crystallization

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Crystallization on EC 3.2.1.129 - endo-alpha-sialidase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

in complex with a dimer of alpha-2,9-linked sialic acid, hanging drop vapor diffusion method, using 6% (w/v) PEG3350, 70 mM CHES buffer, pH 9.5 and 70 mM SrCl2

Enterobacteria phage phi92

I7HXG2

731018

crystal structure of the catalytic domain of endoN from caliphate K1F reveals a functional trimer, folding is mediated by an intramolecular C-terminal chaperone domain

Escherichia phage K1F

-

698998

hanging drop vapor diffusion method, using 16% (w/v) PEG 8000, 0.1 M Tris-HCl pH 7.2, 3% (v/v) 2-propanol

Escherichia phage K1F

-

701477

in complex with oligomeric sialic acid, 1.9 A resolution

Escherichia phage K1F

Q04830

666430

wild type endoNF cocrystallized with oligomeric sialic acid and mutant enzymes H350A and R647A are crystallized by the hanging drop vapor diffusion method, using

Escherichia phage K1F

Q04830

705185