The enzyme has been isolated from gonads of the starfish Asterias rubens. It methylates N-glycolylneuraminate with equal specificity. Oligosaccharides containing N-acetyl-α-neuraminyl-(2→3)-β-D-galactosyl-(1→3)-N-acetyl-D-galactosyl structures are also methylated.
The expected taxonomic range for this enzyme is: Asterias rubens
The enzyme has been isolated from gonads of the starfish Asterias rubens. It methylates N-glycolylneuraminate with equal specificity. Oligosaccharides containing N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl-(1->3)-N-acetyl-D-galactosyl structures are also methylated.
Substrates: the enzyme preforms specific methylation of endogenous and exogenous glycoconjugate-bound sialic acids, usage of desialized human erythrocyte membranes as substrates, methylation of resialylated erythrocyte membranes, overview Products: -
Substrates: free N-acetylneuraminic acid and oligosaccharide- or glycoprotein-bound substrate, the latter is preferred Products: NMR product identification
complete inhibition at 1 mM, reversible by Mn2+ or, to a lesser extent, by Co2+ to 90% and 68% of maximal activity, respectively, no protection by Mg2+
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme 22000fold from gonads to homogeneity by detergent-dependent solubilization, ion exchange chromatography, and two cycles of affinity chromatography on an S-adenosyl-L-homocysteine resin
Nature and biosynthesis of sialic acids in the starfish Asterias rubens. Identification of sialo-oligomers and detection of S-adenosyl-L-methionine: N-acylneuraminate 8-O-methyltransferase and CMP-N-acetylneuraminate monooxygenase activities
The biosynthesis of 8-O-methylated sialic acids in the starfish Asterias rubens. Isolation and characterisation of S-adenosyl-L-methionine: sialate-8-O-methyltransferase
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