DB code: T00064
RLCP classification | 3.900.45300.71 : Transfer | |
---|---|---|
CATH domain | 2.60.120.200 : Jelly Rolls | |
2.120.10.10 : Neuraminidase | Catalytic domain | |
2.40.220.10 : Intramolecular trans-sialidase; domain 3 | ||
E.C. | 4.2.2.15 | |
CSA | 1sll | |
M-CSA | 1sll | |
MACiE |
CATH domain | Related DB codes (homologues) |
---|---|
2.120.10.10 : Neuraminidase | D00173 M00310 T00065 T00208 |
2.60.120.200 : Jelly Rolls | S00148 D00535 D00666 M00185 S00511 T00208 |
Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | CAZy | Pfam |
---|---|---|---|---|
Q27701 |
Anhydrosialidase
|
EC
4.2.2.15
Sialidase L Anhydroneuraminidase |
CBM40
(Carbohydrate-Binding Module Family 40)
GH33 (Glycoside Hydrolase Family 33) |
PF02973
(Sialidase)
[Graphical View] |
KEGG enzyme name |
---|
anhydrosialidase
anhydroneuraminidase sialglycoconjugate N-acylneuraminylhydrolase (2,7-cyclizing) sialidase L |
UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
---|---|---|---|---|---|
Q27701 | NANL_MACDE | Elimination of alpha-sialyl groups in N- acetylneuraminic acid glycosides, releasing 2,7-anhydro-alpha-N- acetylneuraminate. | Secreted, extracellular space. |
KEGG Pathways | Map code | Pathways | E.C. |
---|
Compound table | |||||||||
---|---|---|---|---|---|---|---|---|---|
Substrates | Products | Intermediates | |||||||
KEGG-id | C00270 | C04521 | C00001 | ||||||
E.C. | |||||||||
Compound | N-Acetylneuraminate | 2,7-Anhydro-alpha-N-acetylneuraminic acid | H2O | ||||||
Type | amide group,carbohydrate,carboxyl group | amide group,carbohydrate,carboxyl group | H2O | ||||||
ChEBI |
17012 17012 |
15377 15377 |
|||||||
PubChem |
439197 439197 |
440369 440369 |
22247451 962 22247451 962 |
||||||
1sliA01 | Unbound | Unbound | |||||||
1sllA01 | Unbound | Unbound | |||||||
2sliA01 | Unbound | Unbound | |||||||
3sliA01 | Unbound | Unbound | |||||||
4sliA01 | Unbound | Unbound | |||||||
1sliA02 | Unbound | Unbound | Intermediate-analogue:DAN | ||||||
1sllA02 | Unbound | Unbound | |||||||
2sliA02 | Unbound | Bound:SKD | |||||||
3sliA02 | Unbound | Bound:SKD | |||||||
4sliA02 | Analogue:CNP | Unbound | |||||||
1sliA03 | Unbound | Unbound | |||||||
1sllA03 | Unbound | Unbound | |||||||
2sliA03 | Unbound | Unbound | |||||||
3sliA03 | Unbound | Unbound | |||||||
4sliA03 | Unbound | Unbound |
Reference for Active-site residues | ||
---|---|---|
resource | references | E.C. |
Swiss-prot;Q27701 & literature [4] |
Active-site residues | ||||||||||
---|---|---|---|---|---|---|---|---|---|---|
PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
1sliA01 | ||||||||||
1sllA01 | ||||||||||
2sliA01 | ||||||||||
3sliA01 | ||||||||||
4sliA01 | ||||||||||
1sliA02 | ASP 318;GLU 595;TYR 713 | |||||||||
1sllA02 | ASP 318;GLU 595;TYR 713 | |||||||||
2sliA02 | ASP 318;GLU 595;TYR 713 | |||||||||
3sliA02 | ASP 318;GLU 595;TYR 713 | |||||||||
4sliA02 | ASP 318;GLU 595;TYR 713 | |||||||||
1sliA03 | ||||||||||
1sllA03 | ||||||||||
2sliA03 | ||||||||||
3sliA03 | ||||||||||
4sliA03 |
References for Catalytic Mechanism | ||
---|---|---|
References | Sections | No. of steps in catalysis |
[2]
|
Fig.4, p.526-528 | |
[4]
|
Fig.5, p.326-329 |
References | |
---|---|
[1] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 2254319 |
Journal | J Biol Chem |
Year | 1990 |
Volume | 265 |
Pages | 21629-33 |
Authors | Li YT, Nakagawa H, Ross SA, Hansson GC, Li SC |
Title | A novel sialidase which releases 2,7-anhydro-alpha-N-acetylneuraminic acid from sialoglycoconjugates. |
Related PDB | |
Related UniProtKB | |
[2] | |
Resource | |
Comments | X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 81-759. |
Medline ID | |
PubMed ID | 9562562 |
Journal | Structure |
Year | 1998 |
Volume | 6 |
Pages | 521-30 |
Authors | Luo Y, Li SC, Chou MY, Li YT, Luo M |
Title | The crystal structure of an intramolecular trans-sialidase with a NeuAc alpha2-->3Gal specificity. |
Related PDB | 1sli 1sll |
Related UniProtKB | Q27701 |
[3] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 10513893 |
Journal | Biosci Rep |
Year | 1999 |
Volume | 19 |
Pages | 163-8 |
Authors | Sonnino S, Brocca P, Acquotti D, Bernardi A, Raimondi L, Kiso M, Ishida H, Li SC, Li YT |
Title | The structural basis for the susceptibility of gangliosides to enzymatic degradation. |
Related PDB | |
Related UniProtKB | |
[4] | |
Resource | |
Comments | X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 81-759. |
Medline ID | |
PubMed ID | 9878409 |
Journal | J Mol Biol |
Year | 1999 |
Volume | 285 |
Pages | 323-32 |
Authors | Luo Y, Li SC, Li YT, Luo M |
Title | The 1.8 A structures of leech intramolecular trans-sialidase complexes: evidence of its enzymatic mechanism. |
Related PDB | 2sli 3sli 4sli |
Related UniProtKB | Q27701 |
Comments |
---|
According to the literature [2] & [4], (1) Tyr713 acts as a modulator, (2) Asp318 may act as a general acid to protonate the leaving O2 atom (probably through a water). (3) The departure of the leaving group leads to the oxocarbonium intermediate with a positive charge formed on C2 atom, (4) Asp318 acts as a general base, (5) The activated O7 atom makes a nucleophilic attack on the C2 atom to complete the reaction. |
Created | Updated |
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2005-04-18 | 2009-02-26 |