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Information on EC 3.1.1.53 - sialate O-acetylesterase and Organism(s) Bovine coronavirus and UniProt Accession P15776

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     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.1 Carboxylic-ester hydrolases
                3.1.1.53 sialate O-acetylesterase
IUBMB Comments
Acts on free and glycosidically bound N-acetyl- or N-glycoloyl-neuraminic acid; acts mainly on the 4-O- and 9-O-acetyl groups. Also acts on some other O-acetyl esters, both cyclic and acyclic compounds, which are not sialic acids.
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Bovine coronavirus
UNIPROT: P15776
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Word Map
The taxonomic range for the selected organisms is: Bovine coronavirus
The enzyme appears in selected viruses and cellular organisms
Synonyms
hemagglutinin-esterase, hemagglutinin esterase, sialate-o-acetylesterase, sialic acid acetylesterase, sialate o-acetylesterase, siabb1, sialate 9-o-acetylesterase, sialate-o-acetylesterases, sialic acid-specific 9-o-acetylesterase, sialic acid acetyl esterase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hemagglutinin-esterase
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haemagglutinin esterase
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sialate-4-O-acetylesterase
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sialate-9-O-acetylesterase
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sialate-O-acetylesterase
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sialate-O-acetylesterases
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Sialic acid-specific 9-O-acetylesterase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of carboxylic ester
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
N-acyl-O-acetylneuraminate O-acetylhydrolase
Acts on free and glycosidically bound N-acetyl- or N-glycoloyl-neuraminic acid; acts mainly on the 4-O- and 9-O-acetyl groups. Also acts on some other O-acetyl esters, both cyclic and acyclic compounds, which are not sialic acids.
CAS REGISTRY NUMBER
COMMENTARY hide
89400-31-7
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5-N-acetyl-4,9-di-O-acetylneuraminic acid alpha-methylglycoside + H2O
4,9-di-O-acetylneuraminic acid alpha-methylglycoside + acetate
show the reaction diagram
sialate-9-O-acetylesterase activity
analysis by gas chromatography/mass spectrometry
-
?
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
show the reaction diagram
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
show the reaction diagram
-
-
-
-
?
5-N-acetyl-9-O-acetylneuraminic acid + H2O
5-N-acetylneuraminic acid + acetate
show the reaction diagram
-
-
-
-
?
methyl 6-O-(N-acetyl-9-O-acetyl-alpha-D-neuramin-2-yl)-alpha-D-glucoside + H2O
methyl 6-O-(N-acetyl-alpha-D-neuramin-2-yl)-alpha-D-glucoside + acetate
show the reaction diagram
-
methyl N-acetylneuraminide, 25°C, 60 min, pH 7
NMR-based enzyme assay
-
?
methyl 6-S-(N-acetyl-9-O-acetyl-alpha-D-neuramin-2-yl)-6-thio-alpha-D-glucoside + H2O
methyl 6-S-(N-acetyl-alpha-D-neuramin-2-yl)-alpha-D-glucoside + acetate
show the reaction diagram
-
thio-linked N-acetylneuraminosylglucoside, 25°C, 60 min, pH 7
NMR-based enzyme assay
-
?
N-acetyl-9-O-acetyl-neuraminic acid + H2O
N-acetylneuraminic acid + acetate
show the reaction diagram
-
25°C, 60 min, pH 7, slow activity due to alpha: beta anomeric ratio of about 5: 95
NMR-based enzyme assay
-
?
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
5-N-acetyl-9-O-acetylneuraminic acid + H2O
5-N-acetylneuraminic acid + acetate
show the reaction diagram
-
-
-
-
?
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3,4-dichloroisocoumarin
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ammonium (allyl 5-acetamido-9-O-methyl-3,5-dideoxy-D-glycero-alpha-D-galacto-2-nonulopyranosidonate)
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diammonium (allyl 5-acetamido-3,5-dideoxy-9-O-(P-methylphosphonyl)-D-glycero-alpha-D-galacto-2-nonulopyranosidonate)
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additional information
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synthesis and evaluation of a series of sialosides modified at the 4- and 9-hydroxy group for inhibition of the viral haemagglutinin-esterase activity from various Orthomyxoviruses and Coronaviruses, overview. While no inhibition of the sialate-4-O-acetylesterases from Mouse hepatitis virus strain S or Sialodacryoadenitis virus is found, a 9-O-methyl derivative displays inhibitory activity against recombinant sialate-9-O-acetylesterase from Influenza C virus. No inhibition of Bovine coronavirus by ammonium (allyl 5-acetamido-3,5-dideoxy-4-O-methyl-D-glycero-alpha-D-galacto-2-nonulopyranosidonate) and diammonium (allyl 5-acetamido-3,5-dideoxy-4-O-(P-methylphosphonyl)-D-glycero-alpha-D-galacto-2-nonulopyranosidonate)
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
methyl-linked N-acetyl-neuraminide (N-acetyl-9-O-acetyl-neuraminic acid alpha-methylglycoside) hydrolysed at higher rate than thio-linked N-acetylneuraminosylglucoside (N-acetyl-9-O-acetyl-2,6-alpha-S-glucosyl-neuraminic acid alpha-methylglycoside)
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
assay at room temperature
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
BcoV, strain Mebus
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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besides sialidases, the haemagglutinin-esterases of Influenza C virus, Isavirus, Betacoronaviruses and Toroviruses represent another class of receptor-destroying enzymes, RDEs. They are sialate-O-acetylesterases, SOAE, hydrolysing O-acetyl esters of O-acetylated sialic acid derivatives as sialate-4-O-acetylesterases, 4-SOAE, and sialate-9-O-acetylesterases, 9-SOAE. The enzyme of Bovine coronavirus exhibits sialate-9-O-acetylesterase specificity
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
crystal structure, disulphide-linkage through Cys385, 2fold crystallographic symmetry
heterodimer
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disulfide-bonded
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
apo-enzyme (PDB: 3CL4) or mutant S40A in complex with 5-N-acetyl-4,9-di-O-acetylneuraminic acid alpha-methylglycoside (PDB: 3CL5), hanging drop vapour diffusion, 18°C, 2 weeks, precipitant: 16% polyethylene glycol 8000 and 20% glycerol or 10% polyethylene glycol 3350, hexagonal bipyramide crystals: space groups: P6(5)22, unit cell parameter: a, b: 88.8-89.3, c: 280.4-282.4, soaking with 7 mM 5-N-acetyl-4,9-di-O-acetylneuraminic acid alpha-methylglycoside, molecular replacement using PDB: 1FLC (for apo-enzyme) or wild-type structure (for S40A mutant) as template, three domains: receptor-binding domain (R), acetylase domain (E, strictly conserved), and membrane-proximal domain (MP), homodimer of 2fold crystallographic symmetry with 2 major contact regions (CR1: bridges R domains, CR2: involves MP), disorder of residues 377-388, E-domain: SGNH-hydrolase fold, active site with catalytic triad (Ser40, His329, Asp326) and oxyanion hole (Asn104, Ser40, Gly75), highly variable surface loop (residues 47-54) is site of antigenic variation, R-domain: different from those of hemagglutinin-esterase fusion (HEF) and agglutinin (HA) (plasticity), binding of ligand in opposite orientation involving residues Leu212, Asn214, Ser213, Tyr184, Phe211, Leu266, Leu267 (hydrophobic pocket), coordination of potassium and water by Asp220, Ser221, Gln222, Ser263, Glu265, Leu267
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F211A
abrogated ligand recognition and binding
L266A
abrogated ligand recognition and binding
L267A
abrogated ligand recognition and binding
S40A
catalytically inactive, active site residue, retained lectin activity
Y184A
decreased ligand binding affinity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
from HEK293S cells by protein A-affinity chromatography followed by on-bead thrombin digestion
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
sequence encoding ectodomain (residues 19-388) in plasmid pCD5-BCoVHE-T-Fc for expression with N-terminal CD5 signal peptide and C-terminal thrombin cleavage site followed by human IgG1 Fc domain in N-acetylglucosaminyltransferase-deficient HEK293S cells
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
broad-spectrum antivirals that target orthomyxo- and coronavirus sialate-O-acetylesterases
molecular biology
origin and evolution of viral hemagglutinin-esterases
drug development
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drug design, two essential pharmacophoric groups of ligand: 9-O-acetyl group and C-1 carboxylate group, anti-virus infection
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
De Groot, R.J.
Structure, function and evolution of the hemagglutinin-esterase proteins of corona- and toroviruses
Glycoconj. J.
23
59-72
2006
influenza C virus, bovine coronavirus, Murine coronavirus strain DVIM, Human coronavirus OC43, porcine hemagglutinating encephalomyelitis virus, Puffinosis coronavirus
Manually annotated by BRENDA team
Mayr, J.; Haselhorst, T.; Langereis, M.A.; Dyason, J.C.; Huber, W.; Frey, B.; Vlasak, R.; de Groot, R.J.; von Itzstein, M.
Influenza C virus and bovine coronavirus esterase reveal a similar catalytic mechanism: new insights for drug discovery
Glycoconj. J.
25
393-399
2008
bovine coronavirus, influenza C virus (P07975), influenza C virus, influenza C virus Johannesburg (P07975), bovine coronavirus BcoV
Manually annotated by BRENDA team
Zeng, Q.; Langereis, M.A.; van Vliet, A.L.; Huizinga, E.G.; de Groot, R.J.
Structure of coronavirus hemagglutinin-esterase offers insight into corona and influenza virus evolution
Proc. Natl. Acad. Sci. USA
105
9065-9069
2008
bovine coronavirus (P15776)
Manually annotated by BRENDA team
Stanley, M.; Mayr, J.; Huber, W.; Vlasak, R.; Streicher, H.
Synthesis and inhibitory activity of sialic acid derivatives targeted at viral sialate-O-acetylesterases
Eur. J. Med. Chem.
46
2852-2860
2011
influenza C virus, Murine hepatitis virus, bovine coronavirus, Rat sialodacryoadenitis coronavirus
Manually annotated by BRENDA team