Information on EC 2.1.1.B3 - sialate-8-O-methyltransferase

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The expected taxonomic range for this enzyme is: Asterias rubens

EC NUMBER
COMMENTARY hide
2.1.1.B3
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
sialate-8-O-methyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + N-acetylneuraminic acid = S-adenosyl-L-homocysteine + N-acetyl-8-O-methyl-neuraminate
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:sialate-8-O-methyltransferase
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + CMP-N-acetylneuraminic acid
S-adenosyl-L-homocysteine + CMP-N-acetyl-8-O-methyl-neuraminate
show the reaction diagram
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-
-
-
?
S-adenosyl-L-methionine + colominic acid
?
show the reaction diagram
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-
-
-
?
S-adenosyl-L-methionine + fetuin
?
show the reaction diagram
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-
-
-
?
S-adenosyl-L-methionine + N-acetylneuraminic acid
S-adenosyl-L-homocysteine + N-acetyl-8-O-methyl-neuraminate
show the reaction diagram
S-adenosyl-L-methionine + N-acetylneuraminyl alpha2,3-lactose
S-adenosyl-L-homocysteine + N-acetyl-8-O-methyl-neuraminyl alpha2,3-lactose
show the reaction diagram
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free N-acetylneuraminyl alpha2,3-lactose and oligosaccharide- or glycoprotein-bound substrate, the latter is preferred
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-
?
S-adenosyl-L-methionine + N-acetylneuraminyl alpha2,6-lactose
S-adenosyl-L-homocysteine + N-acetyl-8-O-methyl-neuraminyl alpha2,6-lactose
show the reaction diagram
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free N-acetylneuraminyl alpha2,6-lactose acid and oligosaccharide- or glycoprotein-bound substrate, the latter is preferred
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-
?
S-adenosyl-L-methionine + N-glycoloylneuraminic acid
S-adenosyl-L-homocysteine + N-glycoloyl-8-O-methyl-neuraminate
show the reaction diagram
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free N-glycoloylneuraminic acid and oligosaccharide- or glycoprotein-bound substrate, the latter is preferred
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-
?
additional information
?
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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
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + N-acetylneuraminic acid
S-adenosyl-L-homocysteine + N-acetyl-8-O-methyl-neuraminate
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
activates at 2 mM
Co2+
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activates at 2 mM
Mg2+
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activates at 2 mM
Mn2+
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activates at 2 mM
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Cu2+
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complete inhibition at 2 mM
EDTA
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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+
Fe3+
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18% inhibition at 2 mM
Ni2+
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84% inhibition at 2 mM
Zn2+
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83% inhibition at 2 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.299
N-acetylneuraminic acid
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pH 8.0, 25C
0.044
N-acetylneuraminyl alpha2,3-lactose
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pH 8.0, 25C
0.0071
S-adenosyl-L-methionine
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pH 8.0, 25C, with N-acetylneuraminyl alpha2,3-lactose
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
71.6
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purified enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4 - 8.3
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broad optimum
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 58000 + x * 62000, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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the purified enzyme is quite unstable at 37C
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
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