EC Number   |
General Information |
Reference |
|---|
   2.3.1.45 | evolution |
the N-terminal domain of CASD1 differs from the canonical GDSL/SGNH fold by lacking the conserved residues G and N, and is therefore grouped into pfam family PF13839, i.e. GDSL/SGNH-like acylesterase family found in Pmr5 and Cas1p. While the N-terminal luminal domain of CASD1 displays the characteristic fold of an esterase39, it does not appear to function as such, no esterase activity with synthetic acetylesterase substrate 4-nitrophenylacetate nor towards natural O-acetylated sialoglycoconjugates |
736875 |
| 2.3.1.45 | more |
homology modelling and topology of human enzyme CASD1 residues 83-290, using the crystal structure of an isoamyl acetate-hydrolysing esterase from Saccharomyces cerevisiae, PDB ID 3mil as template, and predicting a GDSL/SGNH-like alpha/beta-fold that forms the scaffold for a catalytic triad composed of S94, D270 and H273, with S94 as part of a conserved GDS sequence motif, overview. the catalyytic triad is formed by D270, H273, and S94 |
736875 |
| 2.3.1.45 | physiological function |
CASD1 is a sialate O-acetyltransferase that catalyzes the transfer of acetyl groups from acetyl-coenzyme A to CMP-activated sialic acid and formation of a covalent acetyl-enzyme intermediate and serves as key enzyme in the biosynthesis of 9-O-acetylated sialoglycans |
736875 |
