Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
4-O-methyl-N-acetylneuraminate + CTP
CMP-4-O-methyl-N-acetylneuraminate + diphosphate
CDP + N-acetylneuraminate
phosphate + CMP-N-acetylneuraminate
CTP + (2S,4S,5R,6R)-6-((1R,2S)-3-azido-1,2-dihydroxy-propyl)-2,4,5-trihydroxy-6-methyl-tetrahydro-pyran-2-carboxylic acid
diphosphate + CMP-(2S,4S,5R,6R)-6-((1R,2S)-3-azido-1,2-dihydroxy-propyl)-2,4,5-trihydroxy-6-methyl-tetrahydro-pyran-2-carboxylic acid
-
-
-
-
?
CTP + (N-4-O-)diacetylneuraminic acid
diphosphate + CMP-N-4-O-diacetylneuraminate
-
(N-4-O-)diacetylneuraminic acid is 46% effective compared to N-acylneuraminate
-
-
?
CTP + 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid
diphosphate + CMP-2-keto-3-deoxy-D-glycero-D-galacto-nononic acid
CTP + 3-deoxy-D-galacto-2-octulosonic acid
diphosphate + CMP-3-deoxy-D-galacto-2-octulosonic acid
-
-
-
-
?
CTP + 3-deoxy-D-glycero-D-galacto-nononate
diphosphate + CMP-3-deoxy-D-glycero-D-galacto-nononate
CTP + 5-deaminoneuraminate
diphosphate + CMP-5-deaminoneuraminate
-
-
-
?
CTP + 8-O-methyl-N-acetylneuraminate
diphosphate + CMP-(8-O-methyl)-N-acetylneuraminate
-
-
-
-
?
CTP + deaminoneuraminic acid
?
-
-
-
-
?
CTP + N-(N-benzyloxycarbonyl-glycyl)-muramic acid
diphosphate + CMP-N-(N-benzyloxycarbonyl-glycyl)-muramic acid
-
-
-
-
?
CTP + N-acetyl-neuraminate
diphosphate + CMP-N-acetylneuraminate
-
-
-
?
CTP + N-acetyl-neuraminic acid
CMP-Neu5Ac + diphosphate
-
-
-
-
?
CTP + N-acetylmuramic acid
diphosphate + CMP-N-acetylmuramic acid
-
-
-
-
?
CTP + N-acetylneuraminate
diphosphate + CMP-N-acetylneuraminate
CTP + N-acetylneuraminic acid
diphosphate + CMP-N-acetylneuraminic acid
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
CTP + N-acylneuraminate methyl ester
diphosphate + CMP-N-acylneuraminate methyl ester
CTP + N-azidoacetylmuramic acid
diphosphate + CMP-N-azidoacetylmuramic acid
-
-
-
-
?
CTP + N-azidomuramic acid
diphosphate + CMP-N-azidomuramic acid
-
-
-
-
?
CTP + N-glycolneuraminate
diphosphate + CMP-N-glycolneuraminate
CTP + N-glycolylneuraminate
diphosphate + CMP-N-glycolylneuraminate
CTP + N-glycolylneuraminic acid
CMP-N-glycolylneuraminate + diphosphate
CTP + N-hydroxyacetylmuramic acid
diphosphate + CMP-N-hydroxyacetylmuramic acid
-
-
-
-
?
CTP + N-hydroxymuramic acid
diphosphate + CMP-N-hydroxymuramic acid
-
-
-
-
?
CTP + N-methylglycolylneuraminate
diphosphate + CMP-N-methylglycolylneuraminate
-
-
-
-
?
CTP + sialic acid
CMP-sialic acid + diphosphate
CTP + sialic acid
diphosphate + CMP-sialic acid
-
-
-
?
deaminoneuraminic acid + CTP
CMP-KDN + diphosphate
N-glycolylneuraminic acid (Neu5Gc) and deaminoneuraminic acid (KDN) are also substrates
-
-
?
fluoroacetylneuraminate + CTP
diphosphate + CMP-N-fluoroacetylneuraminate
N-acetyl-4-O-acetylneuraminate + CTP
diphosphate + CMP-N-acetyl-4-O-acetylneuraminate
N-acetyl-7(8)-O-acetylneuraminate + CTP
diphosphate + CMP-N-acetyl-7(8)-O-acetylneuraminate
N-acetylneuraminic acid + CTP
CMP-Neu5Ac + diphosphate
N-acetylneuraminic acid + CTP
CMP-NeuAc + diphosphate
N-chloroacetylneuraminate + CTP
diphosphate + CMP-N-chloroacetylneuraminate
N-glycolylneuraminic acid + CTP
CMP-N-glycolylneuraminate + diphosphate
N-glycolylneuraminic acid + CTP
CMP-Neu5Gc + diphosphate
N-glycolylneuraminic acid (Neu5Gc) and deaminoneuraminic acid (KDN) are also substrates
-
-
?
TTP + N-acylneuraminate
diphosphate + TMP-N-acylneuraminate
TTP + N-glycolylneuraminic acid
TMP-N-glycolylneuraminate + diphosphate
UDP + N-acetylneuraminate
phosphate + UMP-N-acetylneuraminate
-
-
-
-
?
UDP + N-acylneuraminate
phosphate + UMP-N-acetylneuraminate
UTP + N-acylneuraminate
diphosphate + UMP-N-acylneuraminate
UTP + N-glycolylneuraminic acid
UMP-N-glycolylneuraminate + diphosphate
-
-
-
-
?
additional information
?
-
4-O-methyl-N-acetylneuraminate + CTP
CMP-4-O-methyl-N-acetylneuraminate + diphosphate
-
-
-
?
4-O-methyl-N-acetylneuraminate + CTP
CMP-4-O-methyl-N-acetylneuraminate + diphosphate
-
no activity
-
-
?
CDP + N-acetylneuraminate
phosphate + CMP-N-acetylneuraminate
-
-
-
-
?
CDP + N-acetylneuraminate
phosphate + CMP-N-acetylneuraminate
-
no activity with CDP
-
-
?
CDP + N-acetylneuraminate
phosphate + CMP-N-acetylneuraminate
-
-
-
-
?
CDP + N-acetylneuraminate
phosphate + CMP-N-acetylneuraminate
-
-
-
-
?
CDP + N-acetylneuraminate
phosphate + CMP-N-acetylneuraminate
-
-
-
-
?
CDP + N-acetylneuraminate
phosphate + CMP-N-acetylneuraminate
-
no activity with CDP
-
-
?
CDP + N-acetylneuraminate
phosphate + CMP-N-acetylneuraminate
-
no activity with CDP
-
-
?
CTP + 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid
diphosphate + CMP-2-keto-3-deoxy-D-glycero-D-galacto-nononic acid
recombinant enzyme shows 15times lower activity towards 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid than towards N-acetylneuraminate
-
-
?
CTP + 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid
diphosphate + CMP-2-keto-3-deoxy-D-glycero-D-galacto-nononic acid
enzyme shows high activity towards 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid and towards N-acetylneuraminate
-
-
?
CTP + 3-deoxy-D-glycero-D-galacto-nononate
diphosphate + CMP-3-deoxy-D-glycero-D-galacto-nononate
-
reaction of EC 2.7.7.92
-
?
CTP + 3-deoxy-D-glycero-D-galacto-nononate
diphosphate + CMP-3-deoxy-D-glycero-D-galacto-nononate
-
reaction of EC 2.7.7.92
-
?
CTP + N-acetylneuraminate
diphosphate + CMP-N-acetylneuraminate
-
-
-
?
CTP + N-acetylneuraminate
diphosphate + CMP-N-acetylneuraminate
-
-
-
-
?
CTP + N-acetylneuraminate
diphosphate + CMP-N-acetylneuraminate
-
-
-
?
CTP + N-acetylneuraminate
diphosphate + CMP-N-acetylneuraminate
-
-
-
-
?
CTP + N-acetylneuraminate
diphosphate + CMP-N-acetylneuraminate
-
-
-
-
?
CTP + N-acetylneuraminate
diphosphate + CMP-N-acetylneuraminate
-
-
-
-
?
CTP + N-acetylneuraminate
diphosphate + CMP-N-acetylneuraminate
-
-
-
-
?
CTP + N-acetylneuraminate
diphosphate + CMP-N-acetylneuraminate
-
-
-
-
?
CTP + N-acetylneuraminic acid
diphosphate + CMP-N-acetylneuraminic acid
-
-
-
?
CTP + N-acetylneuraminic acid
diphosphate + CMP-N-acetylneuraminic acid
the enzyme displays specificity for N-acetylneuraminic acid as a substrate
-
-
?
CTP + N-acetylneuraminic acid
diphosphate + CMP-N-acetylneuraminic acid
-
-
-
?
CTP + N-acetylneuraminic acid
diphosphate + CMP-N-acetylneuraminic acid
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
the product of the reaction CMP-N-acylneuraminate is the substrate for the sialylation of glycoconjugates by sialyltransferases
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
the lec32 mutation reduces CMP-NeuAc synthetase activity to undetectable levels and reduces Neu-Ac on glycoproteins and glycolipids by 95%
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
reaction is theoretically reversible, even though the ratio between the velocities in the anabolic and catabolic direction is 1000:1
-
-
r
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
CMP-NeuAc is essential for the formation of capsule polysialylate for strain K1
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
CMP-NeuAc is essential for the formation of capsule polysialylate for strain K1
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
neuroinvasive and septicaemia-causing pathogens often display a polysialic acid capsule that is involved in invasive behaviour. N-Acetylneuraminate is the basic monomer of polysialic acid. The activated form CMP-N-acylneuraminate is synthesized by N-acylneuraminate cytidylyltransferase
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
neuroinvasive and septicaemia-causing pathogens often display a polysialic acid capsule that is involved in invasive behaviour. N-Acetylneuraminate is the basic monomer of polysialic acid. The activated form CMP-N-acylneuraminate is synthesized by N-acylneuraminate cytidylyltransferase
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
production of CMP-N-acetylneuraminate is required for the synthesis of sialylated glycoconjugates
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
enzyme shows pronounced specificity for N-acylneuraminate
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
-
ir
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
the enzyme is involved in the production of activated sialic acids
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
enzyme is equally active with either of the three substrates: N-acylneuraminate, N-glycolylneuraminate and deaminoneuraminic acid
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
changes in the level of sialylation during development are intimately related to variations in the expression of the enzyme, at least in brain, heart, kidney, stomach, intestine and lung
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
the enzyme is involved in synthesis of capsular polysaccharide, the recombinant enzyme can function in K1 capsular polysaccharide biosynthesis in Escherichia coli
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
the enzyme is essential in capsular polysaccharide biosynthesis, activates N-acetylneuraminate for transfer to the nascent capsular polysaccharide
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
the enzyme is essential in capsular polysaccharide biosynthesis, activates N-acetylneuraminate for transfer to the nascent capsular polysaccharide
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
r
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
-
r
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
-
r
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
reaction is freely reversible and the ratio of the velocities in synthesis and degradation direction is 3:1
-
-
r
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
the enzyme produces CMP-N-acetylneuraminate, the nucleotide sugar donor used by sialyltransferase
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
the enzyme produces CMP-N-acetylneuraminate, the nucleotide sugar donor used by sialyltransferase
-
-
?
CTP + N-acylneuraminate methyl ester
diphosphate + CMP-N-acylneuraminate methyl ester
-
-
-
-
?
CTP + N-acylneuraminate methyl ester
diphosphate + CMP-N-acylneuraminate methyl ester
-
-
-
-
?
CTP + N-glycolneuraminate
diphosphate + CMP-N-glycolneuraminate
relatively inferior substrate
-
-
?
CTP + N-glycolneuraminate
diphosphate + CMP-N-glycolneuraminate
-
N-glycolneuraminate is a relatively weaker substrate than N-acylneuraminate
-
-
?
CTP + N-glycolylneuraminate
diphosphate + CMP-N-glycolylneuraminate
-
-
-
-
?
CTP + N-glycolylneuraminate
diphosphate + CMP-N-glycolylneuraminate
-
-
-
?
CTP + N-glycolylneuraminate
diphosphate + CMP-N-glycolylneuraminate
-
-
-
-
?
CTP + N-glycolylneuraminate
diphosphate + CMP-N-glycolylneuraminate
-
-
-
-
?
CTP + N-glycolylneuraminate
diphosphate + CMP-N-glycolylneuraminate
-
-
-
-
?
CTP + N-glycolylneuraminate
diphosphate + CMP-N-glycolylneuraminate
-
-
-
?
CTP + N-glycolylneuraminate
diphosphate + CMP-N-glycolylneuraminate
-
-
-
?
CTP + N-glycolylneuraminate
diphosphate + CMP-N-glycolylneuraminate
-
-
-
-
?
CTP + N-glycolylneuraminate
diphosphate + CMP-N-glycolylneuraminate
-
-
-
-
?
CTP + N-glycolylneuraminate
diphosphate + CMP-N-glycolylneuraminate
-
-
-
-
?
CTP + N-glycolylneuraminate
diphosphate + CMP-N-glycolylneuraminate
-
-
-
-
?
CTP + N-glycolylneuraminate
diphosphate + CMP-N-glycolylneuraminate
-
-
-
-
?
CTP + N-glycolylneuraminate
diphosphate + CMP-N-glycolylneuraminate
-
-
-
r
CTP + N-glycolylneuraminate
diphosphate + CMP-N-glycolylneuraminate
-
-
-
-
?
CTP + N-glycolylneuraminate
diphosphate + CMP-N-glycolylneuraminate
-
-
-
-
?
CTP + N-glycolylneuraminic acid
CMP-N-glycolylneuraminate + diphosphate
-
-
-
-
?
CTP + N-glycolylneuraminic acid
CMP-N-glycolylneuraminate + diphosphate
-
-
-
-
?
CTP + N-glycolylneuraminic acid
CMP-N-glycolylneuraminate + diphosphate
-
-
-
-
?
CTP + N-glycolylneuraminic acid
CMP-N-glycolylneuraminate + diphosphate
-
-
-
-
?
CTP + N-glycolylneuraminic acid
CMP-N-glycolylneuraminate + diphosphate
-
-
-
-
?
CTP + sialic acid
CMP-sialic acid + diphosphate
-
-
-
?
CTP + sialic acid
CMP-sialic acid + diphosphate
-
-
-
-
?
CTP + sialic acid
CMP-sialic acid + diphosphate
-
-
-
-
?
fluoroacetylneuraminate + CTP
diphosphate + CMP-N-fluoroacetylneuraminate
-
-
-
-
?
fluoroacetylneuraminate + CTP
diphosphate + CMP-N-fluoroacetylneuraminate
-
-
-
-
?
fluoroacetylneuraminate + CTP
diphosphate + CMP-N-fluoroacetylneuraminate
-
-
-
-
?
N-acetyl-4-O-acetylneuraminate + CTP
diphosphate + CMP-N-acetyl-4-O-acetylneuraminate
-
-
-
-
?
N-acetyl-4-O-acetylneuraminate + CTP
diphosphate + CMP-N-acetyl-4-O-acetylneuraminate
-
-
-
-
?
N-acetyl-4-O-acetylneuraminate + CTP
diphosphate + CMP-N-acetyl-4-O-acetylneuraminate
-
-
-
-
?
N-acetyl-7(8)-O-acetylneuraminate + CTP
diphosphate + CMP-N-acetyl-7(8)-O-acetylneuraminate
-
-
-
-
?
N-acetyl-7(8)-O-acetylneuraminate + CTP
diphosphate + CMP-N-acetyl-7(8)-O-acetylneuraminate
-
-
-
-
?
N-acetyl-7(8)-O-acetylneuraminate + CTP
diphosphate + CMP-N-acetyl-7(8)-O-acetylneuraminate
-
-
-
-
?
N-acetylneuraminic acid + CTP
CMP-Neu5Ac + diphosphate
-
DmCSAS is shown to be functional both in vitro and in vivo
-
-
?
N-acetylneuraminic acid + CTP
CMP-Neu5Ac + diphosphate
N-glycolylneuraminic acid (Neu5Gc) and deaminoneuraminic acid (KDN) are also substrates
-
-
?
N-acetylneuraminic acid + CTP
CMP-NeuAc + diphosphate
-
bi-bi catalytic mechanism, enzyme also accepts N-glycolylneuraminic acid (NeuGc) as a substrate
-
-
?
N-acetylneuraminic acid + CTP
CMP-NeuAc + diphosphate
-
bi-bi catalytic mechanism, enzyme also accepts N-glycolylneuraminic acid (NeuGc) as a substrate
-
-
?
N-acetylneuraminic acid + CTP
CMP-NeuAc + diphosphate
-
-
-
-
?
N-chloroacetylneuraminate + CTP
diphosphate + CMP-N-chloroacetylneuraminate
-
-
-
-
?
N-chloroacetylneuraminate + CTP
diphosphate + CMP-N-chloroacetylneuraminate
-
-
-
-
?
N-chloroacetylneuraminate + CTP
diphosphate + CMP-N-chloroacetylneuraminate
-
-
-
-
?
N-glycolylneuraminic acid + CTP
CMP-N-glycolylneuraminate + diphosphate
-
-
-
-
?
N-glycolylneuraminic acid + CTP
CMP-N-glycolylneuraminate + diphosphate
-
-
-
-
?
TTP + N-acylneuraminate
diphosphate + TMP-N-acylneuraminate
-
no activity with TTP
-
-
?
TTP + N-acylneuraminate
diphosphate + TMP-N-acylneuraminate
-
-
-
-
?
TTP + N-acylneuraminate
diphosphate + TMP-N-acylneuraminate
-
-
-
-
?
TTP + N-acylneuraminate
diphosphate + TMP-N-acylneuraminate
-
no activity with TTP
-
-
?
TTP + N-acylneuraminate
diphosphate + TMP-N-acylneuraminate
-
no activity with TTP
-
-
?
TTP + N-glycolylneuraminic acid
TMP-N-glycolylneuraminate + diphosphate
-
-
-
-
?
TTP + N-glycolylneuraminic acid
TMP-N-glycolylneuraminate + diphosphate
-
-
-
-
?
UDP + N-acylneuraminate
phosphate + UMP-N-acetylneuraminate
-
-
-
-
?
UDP + N-acylneuraminate
phosphate + UMP-N-acetylneuraminate
-
-
-
-
?
UTP + N-acylneuraminate
diphosphate + UMP-N-acylneuraminate
-
-
-
-
?
UTP + N-acylneuraminate
diphosphate + UMP-N-acylneuraminate
-
no activity with UTP
-
-
?
UTP + N-acylneuraminate
diphosphate + UMP-N-acylneuraminate
-
-
-
-
?
UTP + N-acylneuraminate
diphosphate + UMP-N-acylneuraminate
-
-
-
-
?
UTP + N-acylneuraminate
diphosphate + UMP-N-acylneuraminate
-
no activity with UTP
-
-
?
UTP + N-acylneuraminate
diphosphate + UMP-N-acylneuraminate
-
no activity with UTP
-
-
?
additional information
?
-
enzyme is strictly dependent on CTP
-
-
?
additional information
?
-
enzyme is strictly dependent on CTP
-
-
?
additional information
?
-
-
enzyme is strictly dependent on CTP
-
-
?
additional information
?
-
ATP, GTP and UTP, along with CDP and CMP cannot be used as substrates. The enzyme has a nearly undetectable activity toward 2-keto-3-deoxynononic acid and 2-keto-3-deoxyoctonic acid while no activity is detected with 3-deoxy-D-manno-2-octulosonic acid
-
-
-
additional information
?
-
-
ATP, GTP and UTP, along with CDP and CMP cannot be used as substrates. The enzyme has a nearly undetectable activity toward 2-keto-3-deoxynononic acid and 2-keto-3-deoxyoctonic acid while no activity is detected with 3-deoxy-D-manno-2-octulosonic acid
-
-
-
additional information
?
-
-
does not utilize N-glycolylneuraminic acid as a substrate
-
-
?
additional information
?
-
-
does not utilize N-glycolylneuraminic acid as a substrate
-
-
?
additional information
?
-
the enzyme interacts with fragile X related protein 1
-
-
-
additional information
?
-
-
the enzyme is used for preparative synthesis of CMP-sialic acid derivatives in a one-pot two-enzyme system with EC 4.1.3.3 and EC 2.7.7.43
-
-
?
additional information
?
-
-
does not accept N-glycolylneuraminic acid and triacetylneuraminic acid as substrates
-
-
?
additional information
?
-
no substrate: 2-keto-3-deoxy-D-glycero-D-galacto-nonulosonic acid, kcat/Km value is about 5000fold lower than that of N-acetylneuraminate
-
-
?
additional information
?
-
-
no substrate: 2-keto-3-deoxy-D-glycero-D-galacto-nonulosonic acid, kcat/Km value is about 5000fold lower than that of N-acetylneuraminate
-
-
?
additional information
?
-
-
no activity with N-acetyl-9-O-acetylneuraminate
-
-
?
additional information
?
-
-
no substrates: 6'-thioneuraminate, 6-ketodeoxyoctulosonate
-
-
?
additional information
?
-
-
no substrates: 6'-thioneuraminate, 6-ketodeoxyoctulosonate
-
-
?
additional information
?
-
SaV CSS is a bifunctional enzyme having both CMP-sialic acid synthetase and acetylhydrolase (acylesterase) activities
-
-
?
additional information
?
-
-
SaV CSS is a bifunctional enzyme having both CMP-sialic acid synthetase and acetylhydrolase (acylesterase) activities
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CTP + N-acetylneuraminate
diphosphate + CMP-N-acetylneuraminate
-
-
-
?
CTP + N-acetylneuraminic acid
diphosphate + CMP-N-acetylneuraminic acid
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
CTP + N-glycolneuraminate
diphosphate + CMP-N-glycolneuraminate
-
N-glycolneuraminate is a relatively weaker substrate than N-acylneuraminate
-
-
?
CTP + sialic acid
CMP-sialic acid + diphosphate
CTP + sialic acid
diphosphate + CMP-sialic acid
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
the product of the reaction CMP-N-acylneuraminate is the substrate for the sialylation of glycoconjugates by sialyltransferases
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
the lec32 mutation reduces CMP-NeuAc synthetase activity to undetectable levels and reduces Neu-Ac on glycoproteins and glycolipids by 95%
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
CMP-NeuAc is essential for the formation of capsule polysialylate for strain K1
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
CMP-NeuAc is essential for the formation of capsule polysialylate for strain K1
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
neuroinvasive and septicaemia-causing pathogens often display a polysialic acid capsule that is involved in invasive behaviour. N-Acetylneuraminate is the basic monomer of polysialic acid. The activated form CMP-N-acylneuraminate is synthesized by N-acylneuraminate cytidylyltransferase
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
neuroinvasive and septicaemia-causing pathogens often display a polysialic acid capsule that is involved in invasive behaviour. N-Acetylneuraminate is the basic monomer of polysialic acid. The activated form CMP-N-acylneuraminate is synthesized by N-acylneuraminate cytidylyltransferase
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
production of CMP-N-acetylneuraminate is required for the synthesis of sialylated glycoconjugates
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
the enzyme is involved in the production of activated sialic acids
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
changes in the level of sialylation during development are intimately related to variations in the expression of the enzyme, at least in brain, heart, kidney, stomach, intestine and lung
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
the enzyme is involved in synthesis of capsular polysaccharide, the recombinant enzyme can function in K1 capsular polysaccharide biosynthesis in Escherichia coli
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
the enzyme is essential in capsular polysaccharide biosynthesis, activates N-acetylneuraminate for transfer to the nascent capsular polysaccharide
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
the enzyme is essential in capsular polysaccharide biosynthesis, activates N-acetylneuraminate for transfer to the nascent capsular polysaccharide
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
the enzyme produces CMP-N-acetylneuraminate, the nucleotide sugar donor used by sialyltransferase
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
the enzyme produces CMP-N-acetylneuraminate, the nucleotide sugar donor used by sialyltransferase
-
-
?
CTP + sialic acid
CMP-sialic acid + diphosphate
-
-
-
?
CTP + sialic acid
CMP-sialic acid + diphosphate
-
-
-
-
?
CTP + sialic acid
CMP-sialic acid + diphosphate
-
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.56 - 3
2-keto-3-deoxy-D-glycero-D-galacto-nononic acid
0.56 - 3
3-deoxy-D-glycero-D-galacto-nononate
2.5
4-O-methyl-N-acetylneuraminate
-
pH 7, 37°C
1.5 - 5.3
8-O-methyl-N-acetylneuraminate
2.1
CDP
-
pH 9.0, 37°C, reaction with N-acetylneuraminate
0.62
deaminoneuraminic acid
-
1.2 - 1.4
N-acetyl-4-O-acetylneuraminate
1.1 - 1.6
N-acetyl-7(8)-O-acetylneuraminate
0.00036 - 7.6
N-acetylneuraminate
1.3
N-acetylneuraminate methyl ester
-
pH 9.0, 37°C, reaction with CTP
0.26 - 2.8
N-acetylneuraminic acid
0.127 - 4
N-acylneuraminate
1.483 - 3.5
N-glycolneuraminate
-
1.2 - 6.2
N-glycolylneuraminate
0.16 - 0.35
N-glycolylneuraminic acid
2 - 7
N-methylglycolylneuraminate
8.1
TTP
-
pH 9.0, 37°C, reaction with N-acetylneuraminate
3
UDP
-
pH 9.0, 37°C, reaction with N-acetylneuraminate
2.7
UTP
-
pH 9.0, 37°C, reaction with N-acetylneuraminate
0.56
2-keto-3-deoxy-D-glycero-D-galacto-nononic acid
pH 9.0, 37°C
3
2-keto-3-deoxy-D-glycero-D-galacto-nononic acid
pH 9.0, 37°C
0.56
3-deoxy-D-glycero-D-galacto-nononate
pH 9.0, 25°C
3
3-deoxy-D-glycero-D-galacto-nononate
pH 9.0, 25°C
1.5
8-O-methyl-N-acetylneuraminate
-
mutant S81R, pH 8.5, 37°C
5.3
8-O-methyl-N-acetylneuraminate
-
wild-type, pH 8.5, 37°C
0.00046
CTP
-
pH 9.0, 37°C
0.0106
CTP
-
pH 7.1, 25°C
0.017
CTP
wild-type, pH 7.5, 22°C
0.026
CTP
mutant D211A, pH 7.5, 22°C
0.031
CTP
mutant Q104A, pH 7.5, 22°C
0.034
CTP
CMP-sialic acid synthetase
0.035
CTP
-
at pH 7.1 and 37°C
0.04
CTP
mutant Y179A, pH 7.5, 22°C
0.042
CTP
N-terminal domain of CMP-sialic acid synthetase
0.043
CTP
N-terminal domain and C-terminal domain of CMP-sialic acid synthetase
0.048
CTP
mutant R173A, pH 7.5, 22°C
0.052
CTP
mutant F193A, pH 7.5, 22°C
0.08
CTP
-
at pH 7.5 and 25°C
0.15
CTP
mutant F192A, pH 7.5, 22°C
0.16
CTP
-
wild-type, pH 8.5, 37°C
0.22
CTP
-
mutant S81R, pH 8.5, 37°C
0.24
CTP
-
wild-type, pH 8.5, 37°C
0.24
CTP
-
at 50°C, 10 mM MnCl2, 50 mM Tris buffer (pH 9.5)
0.27
CTP
mutant N175A, pH 7.5, 22°C
0.36
CTP
-
pH 9.0, 37°C, reaction with N-glycolylneuraminate
0.45
CTP
at pH 8.0 and 37°C
0.59
CTP
-
wild-type, pH 8.5, 37°C
1.77
CTP
-
pH 9.0, 37°C, reaction with N-acetylneuraminate
2.6
CTP
-
pH 9.0, 37°C, reaction with N-acetylneuraminate methyl ester
1.2
N-acetyl-4-O-acetylneuraminate
-
37°C, crude enzyme extract
1.3
N-acetyl-4-O-acetylneuraminate
-
37°C, crude enzyme extract
1.4
N-acetyl-4-O-acetylneuraminate
-
37°C, crude enzyme extract
1.1
N-acetyl-7(8)-O-acetylneuraminate
-
37°C, crude enzyme extract
1.1
N-acetyl-7(8)-O-acetylneuraminate
-
37°C, crude enzyme extract
1.6
N-acetyl-7(8)-O-acetylneuraminate
-
37°C, crude enzyme extract
0.00036
N-acetylneuraminate
-
pH 9.0, 37°C
0.066
N-acetylneuraminate
mutant D211A, pH 7.5, 22°C
0.068
N-acetylneuraminate
wild-type, pH 7.5, 22°C
0.076
N-acetylneuraminate
-
pH 7.1, 25°C
0.1
N-acetylneuraminate
-
mutant S81R, pH 8.5, 37°C
0.11
N-acetylneuraminate
mutant Y179A, pH 7.5, 22°C
0.14
N-acetylneuraminate
-
wild-type, pH 8.5, 37°C
0.18
N-acetylneuraminate
-
wild-type, pH 8.5, 37°C
0.22
N-acetylneuraminate
-
wild-type, pH 8.5, 37°C
0.26
N-acetylneuraminate
-
pH 7.1, 37°C
0.26
N-acetylneuraminate
pH 9.0, 37°C
0.29
N-acetylneuraminate
mutant R173A, pH 7.5, 22°C
0.34
N-acetylneuraminate
pH 8.5, 37°C
0.34
N-acetylneuraminate
-
pH 9.0, 37°C
0.38
N-acetylneuraminate
mutant F192A, pH 7.5, 22°C
0.7
N-acetylneuraminate
-
pH 9, 37°C
0.78
N-acetylneuraminate
mutant F193A, pH 7.5, 22°C
0.867
N-acetylneuraminate
-
pH 9.0, 30°C
1
N-acetylneuraminate
-
pH 9, 37°C
1.2
N-acetylneuraminate
-
-
1.2
N-acetylneuraminate
-
37°C, crude enzyme extract
1.3
N-acetylneuraminate
-
pH 8.0, 37°C
1.4
N-acetylneuraminate
-
-
1.4
N-acetylneuraminate
-
37°C, crude enzyme extract
1.6
N-acetylneuraminate
-
pH 9.0, 37°C
1.6
N-acetylneuraminate
-
pH 9.0, 37°C, reaction with TTP
1.6
N-acetylneuraminate
mutant N175A, pH 7.5, 22°C
1.8
N-acetylneuraminate
-
pH 9.0, 37°C, reaction with CDP
1.82
N-acetylneuraminate
-
pH 9.0, 37°C, reaction with CTP
1.9
N-acetylneuraminate
-
pH 9.0, 37°C, reaction with UTP
1.9
N-acetylneuraminate
-
pH 9.0, 37°C, reaction with UDP
2.1
N-acetylneuraminate
-
pH 9.3, 30°C
2.2
N-acetylneuraminate
-
-
2.6
N-acetylneuraminate
mutant Q104A, pH 7.5, 22°C
2.8
N-acetylneuraminate
pH 9.0, 37°C
4
N-acetylneuraminate
-
pH 9.0, 37°C
7.6
N-acetylneuraminate
-
-
0.26
N-acetylneuraminic acid
pH 9.0, 25°C
0.41
N-acetylneuraminic acid
at pH 8.0 and 37°C
2.8
N-acetylneuraminic acid
pH 9.0, 25°C
0.127
N-acylneuraminate
-
at pH 7.5 and 25°C
0.13
N-acylneuraminate
-
-
0.13
N-acylneuraminate
-
at 50°C, 10 mM MnCl2, 50 mM Tris buffer (pH 9.5)
0.26
N-acylneuraminate
-
at pH 7.1 and 37°C
0.34
N-acylneuraminate
-
-
0.8
N-acylneuraminate
-
pH 9.0, 37°C
1.82
N-acylneuraminate
-
-
4
N-acylneuraminate
-
at 37°C
1.483
N-glycolneuraminate
-
at pH 7.5 and 25°C
-
3.5
N-glycolneuraminate
at pH 8.0 and 37°C
-
1.2
N-glycolylneuraminate
-
37°C, crude enzyme extract
1.3
N-glycolylneuraminate
-
37°C, crude enzyme extract
1.5
N-glycolylneuraminate
-
37°C, crude enzyme extract
2.3
N-glycolylneuraminate
-
pH 9.0, 37°C
2.3
N-glycolylneuraminate
-
pH 9.0, 37°C
2.6
N-glycolylneuraminate
pH 8.5, 37°C
2.9
N-glycolylneuraminate
-
pH 9.3, 30°C
3
N-glycolylneuraminate
-
pH 9.0, 37°C, reaction with CTP
4
N-glycolylneuraminate
-
mutant S81R, pH 8.5, 37°C
6.2
N-glycolylneuraminate
-
wild-type, pH 8.5, 37°C
0.16
N-glycolylneuraminic acid
-
at 50°C, 10 mM MnCl2, 50 mM Tris buffer (pH 9.5)
0.35
N-glycolylneuraminic acid
-
2
N-methylglycolylneuraminate
-
wild-type, pH 8.5, 37°C
7
N-methylglycolylneuraminate
-
mutant S81R, pH 8.5, 37°C
0.045
sialic acid
CMP-sialic acid synthetase, substrate N-acetylneuraminic acid
0.063
sialic acid
N-terminal domain and C-terminal domain of CMP-sialic acid synthetase, substrate N-acetylneuraminic acid
0.07
sialic acid
N-terminal domain of CMP-sialic acid synthetase, substrate N-acetylneuraminic acid
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DELTA1-227
-
mutant enzyme shows no CMP-N-acetylneuraminic acid synthetase activity, mutant enzyme is able to hydrolyze platelet activating factor
DELTA1-229
-
mutant enzyme shows no CMP-N-acetylneuraminic acid synthetase activity, mutant enzyme is not able to hydrolyze platelet activating factor
DELTA230-418
-
mutant enzyme shows 43% of the wild-type activity with CTP and N-acylneuraminate as substrates, decrease in stability compared to wild-type enzyme
DELTA247-418
-
mutant enzyme shows 15% of the wild-type activity with CTP and N-acylneuraminate as substrates, decrease in stability compared to wild-type enzyme
DELTA340-418
-
mutant enzyme shows 65% of the wild-type activity with CTP and N-acylneuraminate as substrates, as stable as wild-type enzyme
DELTA384-418
-
mutant enzyme shows 31% of the wild-type activity with CTP and N-acylneuraminate as substrates, as stable as wild-type enzyme
DELTA396-418
-
mutant enzyme shows 38% of the wild-type activity with CTP and N-acylneuraminate as substrates, as stable as wild-type enzyme
DELTA1-227
-
mutant enzyme shows no CMP-N-acetylneuraminic acid synthetase activity, mutant enzyme is able to hydrolyze platelet activating factor
-
DELTA340-418
-
mutant enzyme shows 65% of the wild-type activity with CTP and N-acylneuraminate as substrates, as stable as wild-type enzyme
-
DELTA384-418
-
mutant enzyme shows 31% of the wild-type activity with CTP and N-acylneuraminate as substrates, as stable as wild-type enzyme
-
DELTA396-418
-
mutant enzyme shows 38% of the wild-type activity with CTP and N-acylneuraminate as substrates, as stable as wild-type enzyme
-
DELTA408-424
deletion mutant devoid of the second putative nuclear export signal, by immunofluorescent microscopy it is shown that this deletion mutant has an increased nuclear localisation combined with a decreased cytoplasmic localisation
DELTA61-69
deletion mutant devoid of the first putative nuclear export signal, by immunofluorescent microscopy it is shown that is deletion mutant has an increased nuclear localisation combined with a decreased cytoplasmic localisation
K198A
-
mutant enzyme is active at moderately reduced level
R199A
-
inactive mutant protein
R199A/R202A
-
inactive mutant protein
R201A
-
mutant enzyme is active at moderately reduced level
R202A
-
mutant enzyme shows drastically reduced activity
E162A
the mutant enzyme shows 14.5% activity compared to the wild type enzyme
E162Q
the mutant enzyme shows 15.3% activity compared to the wild type enzyme
F192A
8fold increase on Km value for CTP
F193A
3fold increase on Km value for CTP
N175A
16fold increases in the Km value for CTP and 23fold for N-acetylneuraminate
Q104A
40fold inccrease in Km value for N-acetylneuraminate
Q104E
dramatic loss of activity. Residue involved in metal binding
Q104L
dramatic loss of activity. Residue involved in metal binding
Q104N
dramatic loss of activity. Residue involved in metal binding
Q163A
-
mutant displays improved substrate promiscuity
R165A
the mutant enzyme shows 0.163% activity compared to the wild type enzyme
R173A
38fold increase in Km value for N-acetylneuraminate
S31R
-
mutant displays improved substrate promiscuity, catalytic activities for substrates N-glycolylneuraminate, N-methylglycolylneuraminate and 8-O-methyl N-acetyl-neuraminate are improved compared to wild-type
Y179A
200fold decrease in kcat value
N35Q
site-directed mutagenesis of the glycosylation site, the mutant shows enzyme activity
N35Q
the mutant shows about 2.3fold increased activity compared to the wild type enzyme
N66Q
site-directed mutagenesis of the glycosylation site, the mutant shows enzyme activity
N66Q
the mutant shows about 1.2fold increased activity compared to the wild type enzyme
D209A
almost complete loss of activity. Residue involved in metal binding
D209A
the mutation is detrimental to enzyme function
D211A
dramatic loss of activity. Residue involved in metal binding
D211A
the mutation is detrimental to enzyme function
K142A
10000fold reduction in kcat with an insignificant, fourfold, rise in Km for CTP
K142A
dramatic loss of activity. Residue involved in metal binding
additional information
-
construction of a DELTAN-AaCSS mutant which gives a single band at 517 kDa, but not a smear in the high-molecular mass region. Furthermore, DELTANAaCSS shows in vitro activity to Neu5Ac. Cleavage of the N-terminal hydrophobic region of the CSSs is critical for the enzyme activity
additional information
construction of a DELTAN-AaCSS mutant which gives a single band at 517 kDa, but not a smear in the high-molecular mass region. Furthermore, DELTANAaCSS shows in vitro activity to Neu5Ac. Cleavage of the N-terminal hydrophobic region of the CSSs is critical for the enzyme activity
additional information
presence of four basic clusters BC1-BC4 in the protein sequence. Deletion of BC3 does not impair nuclear import of isoform Cmas1, deletion of BC1 or BC2, individually or in combination, entail retention in the cytoplasm. neither the deletion of BC1 nor BC2 alters enzymatic activity
additional information
presence of four basic clusters BC1-BC4 in the protein sequence. Deletion of BC3 does not impair nuclear import of isoform Cmas1, deletion of BC1 or BC2, individually or in combination, entail retention in the cytoplasm. neither the deletion of BC1 nor BC2 alters enzymatic activity
additional information
-
presence of four basic clusters BC1-BC4 in the protein sequence. Deletion of BC3 does not impair nuclear import of isoform Cmas1, deletion of BC1 or BC2, individually or in combination, entail retention in the cytoplasm. neither the deletion of BC1 nor BC2 alters enzymatic activity
additional information
-
in contrast to its mammalian counterparts DmCSAS protein begins with an N-terminal sequence rich in hydrophobic amino acids characteristic of a signal/anchoring sequence
additional information
-
multiple alignment among the Drosophila melanogaster, human, mouse, Escherichia coli and Neisseria meningitidis CSAS enzymes shows that all proteins are homologous over the length of the catalytic domain
additional information
-
replacement of the N-terminal leader sequence of DmCSAS with the human CSAS N-terminal sequence results in the redirection of the chimeric CSAS protein to the nucleus but with concomitant loss of activity
additional information
-
a series of deletions from the 3'-end of the CMP-NeuAc synthetase coding region is constructed and expressed in Escherichia coli. As a result, the catalytic domain required for CMP-NeuAc synthetase is found to be in the N-terminal half consisting of amino acids 1229. The C-terminal half consisting of amino acids 228418 exhibits platelet-activating factor acetylhydrolase activity
additional information
-
a series of deletions from the 3'-end of the CMP-NeuAc synthetase coding region is constructed and expressed in Escherichia coli. As a result, the catalytic domain required for CMP-NeuAc synthetase is found to be in the N-terminal half consisting of amino acids 1229. The C-terminal half consisting of amino acids 228418 exhibits platelet-activating factor acetylhydrolase activity
-
additional information
by deletion mutant analysis it is demonstrated that mouse CSS contains two nuclear export signals which regulate the transport of the protein from nucleus towards cytosol
additional information
-
by deletion mutant analysis it is demonstrated that mouse CSS contains two nuclear export signals which regulate the transport of the protein from nucleus towards cytosol
additional information
the two nuclear export signals of mouse CSS are conserved among mammals and fish CSSs but they are not present in bacteria or insect CSS
additional information
-
the two nuclear export signals of mouse CSS are conserved among mammals and fish CSSs but they are not present in bacteria or insect CSS
additional information
generation of mouse embryonic stem cell (mESC) lines that lack CMP-Sia synthetase (CMAS) and thereby the ability to activate Sia to CMP-Sia, phenotype, overview. The Cmas targeting strategy uses a targeting vector with diphtheria toxin cassette (DT) to increase homologous recombination. Cmas-/- mESC accumulate intracellular Neu5Ac. alpha2,3- and alpha2,6-Sialylated N-glycans are absent in Cmas-/- mESCs
additional information
-
generation of mouse embryonic stem cell (mESC) lines that lack CMP-Sia synthetase (CMAS) and thereby the ability to activate Sia to CMP-Sia, phenotype, overview. The Cmas targeting strategy uses a targeting vector with diphtheria toxin cassette (DT) to increase homologous recombination. Cmas-/- mESC accumulate intracellular Neu5Ac. alpha2,3- and alpha2,6-Sialylated N-glycans are absent in Cmas-/- mESCs
additional information
amino acid sequence alignment of SaV CSS indicate that the C-terminus belongs to the newly discovered SGNH-hydrolase subfamily of serine esterases/lipases
additional information
-
amino acid sequence alignment of SaV CSS indicate that the C-terminus belongs to the newly discovered SGNH-hydrolase subfamily of serine esterases/lipases
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Kean, E.L.; Roseman, S.
The sialic acids. X. Purification and properties of cytidine 5-monophosphosialic acid synthetase
J. Biol. Chem.
241
5643-5650
1966
Bos taurus, Ovis aries, Homo sapiens, Sus scrofa
brenda
Kolisis, F.N.
Studies on acylneuraminate cytidylytransferase from human placenta
Arch. Int. Physiol. Biochim.
92
179-184
1984
Homo sapiens
brenda
Haft, R.F.; Wessels, M.R.
Characterization of CMP-N-acetylneuraminic acid synthetase of group B streptococci
J. Bacteriol.
176
7372-7374
1994
Streptococcus sp., Streptococcus sp. Ib
brenda
Schmelter, T.; Ivanov, S.; Wember, M.; Stangier, P.; Thiem, J.; Schauer, R.
Partial purification and characterization of cytidine-5-monophosphosialate synthase from rainbow trout liver
Biol. Chem. Hoppe-Seyler
374
337-342
1993
Oncorhynchus mykiss
brenda
Edwards, U.; Frosch, M.
Sequence and functional analysis of the cloned Neisseria meningitidis CMP neunac synthetase
FEMS Microbiol. Lett.
96
161-166
1992
Neisseria meningitidis
-
brenda
Vann, W.F.; Silver, R.P.; Abeijon, C.; Chang, K.; Aaronson, W.; Sutton, A.; Finn, C.W.; Lindner, W.; Kotsatos, M.
Purification, properties, and genetic location of Escherichia coli cytidine 5-monophosphate N-acetylneuraminic acid synthetase
J. Biol. Chem.
262
17556-17562
1987
Escherichia coli, Escherichia coli O18:K1
brenda
Rodriguez-Aparicio, L.B.; Luengo, J.M.; Gonzalez-Clemente, C.; Reglero, A.
Purification and characterization of the nuclear cytidine 5-monophosphate N-acetylneuraminic acid synthetase from rat liver
J. Biol. Chem.
267
9257-9263
1992
Rattus norvegicus
brenda
Schauer, R.; Wember, M.
Studies on the substrate specificity of acylneuraminate cytidylyltransferase and sialytransferase of submandibular glands from cow, pig and horse
Hoppe-Seyler's Z. Physiol. Chem.
354
1405-1414
1973
Bos taurus, Equus caballus, Sus scrofa
brenda
Schauer, R.; Haverkamp, J.; Ehrlich, K.
Isolation and characterization of acylneuraminate cytidylyltransferase from frog liver
Hoppe-Seyler's Z. Physiol. Chem.
361
641-648
1980
Pelophylax lessonae
brenda
Haverkamp, J.; Beau, J.M.; Schauer, R.
Improved synthesis of CMP-sialates using enzymes from frog liver and equine submandibular gland
Hoppe-Seyler's Z. Physiol. Chem.
360
159-166
1979
Equus caballus, Pelophylax lessonae
brenda
Corfield, A.P.; Schauer, R.; Wember, M.
The preparation of CMP-sialic acids by using CMP-acylneuraminate synthase from frog liver immobilized on sepharose 4B
Biochem. J.
177
1-7
1979
Pelophylax lessonae
brenda
Karwaski, M.F.; Wakarchuk, W.W.; Gilbert, M.
High-level expression of recombinant Neisseria CMP-sialic acid synthetase in Escherichia coli
Protein Expr. Purif.
25
237-240
2002
Neisseria meningitidis (P0A0Z8), Neisseria meningitidis, Neisseria meningitidis 406Y (P0A0Z8)
brenda
Vionnet, J.; Concepcion, N.; Warner, T.; Zapata, G.; Hanover, J.; Vann, W.F.
Purification of CMP-N-acetylneuraminic acid synthetase from bovine anterior pituitary glands
Glycobiology
9
481-487
1999
Bos taurus
brenda
Nakata, D.; Munster, A.K.; Gerardy-Schahn, R.; Aoki, N.; Matsuda, T.; Kitajima, K.
Molecular cloning of a unique CMP-sialic acid synthetase that effectively utilizes both deaminoneuraminic acid (KDN) and N-acetylneuraminic acid (Neu5Ac) as substrates
Glycobiology
11
685-692
2001
Oncorhynchus mykiss (Q90WG6), Oncorhynchus mykiss, Mus musculus (Q99KK2), Mus musculus
brenda
Revilla-Nuin, B.; Reglero, A.; Feo, J.C.; Rodriguez-Aparicio, L.B.; Ferrero, M.A.
Identification, expression and tissue distribution of cytidine 5'-monophosphate N-acetylneuraminic acid synthetase activity in the rat
Glycoconj. J.
15
233-241
1998
Rattus norvegicus
brenda
Kittelmann, M.; Klein, T.; Kragl, U.; Wandrey, C.; Ghisalba, O.
CMP-N-acetyl neuraminic-acid synthetase from Escherichia coli: fermentative production and application for the preparative synthesis of CMP-neuraminic acid
Appl. Microbiol. Biotechnol.
44
59-67
1995
Escherichia coli, Escherichia coli K-235
brenda
Haft, R.F.; Wessels, M.R.; Mebane, M.F.; Conaty, N.; Rubens, C.E.
Characterization of cpsF and its product CMP-N-acetylneuraminic acid synthetase, a group B streptococcal enzyme that can function in K1 capsular polysaccharide biosynthesis in Escherichia coli
Mol. Microbiol.
19
555-563
1996
Streptococcus sp.
brenda
Bravo, I.G.; Barrallo, S.; Ferrero, M.A.; Rodriguez-Aparicio, L.B.; Martinez-Blanco, H.; Reglero, A.
Kinetic properties of the acylneuraminate cytidylyltransferase from Pasteurella haemolytica A2
Biochem. J.
358
585-598
2001
Mannheimia haemolytica, Mannheimia haemolytica A2
brenda
Munster, A.K.; Eckhardt, M.; Potvin, B.; Muhlenhoff, M.; Stanley, P.; Gerardy-Schahn, R.
Mammalian cytidine 5'-monophosphate N-acetylneuraminic acid synthetase: a nuclear protein with evolutionarily conserved structural motifs
Proc. Natl. Acad. Sci. USA
95
9140-9145
1998
Mus musculus (Q99KK2), Mus musculus
brenda
Tullius, M.V.; Munson, R.S., Jr.; Wang, J.; Gibson, B.W.
Purification, cloning, and expression of a cytidine 5'-monophosphate N-acetylneuraminic acid synthetase from Haemophilus ducreyi
J. Biol. Chem.
271
15373-15380
1996
[Haemophilus] ducreyi, [Haemophilus] ducreyi 35000
brenda
Potvin, B.; Raju, T.S.; Stanley, P.
Lec32 is a new mutation in Chinese hamster ovary cells that essentially abrogates CMP-N-acetylneuraminic acid synthetase activity
J. Biol. Chem.
270
30415-30421
1995
Cricetulus griseus
brenda
Gilbert, M.; Watson, D.C.; Wakarchuk, W.W.
Purification and characterization of the recombinant CMP-sialic acid synthetase from Neisseria meningitidis
Biotechnol. Lett.
19
417-420
1997
Neisseria meningitidis (P0A0Z8), Neisseria meningitidis 406Y (P0A0Z8)
-
brenda
Samuels, N.M.; Gibson, B.W.; Miller, S.M.
Investigation of the kinetic mechanism of cytidine 5'-monophosphate N-acetylneuraminic acid synthetase from Haemophilus ducreyi with new insights on rate-limiting steps from product inhibition analysis
Biochemistry
38
6195-6203
1999
[Haemophilus] ducreyi
brenda
Mosimann, S.C.; Gilbert, M.; Dombroswki, D.; To, R.; Wakarchuk, W.; Strynadka, N.C.
Structure of a sialic acid-activating synthetase, CMP-acylneuraminate synthetase in the presence and absence of CDP
J. Biol. Chem.
276
8190-8196
2001
Neisseria meningitidis (P0A0Z8), Neisseria meningitidis
brenda
Knorst, M.; Fessner, W.D.
CMP-sialate synthetase from Neisseria meningitidis - overexpression and application to the synthesis of oligosaccharides containing modified sialic acids
Adv. Synth. Catal.
343
698-710
2001
Neisseria meningitidis
-
brenda
Bravo, I.G.; Reglero, A.
The cytidylyltransferases family: properties, kinetics, genomic and phylogeny: The cytidylyltransferases family: properties, kinetics, genomic and phylogeny
Recent Res. Devel. Biochem.
4
223-254
2003
Bos taurus, Cricetinae, Equus caballus, Erinaceidae, Escherichia coli, Homo sapiens, Mannheimia haemolytica, Neisseria meningitidis, Oncorhynchus mykiss, Rattus norvegicus, Streptococcus agalactiae, Sus scrofa, [Haemophilus] ducreyi
-
brenda
Fujita, A.; Sato, C.; Munster-Kuhnel, A.K.; Gerardy-Schahn, R.; Kitajima, K.
Development of a simple and efficient method for assaying cytidine monophosphate sialic acid synthetase activity using an enzymatic reduced nicotinamide adenine dinucleotide/oxidized nicotinamide adenine dinucleotide converting system
Anal. Biochem.
337
12-21
2005
Mus musculus, Oncorhynchus mykiss
brenda
Yu, H.; Karpel, R.; Chen, X.
Chemoenzymatic synthesis of CMP-sialic acid derivatives by a one-pot two-enzyme system: comparison of substrate flexibility of three microbial CMP-sialic acid synthetases
Bioorg. Med. Chem.
12
6427-6435
2004
Neisseria meningitidis
brenda
Liu, G.; Jin, C.
CMP-N-acetylneuraminic acid synthetase from Escherichia coli K1 is a bifunctional enzyme: identification of minimal catalytic domain for synthetase activity and novel functional domain for platelet-activating factor acetylhydrolase activity
J. Biol. Chem.
279
17738-17749
2004
Escherichia coli, Escherichia coli K1
brenda
Feo-Manga, J.C.; Rodriguez-Aparicio, L.B.; Ferrero, M.A.; Reglero, A.
Purification and partial characterization of CMP-Neu5Ac synthetase from rat brain
Anal. Chim. Acta
564
141-150
2006
Rattus norvegicus
-
brenda
Mizanur, R.M.; Pohl, N.L.
Cloning and characterization of a heat-stable CMP-N-acylneuraminic acid synthetase from Clostridium thermocellum
Appl. Microbiol. Biotechnol.
76
827-834
2007
Acetivibrio thermocellus, Acetivibrio thermocellus ATCC 27405
brenda
Misaki, R.; Fujiyama, K.; Seki, T.
Expression of human CMP-N-acetylneuraminic acid synthetase and CMP-sialic acid transporter in tobacco suspension-cultured cell
Biochem. Biophys. Res. Commun.
339
1184-1189
2006
Homo sapiens
brenda
Fujita, A.; Sato, C.; Kitajima, K.
Identification of the nuclear export signals that regulate the intracellular localization of the mouse CMP-sialic acid synthetase
Biochem. Biophys. Res. Commun.
355
174-180
2007
Mus musculus (Q99KK2), Mus musculus
brenda
Yu, H.; Ryan, W.; Yu, H.; Chen, X.
Characterization of a bifunctional cytidine 5-monophosphate N-acetylneuraminic acid synthetase cloned from Streptococcus agalactiae
Biotechnol. Lett.
28
107-113
2006
Streptococcus agalactiae (Q9AFG9), Streptococcus agalactiae
brenda
Viswanathan, K.; Tomiya, N.; Park, J.; Singh, S.; Lee, Y.C.; Palter, K.; Betenbaugh, M.J.
Expression of a functional Drosophila melanogaster CMP-sialic acid synthetase. Differential localization of the Drosophila and human enzymes
J. Biol. Chem.
281
15929-15940
2006
Drosophila melanogaster
brenda
Mizanur, R.M.; Pohl, N.L.
Bacterial CMP-sialic acid synthetases: production, properties, and applications
Appl. Microbiol. Biotechnol.
80
757-765
2008
Acetivibrio thermocellus, Escherichia coli, [Haemophilus] ducreyi, Mannheimia haemolytica, Neisseria meningitidis, Escherichia coli K-235, Mannheimia haemolytica A2
brenda
Yu, C.C.; Lin, P.C.; Lin, C.C.
Site-specific immobilization of CMP-sialic acid synthetase on magnetic nanoparticles and its use in the synthesis of CMP-sialic acid
Chem. Commun. (Camb. )
21
1308-1310
2008
Neisseria meningitidis
brenda
Tiralongo, J.; Fujita, A.; Sato, C.; Kitajima, K.; Lehmann, F.; Oschlies, M.; Gerardy-Schahn, R.; Muenster-Kuehnel, A.K.
The rainbow trout CMP-sialic acid synthetase utilises a nuclear localization signal different from that identified in the mouse enzyme
Glycobiology
17
945-954
2007
Oncorhynchus mykiss (Q90WG6), Oncorhynchus mykiss
brenda
Oschlies, M.; Dickmanns, A.; Haselhorst, T.; Schaper, W.; Stummeyer, K.; Tiralongo, J.; Weinhold, B.; Gerardy-Schahn, R.; von Itzstein, M.; Ficner, R.; Muenster-Kuehnel, A.K.
A C-terminal phosphatase module conserved in vertebrate CMP-sialic acid synthetases provides a tetramerization interface for the physiologically active enzyme
J. Mol. Biol.
393
83-97
2009
Mus musculus (Q99KK2), Mus musculus
brenda
Wong, J.H.; Sahni, U.; Li, Y.; Chen, X.; Gervay-Hague, J.
Synthesis of sulfone-based nucleotide isosteres: identification of CMP-sialic acid synthetase inhibitors
Org. Biomol. Chem.
7
27-29
2009
Neisseria meningitidis
brenda
Li, Y.; Yu, H.; Cao, H.; Muthana, S.; Chen, X.
Pasteurella multocida CMP-sialic acid synthetase and mutants of Neisseria meningitidis CMP-sialic acid synthetase with improved substrate promiscuity
Appl. Microbiol. Biotechnol.
93
2411-2423
2012
[Haemophilus] ducreyi, Neisseria meningitidis, Pasteurella multocida, Pasteurella multocida ATCC 15742
brenda
Kajiwara, H.; Mine, T.; Miyazaki, T.; Yamamoto, T.
A CMP-N-acetylneuraminic acid synthetase purified from a marine bacterium, Photobacterium leiognathi JT-SHIZ-145
Biosci. Biotechnol. Biochem.
75
47-53
2011
Photobacterium leiognathi, Photobacterium leiognathi JT-SHIZ-145
brenda
Horsfall, L.E.; Nelson, A.; Berry, A.
Identification and characterization of important residues in the catalytic mechanism of CMP-Neu5Ac synthetase from Neisseria meningitidis
FEBS J.
277
2779-2790
2010
Neisseria meningitidis (P0A0Z8), Neisseria meningitidis
brenda
Schaper, W.; Bentrop, J.; Ustinova, J.; Blume, L.; Kats, E.; Tiralongo, J.; Weinhold, B.; Bastmeyer, M.; Muenster-Kuehnel, A.K.
Identification and biochemical characterization of two functional CMP-sialic acid synthetases in Danio rerio
J. Biol. Chem.
287
13239-13248
2012
Danio rerio (H9BFW7), Danio rerio (Q0E671), Danio rerio
brenda
Bose, S.; Purkait, D.; Joseph, D.; Nayak, V.; Subramanian, R.
Structural and functional characterization of CMP-N-acetylneuraminate synthetase from Vibrio cholerae
Acta Crystallogr. Sect. D
75
564-577
2019
Vibrio cholerae
brenda
Mertsalov, I.B.; Novikov, B.N.; Scott, H.; Dangott, L.; Panin, V.M.
Characterization of Drosophila CMP-sialic acid synthetase activity reveals unusual enzymatic properties
Biochem. J.
473
1905-1916
2016
Drosophila melanogaster (Q8IQV0), Drosophila melanogaster
brenda
Matthews, M.M.; McArthur, J.B.; Li, Y.; Yu, H.; Chen, X.; Fisher, A.J.
Catalytic cycle of Neisseria meningitidis CMP-sialic acid synthetase illustrated by high-resolution protein crystallography
Biochemistry
59
3157-3168
2020
Neisseria meningitidis (P0A0Z8), Neisseria meningitidis
brenda
Abeln, M.; Borst, K.M.; Cajic, S.; Thiesler, H.; Kats, E.; Albers, I.; Kuhn, M.; Kaever, V.; Rapp, E.; Muenster-Kuehnel, A.; Weinhold, B.
Sialylation is dispensable for early murine embryonic development in vitro
ChemBioChem
18
1305-1316
2017
Mus musculus (Q99KK2), Mus musculus
brenda
Di, W.; Fujita, A.; Hamaguchi, K.; Delannoy, P.; Sato, C.; Kitajima, K.
Diverse subcellular localizations of the insect CMP-sialic acid synthetases
Glycobiology
27
329-341
2017
Aedes aegypti, Aedes aegypti (Q0IG96), Tribolium castaneum, Tribolium castaneum (A0A2Z5TXA4), Mus musculus (A0A0R4J0B4), Drosophila melanogaster (Q8IQV0), Drosophila melanogaster
brenda
Urbanek, K.; Sutherland, D.M.; Orchard, R.C.; Wilen, C.B.; Knowlton, J.J.; Aravamudhan, P.; Taylor, G.M.; Virgin, H.W.; Dermody, T.S.
Cytidine monophosphate N-acetylneuraminic acid synthetase and solute carrier family 35 member A1 are required for reovirus binding and infection
J. Virol.
95
e01571-20
2020
Mus musculus (Q99KK2), Mus musculus
brenda
Ma, Y.; Tian, S.; Wang, Z.; Wang, C.; Chen, X.; Li, W.; Yang, Y.; He, S.
CMP-N-acetylneuraminic acid synthetase interacts with fragile X related protein 1
Mol. Med. Rep.
14
1501-1508
2016
Homo sapiens (Q8NFW8)
brenda
O Day, E.M.; Idos, G.E.; Hill, C.; Chen, J.W.; Wagner, G.
Cytidine monophosphate N-acetylneuraminic acid synthetase enhances invasion of human triple-negative breast cancer cells
OncoTargets Ther.
11
6827-6838
2018
Homo sapiens (Q8NFW8), Homo sapiens
brenda