Information on EC 2.3.1.44 - N-acetylneuraminate 4-O-acetyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.3.1.44
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RECOMMENDED NAME
GeneOntology No.
N-acetylneuraminate 4-O-acetyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + N-acetylneuraminate = CoA + N-acetyl-4-O-acetylneuraminate
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
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SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:N-acetylneuraminate 4-O-acetyltransferase
Both free and glycosidically bound N-acetyl- and N-glycolyl- neuraminates can act as O-acetyl acceptors.
CAS REGISTRY NUMBER
COMMENTARY hide
51004-25-2
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
australian monotreme echidna
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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
acetyl-CoA + ganglioside 9-O-acetyl-GD3
CoA + N-acetylated ganglioside 9-O-acetyl-GD3
show the reaction diagram
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110% of the acitivity with ganglioside GD3
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acetyl-CoA + ganglioside GD1a
CoA + N-acetylated ganglioside GD1a
show the reaction diagram
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90% of the acitivity with ganglioside GD3
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acetyl-CoA + ganglioside GD2
CoA + N-acetylated ganglioside GD2
show the reaction diagram
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48% of the acitivity with ganglioside GD3
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acetyl-CoA + ganglioside GD3
CoA + N-acetylated ganglioside GD3
show the reaction diagram
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acetyl-CoA + ganglioside GQ1b
CoA + N-acetylated ganglioside GQ1b
show the reaction diagram
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125% of the acitivity with ganglioside GD3
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acetyl-CoA + ganglioside GT1b
CoA + N-acetylated ganglioside GT1b
show the reaction diagram
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80% of the acitivity with ganglioside GD3
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acetyl-CoA + N-acetylneuraminate
CoA + N-acetyl-4-O-acetylneuraminate
show the reaction diagram
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
acetyl-CoA + N-acetylneuraminate
CoA + N-acetyl-4-O-acetylneuraminate
show the reaction diagram
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3',5'-ADP
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80% inhibition at 1 mM
3'-dephospho-coenzyme A
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50% inhibition at 0.022 mM
3-dephospho-CoA
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4,4-diisothiocyanatostilbene-2,2-disulfonate
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5'-ADP
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ATP
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20% inhibition at 1 mM
beta-NAD+
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coenzyme A
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50% inhibition at 0.013 mM
desulfo-coenzyme A
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50% inhibition at 0.013 mM
IDP
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30% inhibition at 1 mM
IMP
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16% inhibition at 1 mM
ITP
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58% inhibition at 1 mM
NADPH
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18% inhibition at 1 mM
p-chloromercuribenzoate
pyridoxal 5'-phosphate
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75% inhibition at 1 mM
saponin
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Triton-X
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00061 - 0.0321
acetyl-CoA
0.0012
ganglioside GD3
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0042 - 0.24
CoA
0.0148
coenzyme A
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.7
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in 70 mM potassium phosphate buffer and the presence of 90 mM KCl
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 8.5
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5.2 - 8.5
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5.6
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solubilized enzyme, presence of KCl and K2HPO4
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0 - 55
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0 - 50
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
analysis of solubilisation by detergent CHAPS. Need for an unknown low molecular mass and heat-stable cofactor
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