EC Number   |
General Information |
Reference |
|---|
   3.1.1.53 | evolution |
although the backbone of the structure is similar to previously characterized family members, sequence comparisons indicate that this family can be further subdivided into two subfamilies with somewhat different fingerprints. NanS is the founding member of group II. Sequence motifs and two subfamilies of SGNH hydrolases, overview |
716859 |
| 3.1.1.53 | evolution |
in apparent contrast to human and ungulate host range variants of Betacoronavirus-1, murine coronaviruses actually bind to O-Ac-sialic acids via hemagglutinin-esterase exclusively. Apparently, expansion of group A betacoronaviruses into new hosts and niches is accompanied by changes in hemagglutinin-esterase ligand and substrate preference and in the roles of hemagglutinin-esterase and sialidase in Sia receptor usage |
-, 716066 |
| 3.1.1.53 | malfunction |
decreased sialate-O-acetylesterase activity occurs both in lysosomal and cytosolic fractions of childhood acute lymphoblastic leukemia, ALL, cell lines and primary cells from bone marrow of patients compared to peripheral blood mononuclear cells from healthy donors, which preferentially hydrolyse O-acetyl groups at C-9 of Sia |
715136 |
| 3.1.1.53 | malfunction |
defective variants of the enzyme are associated with an increased risk of various autoimmune diseases such as type 1 diabetes. Enzyme mutation A467V is involved in anti-PIT-1 antibody syndrome, phenotypes, overview |
729642 |
| 3.1.1.53 | malfunction |
mice with a mutation in sialate: O-acetyl esterase (inframe deletion of exon 2, resulting in a protein lacking esterase activity) exhibit enhanced B cell receptor activation, defects in peripheral B cell development, and spontaneously develop antichromatin autoantibodies and glomerular immune complex deposits. The 9-O-acetylation state of sialic acid regulates the function of CD22, a Siglec that functions in vivo as an inhibitor of BCR signaling |
699276 |
| 3.1.1.53 | more |
SsNeuAc contains a asignature consensus sequence for serine esterase, Gly-Xaa-Ser-Xaa-Gly, is found within the C-terminal half |
714062 |
| 3.1.1.53 | more |
the NanS catalytic center contains Ser19 and His301 but no Asp/Glu is present to form the classical catalytic triad |
716859 |
| 3.1.1.53 | physiological function |
a SiaBb1 construct that lacks the SGNH hydrolase and Lam G domains cannot catalyze 4-nitrophenyl acetate hydrolysis, but retains sialidase activity |
750104 |
| 3.1.1.53 | physiological function |
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 |
714901 |
| 3.1.1.53 | physiological function |
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 Influenza C virus exhibits sialate-9-O-acetylesterase specificity |
714901 |
