Information on EC 4.2.2.15 - anhydrosialidase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
4.2.2.15
-
RECOMMENDED NAME
GeneOntology No.
anhydrosialidase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
elimination of alpha-sialyl groups in N-acetylneuraminic acid glycosides, releasing 2,7-anhydro-alpha-N-acetylneuraminate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
glycoconjugate sialyl-lyase (2,7-cyclizing)
Also acts on N-glycolylneuraminate glycosides. cf. EC 3.2.1.18 (exo-alpha-sialidase) and EC 3.2.1.129 (endo-alpha-sialidase).
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
alpha-(2,3)-specific trans-salidase
-
-
-
-
anhydroneuraminidase
-
-
-
-
EC 3.2.1.138
-
-
formerly
-
neuraminidase B
-
-
neuraminidase, anhydro-
-
-
-
-
sialglycoconjugate N-acylneuraminylhydrolase (2,7-cyclizing)
-
-
-
-
sialidase L
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
157857-11-9
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-methylumbelliferyl-alpha-N-acetylneuraminic acid + H2O
4-methylumbelliferone + 2,7-anhydro-alpha-N-acetylneuraminic acid
show the reaction diagram
-
only sialoglycoconjugates, not free alpha-N-acetylneuraminic acid
-
?
4-methylumbelliferyl-alpha-N-acetylneuraminic acid + H2O
4-methylumbelliferone + 2,7-anhydro-alpha-N-acetylneuraminic acid
show the reaction diagram
-
strict specificity towards the hydrolysis of NeuAcalpha(2-3)Gal-linkages
-
?
4-methylumbelliferyl-alpha-N-acetylneuraminic acid + H2O
4-methylumbelliferone + 2,7-anhydro-alpha-N-acetylneuraminic acid
show the reaction diagram
-
strict specificity towards the hydrolysis of NeuAcalpha(2-3)Gal-linkages
-
-
?
4-methylumbelliferyl-alpha-N-acetylneuraminic acid glycoproteins or ganglioside + H2O
2,7-anhydro-alpha-N-acetylneuraminic acid
show the reaction diagram
-
-
-
?
4-methylumbelliferyl-alpha-N-acetylneuraminic acid glycoproteins or ganglioside + H2O
2,7-anhydro-alpha-N-acetylneuraminic acid
show the reaction diagram
-
-
-
?
4-methylumbelliferyl-alpha-N-acetylneuraminic acid glycoproteins or ganglioside + H2O
2,7-anhydro-alpha-N-acetylneuraminic acid
show the reaction diagram
-
-
-
-
?
alpha-(2,3)-sialyl oligosacharides
?
show the reaction diagram
-
-
-
-
?
human alpha-1 acid glycoprotein + H2O
2,7-anhydro-alpha-N-acetylneuraminic acid + ?
show the reaction diagram
-
NanB preferentially cleaves alpha2-3 linked sialic acid from human alpha-1 glycoprotein
-
-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
4-methylumbelliferyl-alpha-N-acetylneuraminic acid glycoproteins or ganglioside + H2O
2,7-anhydro-alpha-N-acetylneuraminic acid
show the reaction diagram
-
-
-
?
4-methylumbelliferyl-alpha-N-acetylneuraminic acid glycoproteins or ganglioside + H2O
2,7-anhydro-alpha-N-acetylneuraminic acid
show the reaction diagram
-
-
-
?
4-methylumbelliferyl-alpha-N-acetylneuraminic acid glycoproteins or ganglioside + H2O
2,7-anhydro-alpha-N-acetylneuraminic acid
show the reaction diagram
-
-
-
-
?
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
-
not: 2-deoxy-2,3-dehydroacetylneuraminic acid, EDTA, Ca2+, Mg2+, Mn2+
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.68
-
4-methylumbelliferyl-alpha-N-acetylneuraminic acid
-
pH 5.5, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
-
assay at
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
-
-
isoelectric focusing
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 84000, SDS-PAGE
monomer
-
1* 83000
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
crystal structure of NanB in complex with its reaction product 2,7-anhydro-Neu5Ac is reported. NanB crystal structure consists of an N-terminal lectin-like domain (L-domain, residues 30-227), a catalytic six-bladed beta-propeller domain (N-domain, residues 228-345 and 457-697), and an irregular beta-stranded domain inserted into the catalytic domain (I-domain, residues 346-456)
-
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
50% loss of activity after one freeze and thawing cycle, in presence of 10% glycerol stable to several freeze and thawing cycles
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20°C, 10% glycerol, stable for more than 4 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Escherichia coli
-
NanB sequence lacking the first 29 residues is PCR-amplified from Streptococcus pneumoniae DNA, cloned into the pOPINF vector and expressed in Escherichia coli
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
synthesis
-
synthesis of sialyl oligosaccharides using enzyme, since it is difficult to obtain them from natural sources