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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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.
specific for alpha-anomer of N-acetyl-9-O-acetyl-neuraminic acid, N-acetyl-9-O-acetyl-neuraminic acid beta-methylglycoside is no substrate (60 min, 25°C, pH 7)
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)
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
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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
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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