Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Kelm, A.; Shaw, L.; Schauer, R.; Reuter, G.
    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 (1998), Eur. J. Biochem., 251, 874-884.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.1.1.B3 Cu2+ complete inhibition at 2 mM Asterias rubens
2.1.1.B3 EDTA 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+ Asterias rubens
2.1.1.B3 Fe3+ 18% inhibition at 2 mM Asterias rubens
2.1.1.B3 Ni2+ 84% inhibition at 2 mM Asterias rubens
2.1.1.B3 Zn2+ 83% inhibition at 2 mM Asterias rubens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.1.1.B3 0.0071
-
 S-adenosyl-L-methionine pH 8.0, 25°C, with N-acetylneuraminyl alpha2,3-lactose Asterias rubens
2.1.1.B3 0.044
-
 N-acetylneuraminyl alpha2,3-lactose pH 8.0, 25°C Asterias rubens
2.1.1.B3 0.299
-
 N-acetylneuraminic acid pH 8.0, 25°C Asterias rubens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.1.1.B3 membrane
-
 Asterias rubens 16020
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.1.1.B3 Ca2+ activates at 2 mM Asterias rubens
2.1.1.B3 Co2+ activates at 2 mM Asterias rubens
2.1.1.B3 Mg2+ activates at 2 mM Asterias rubens
2.1.1.B3 Mn2+ activates at 2 mM Asterias rubens

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.1.1.B3 58000
-
 x * 58000 + x * 62000, SDS-PAGE Asterias rubens
2.1.1.B3 62000
-
 x * 58000 + x * 62000, SDS-PAGE Asterias rubens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.1.B3 S-adenosyl-L-methionine + N-acetylneuraminic acid Asterias rubens
-
 S-adenosyl-L-homocysteine + N-acetyl-8-O-methyl-neuraminate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.B3 Asterias rubens
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.1.B3 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 Asterias rubens

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.1.1.B3 gonad
-
 Asterias rubens
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.1.1.B3 71.6
-
 purified enzyme Asterias rubens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.B3 additional information 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 Asterias rubens ?
-
 ?
2.1.1.B3 S-adenosyl-L-methionine + CMP-N-acetylneuraminic acid
-
 Asterias rubens S-adenosyl-L-homocysteine + CMP-N-acetyl-8-O-methyl-neuraminate
-
 ?
2.1.1.B3 S-adenosyl-L-methionine + colominic acid
-
 Asterias rubens ?
-
 ?
2.1.1.B3 S-adenosyl-L-methionine + fetuin
-
 Asterias rubens ?
-
 ?
2.1.1.B3 S-adenosyl-L-methionine + N-acetylneuraminic acid
-
 Asterias rubens S-adenosyl-L-homocysteine + N-acetyl-8-O-methyl-neuraminate
-
 ?
2.1.1.B3 S-adenosyl-L-methionine + N-acetylneuraminic acid free N-acetylneuraminic acid and oligosaccharide- or glycoprotein-bound substrate, the latter is preferred Asterias rubens S-adenosyl-L-homocysteine + N-acetyl-8-O-methyl-neuraminate NMR product identification ?
2.1.1.B3 S-adenosyl-L-methionine + N-acetylneuraminyl alpha2,3-lactose free N-acetylneuraminyl alpha2,3-lactose and oligosaccharide- or glycoprotein-bound substrate, the latter is preferred Asterias rubens S-adenosyl-L-homocysteine + N-acetyl-8-O-methyl-neuraminyl alpha2,3-lactose
-
 ?
2.1.1.B3 S-adenosyl-L-methionine + N-acetylneuraminyl alpha2,6-lactose free N-acetylneuraminyl alpha2,6-lactose acid and oligosaccharide- or glycoprotein-bound substrate, the latter is preferred Asterias rubens S-adenosyl-L-homocysteine + N-acetyl-8-O-methyl-neuraminyl alpha2,6-lactose
-
 ?
2.1.1.B3 S-adenosyl-L-methionine + N-glycoloylneuraminic acid free N-glycoloylneuraminic acid and oligosaccharide- or glycoprotein-bound substrate, the latter is preferred Asterias rubens S-adenosyl-L-homocysteine + N-glycoloyl-8-O-methyl-neuraminate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.1.1.B3 ? x * 58000 + x * 62000, SDS-PAGE Asterias rubens

Synonyms

EC Number Synonyms Comment Organism
2.1.1.B3 S-adenosyl-L-methionine: sialate-8-O-methyltransferase
-
 Asterias rubens
2.1.1.B3 sialate-8-O-methyltransferase
-
 Asterias rubens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.1.1.B3 37
-
-
 Asterias rubens

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.1.1.B3 37
-
 the purified enzyme is quite unstable at 37°C Asterias rubens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.1.1.B3 7.4 8.3 broad optimum Asterias rubens