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Information on EC 2.7.7.43 - N-acylneuraminate cytidylyltransferase
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2.7.7.43 N-acylneuraminate cytidylyltransferaseIUBMB Comments
Acts on N-acetyl- and N-glycolyl- derivatives.
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Word Map
- 2.7.7.43
-
sialylation
-
sialyltransferase
- meningitidis
-
polysialic
- lipooligosaccharide
-
sialoglycoconjugates
- n-acetylmannosamine
- ducreyi
- synthesis
- kdn
- mannac
- neu5gc
- agriculture
- medicine
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
Synonyms
AaCSS, acylneuraminate cytidyltransferase, CMAS, Cmas1, Cmas2, CMP sialate pyrophosphorylase, CMP-N-acetylneuraminate synthase, CMP-N-acetylneuraminate synthetase, CMP-N-acetylneuraminic acid synthase, CMP-N-acetylneuraminic acid synthetase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acylneuraminate cytidyltransferase
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CMAS
CMP sialate pyrophosphorylase
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CMP-N-acetylneuraminate synthase
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CMP-N-acetylneuraminate synthetase
CMP-N-acetylneuraminic acid synthase
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CMP-N-acetylneuraminic acid synthetase
CMP-N-acylneuraminic acid synthetase
CMP-NANA synthetase
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CMP-Neu5Ac synthetase
CMP-NeuAc synthetase
CMP-NeuNAc synthetase
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-
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CMP-Sia synthetase
CMP-sialate synthase
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CMP-sialate synthetase
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CMP-sialic acid synthetase
CMP-sialic synthetase
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CMPsialate pyrophosphorylase
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CMPsialate synthase
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CSS
cytidine 5'-monophosphate N-acetylneuraminic acid synthetase
cytidine 5'-monophospho-N-acetylneuraminic acid synthetase
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cytidine 5'-monophosphosialic acid synthetase
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cytidine 5-monophosphate N-acetylneuraminic acid synthetase
cytidine monophosphate N-acetylneuraminic acid synthetase
cytidine monophosphate sialic acid synthetase
cytidine monophosphate-N-acetylneuraminic acid synthetase
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cytidine monophospho-sialic acid synthetase
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cytidine monophosphoacetylneuraminic synthetase
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cytidine monophosphosialate pyrophosphorylase
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cytidine monophosphosialate synthetase
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cytidyltransferase, acylneuraminate
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cytidylyltransferase, acetylneuraminate
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sialate cytidylyltransferase
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CMP-N-acetylneuraminate synthetase
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CMP-N-acetylneuraminic acid synthetase
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CMP-Neu5Ac synthetase
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CMP-NeuAc synthetase
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CMP-Sia synthetase
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CMP-sialic acid synthetase
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cytidine 5'-monophosphate N-acetylneuraminic acid synthetase
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cytidine 5-monophosphate N-acetylneuraminic acid synthetase
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cytidine 5-monophosphate N-acetylneuraminic acid synthetase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
CTP + N-acetylneuraminate = diphosphate + CMP-N-acylneuraminate
typical ordered-sequential kinetic behaviour, enzyme does not bind N-acetylneuraminate in the absence of CTP
CTP + N-acetylneuraminate = diphosphate + CMP-N-acylneuraminate
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CTP + N-acylneuraminate = diphosphate + CMP-N-acylneuraminate
ping pong bi bi mechanism with CTP as the first substrate and CMP-NeuAc as the last product
-
CTP + N-acylneuraminate = diphosphate + CMP-N-acylneuraminate
ordered bi-bi kinetic mechanism. CTP binds first and CMP-NeuAc dissociates last. The rate-limiting step appears to be dissociation of CMP-NeuAc
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CTP + N-acylneuraminate = diphosphate + CMP-N-acylneuraminate
ping pong bi bi mechanism with CTP as the first substrate and CMP-NeuAc as the last product
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CTP + N-acylneuraminate = diphosphate + CMP-N-acylneuraminate
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nucleotidyl group transfer
nucleotidyl group transfer
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-
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-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
CTP:N-acylneuraminate cytidylyltransferase
Acts on N-acetyl- and N-glycolyl- derivatives.
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CAS REGISTRY NUMBER
COMMENTARY
9067-82-7
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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 + N-(N-benzyloxycarbonyl-glycyl)-muramic acid
diphosphate + CMP-N-(N-benzyloxycarbonyl-glycyl)-muramic acid
-
-
-
-
?
CTP + N-acetyl-neuraminate
diphosphate + CMP-N-acetylneuraminate
-
-
-
?
CTP + N-acetylmuramic acid
diphosphate + CMP-N-acetylmuramic acid
-
-
-
-
?
CTP + N-azidoacetylmuramic acid
diphosphate + CMP-N-azidoacetylmuramic acid
-
-
-
-
?
CTP + N-azidomuramic acid
diphosphate + CMP-N-azidomuramic acid
-
-
-
-
?
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
-
-
-
-
?
deaminoneuraminic acid + CTP
CMP-KDN + diphosphate
N-glycolylneuraminic acid (Neu5Gc) and deaminoneuraminic acid (KDN) are also substrates
-
-
?
N-acetyl-7(8)-O-acetylneuraminate + CTP
diphosphate + CMP-N-acetyl-7(8)-O-acetylneuraminate
N-glycolylneuraminic acid + CTP
CMP-Neu5Gc + diphosphate
N-glycolylneuraminic acid (Neu5Gc) and deaminoneuraminic acid (KDN) are also substrates
-
-
?
UDP + N-acetylneuraminate
phosphate + UMP-N-acetylneuraminate
-
-
-
-
?
UTP + N-glycolylneuraminic acid
UMP-N-glycolylneuraminate + diphosphate
-
-
-
-
?
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
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no activity
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-
?
CDP + N-acetylneuraminate
phosphate + CMP-N-acetylneuraminate
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no activity with CDP
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?
CDP + N-acetylneuraminate
phosphate + CMP-N-acetylneuraminate
-
-
-
-
?
CDP + N-acetylneuraminate
phosphate + CMP-N-acetylneuraminate
-
-
-
-
?
CDP + N-acetylneuraminate
phosphate + CMP-N-acetylneuraminate
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-
-
-
?
CDP + N-acetylneuraminate
phosphate + CMP-N-acetylneuraminate
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no activity with CDP
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-
?
CDP + N-acetylneuraminate
phosphate + CMP-N-acetylneuraminate
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no activity with CDP
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?
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
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?
CTP + 3-deoxy-D-glycero-D-galacto-nononate
diphosphate + CMP-3-deoxy-D-glycero-D-galacto-nononate
-
reaction of EC 2.7.7.92
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?
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
-
-
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?
CTP + N-acetylneuraminic acid
diphosphate + CMP-N-acetylneuraminic acid
the enzyme displays specificity for N-acetylneuraminic acid as a substrate
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?
CTP + N-acetylneuraminic acid
diphosphate + CMP-N-acetylneuraminic acid
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-
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?
CTP + N-acetylneuraminic acid
diphosphate + CMP-N-acetylneuraminic acid
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
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?
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
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?
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%
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?
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
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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
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?
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
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?
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
-
-
-
-
?
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
-
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
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
-
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
-
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
-
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
-
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
[Haemophilus] ducreyi 35000
-
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
[Haemophilus] ducreyi 35000
-
-
-
-
?
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
-
-
-
-
?
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-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
-
-
-
-
?
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
?
-
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
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
CTP + N-acetylneuraminic acid
diphosphate + CMP-N-acetylneuraminic acid
-
-
-
?
CTP + N-glycolneuraminate
diphosphate + CMP-N-glycolneuraminate
-
N-glycolneuraminate is a relatively weaker substrate than 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
-
CMP-NeuAc is essential for the formation of capsule polysialylate for strain K1
-
-
?
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
-
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
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
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
-
the enzyme produces CMP-N-acetylneuraminate, the nucleotide sugar donor used by sialyltransferase
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
[Haemophilus] ducreyi 35000
-
the enzyme produces CMP-N-acetylneuraminate, the nucleotide sugar donor used by sialyltransferase
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
Fe2+
Mg2+
Mn2+
Zn2+
Ca2+
-
divalent metal ion is strictly required, with 20 mM Ca2+ 13% of the activation compared to activation by Mg2+
Co2+
the enzyme can function with a broad range of metal cofactors like Zn2+, Fe2+, Co2+ and Mn2+
Co2+
-
divalent metal ion is strictly required, with 20 mM Mn2+ 27% of the activation compared to activation by Mg2+
Fe2+
the enzyme can function with a broad range of metal cofactors like Zn2+, Fe2+, Co2+ and Mn2+
Mg2+
the activity of the enzyme with Mg2+ is low, 20 mM Mg2+ is used in assay conditions
Mg2+
-
divalent metal ion is strictly required, maximal activity at 10 mM
Mg2+
-
required for activity, maximum activity at 10 mM Mg2+, decreasing at higher Mg2+ concentrations
Mg2+
required for CMP-sialic acid synthetase activity but not for acetylhydrolase activity
Mg2+
-
absolutely required for activity, 20 mM Mg2+ gives the most activity
Mn2+
the enzyme can function with a broad range of metal cofactors like Zn2+, Fe2+, Co2+ and Mn2+
Mn2+
-
absolute requirement for a divalent cation for activity, maximum activity at 10 mM Mn2+
Mn2+
-
required for activity, can be replaced by Mg2+, Co2+, and Zn2+ in decreasing order
Mn2+
-
the enzyme has an absolute requirement for a divalent cation for activity and reaches maximum activity in the presence of 10 mM Mn2+
Mn2+
-
divalent metal ion is strictly required, with 20 mM Mn2+ 28% of the activation compared to activation by Mg2+
Mn2+
required for CMP-sialic acid synthetase activity but not for acetylhydrolase activity, maximum activity with 4 mM MnCl
Mn2+
-
required for activity, Mn2+ is only 40% as effective as Mg2+ at 20 mM
Zn2+
the enzyme can function with a broad range of metal cofactors like Zn2+, Fe2+, Co2+ and Mn2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
saturated sulfo-UDP ester
-
1 mM, 37ĆĀ°C, pH 8.5, 15 min, 24% inhibition
EDTA
-
treatment with EDTA results in loss of catalytic activity which can be restored by the addition of either Mg2+ or Mn2+
Mn2+
both catalytic functions are impaired by high concentrations of Mn2+
additional information
-
the addition of monovalent cations (K+, Na+) to the reaction mixtures has no effect on the enzyme activity
-
additional information
-
enzyme is inhibited by thiol-modifying reagents; enzyme is not inhibited by thiol-containing reagents like GSH, mercaptoethanol and cysteine
-
additional information
no activity is detected when the enzyme is substituted with 5-35 mM Co2+ or Ca2+
-
additional information
-
no activity is detected when the enzyme is substituted with 5-35 mM Co2+ or Ca2+
-
additional information
-
dithiothreitol has little effect on enzyme activity
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
20-30 mM, 3fold stimulation with N-acetylneuraminate as substrate, 1.5fold increase in activity with 4-O-methyl-N-acetylneuraminate as substrate
2-mercaptoethanol
-
1 mM is required for optimal activity of both crude and purified enzyme
dithiothreitol
-
Dithiothreitol at a concentration of 0.2 mM stimulates enzyme activity by 158%
additional information
-
mercaptoethanol has no stimulatory effect
-
additional information
-
no enhancement of activity with dithiothreitol, glutathione, or beta-mercaptoethanol
-
additional information
no necessity of including a sulfhydryl reagent, such as dithiothreitol, in the assay reaction
-
additional information
-
no necessity of including a sulfhydryl reagent, such as dithiothreitol, in the assay reaction
-
additional information
DTT has no effect on enzyme activity
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Infections
Cytidine Monophosphate N-Acetylneuraminic Acid Synthetase and Solute Carrier Family 35 Member A1 Are Required for Reovirus Binding and Infection.
Meningitis
[Minimal functional domain of cytidine 5'-monophosphate N-acetylneuraminic acid (CMP-NeuAc) synthetase from Escherichia coli]
Neoplasms
Sialic acid metabolism in rats undergoing chemically-induced mammary gland carcinogenesis in specific dietary states.
Neoplasms
Synthesis of double mesoporous core-shell silica spheres with tunable core porosity and their drug release and cancer cell apoptosis properties.
Triple Negative Breast Neoplasms
Cytidine monophosphate N-acetylneuraminic acid synthetase enhances invasion of human triple-negative breast cancer cells.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.3
N-acetylneuraminate methyl ester
-
pH 9.0, 37ĆĀ°C, reaction with CTP
0.043
CTP
N-terminal domain and C-terminal domain of CMP-sialic acid synthetase
0.24
CTP
-
at 50ĆĀ°C, 10 mM MnCl2, 50 mM Tris buffer (pH 9.5)
2.6
CTP
-
pH 9.0, 37ĆĀ°C, reaction with N-acetylneuraminate methyl ester
0.13
N-acylneuraminate
-
at 50ĆĀ°C, 10 mM MnCl2, 50 mM Tris buffer (pH 9.5)
0.16
N-glycolylneuraminic acid
-
at 50ĆĀ°C, 10 mM MnCl2, 50 mM Tris buffer (pH 9.5)
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
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.33
CTP
-
at 50ĆĀ°C, 10 mM MnCl2, 50 mM Tris buffer (pH 9.5)
3.87
CTP
N-terminal domain and C-terminal domain of CMP-sialic acid synthetase
2.25
N-acylneuraminate
-
at 50ĆĀ°C, 10 mM MnCl2, 50 mM Tris buffer (pH 9.5)
1.66
N-glycolylneuraminic acid
-
at 50ĆĀ°C, 10 mM MnCl2, 50 mM Tris buffer (pH 9.5)
2.29
sialic acid
CMP-sialic acid synthetase, substrate N-acetylneuraminic acid
3.47
sialic acid
N-terminal domain and C-terminal domain of CMP-sialic acid synthetase, substrate N-acetylneuraminic acid
3.56
sialic acid
N-terminal domain of CMP-sialic acid synthetase, substrate N-acetylneuraminic acid
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.13
2-deoxy-2,3-dehydro-N-acetylneuraminic acid
Neisseria meningitidis
at pH 8.5 and 37ĆĀ°C
additional information
CDP
Neisseria meningitidis
-
1 mM, 37ĆĀ°C, pH 8.5, 15 min, 14% inhibition
additional information
saturated sulfo-CDP
Neisseria meningitidis
-
1 mM, 37ĆĀ°C, pH 8.5, 15 min, 55% inhibition
additional information
saturated sulfo-UDP
Neisseria meningitidis
-
1 mM, 37ĆĀ°C, pH 8.5, 15 min, 35% inhibition
additional information
saturated sulfo-UDP ester
Neisseria meningitidis
-
1 mM, 37ĆĀ°C, pH 8.5, 15 min, 24% inhibition
additional information
sulfo-CDP
Neisseria meningitidis
-
1 mM, 37ĆĀ°C, pH 8.5, 15 min, 47% inhibition
additional information
sulfo-CTP
Neisseria meningitidis
-
1 mM, 37ĆĀ°C, pH 8.5, 15 min, 39% inhibition
additional information
sulfo-UDP
Neisseria meningitidis
-
1 mM, 37ĆĀ°C, pH 8.5, 15 min, 6% inhibition
additional information
sulfo-UTP
Neisseria meningitidis
-
1 mM, 37ĆĀ°C, pH 8.5, 15 min, 33% inhibition
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.2
substrate N-glycolylneuraminate, pH 7.5, temperature not specified in the publication
0.3
substrate 5-deaminoneuraminate, pH 7.5, temperature not specified in the publication
2.7
substrate N-glycolylneuraminate, pH 7.5, temperature not specified in the publication
3.3
substrate 5-deaminoneuraminate, pH 7.5, temperature not specified in the publication
4.5
substrate N-acetylneuraminate, pH 7.5, temperature not specified in the publication
additional information
additional information
-
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
additional information
-
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
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5
9.5
8
-
at an ionic strength ranging between 50-250 mM, in Tris-HCl buffer, glycine-NaOH as well as in phosphate buffer
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 9
the enzyme has a relatively narrow optimum around pH 8.0. In standard assay conditions, the enzyme activity declines precipitously at lower pH, dropping to 20% around pH 7.4 and becoming practically negligible below pH 7.0. The enzyme activity also declines substantially but more gradually, losing around 50% at pH 9.0. The enzyme exhibits significant activity at pH 6.5 in the presence of Mn2+, Co2+, Zn2+, Fe2+ and Ni2+
7 - 10
-
pH 7.0: about 90% of maximal activity, pH 10.0: about 70% of maximal activity
7 - 12.5
-
activity decreases dramatically below pH 7.0 and above pH 12.5
7.5 - 9
7.5 - 9.5
-
pH 7.5: about 20% of maximal activity, pH 8.0: about 90% of maximal activity, pH 9.5: about 65% of maximal activity
8 - 13
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
40 - 60
-
immobilized enzyme yields maximal activity at 40ĆĀ°C which is maintained up to 60ĆĀ°C, whereas the activity of the soluble enzyme decreases sharply above 40ĆĀ°C
45
50
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 45
the enzyme activity steadily increases with temperature from 20 C to 45 C by approximately an order of magnitude. The activity declines dramatically at temperatures above 45 C
25 - 42
-
4ĆĀ°C: activity is undetectable, 25-37ĆĀ°C: maximal activity, 42ĆĀ°C: 12% of maximal activity
30 - 50
-
30ĆĀ°C: about 40% of maximal activity, 50ĆĀ°C: about 90% of maximal activity
37 - 60
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
wild-type and glycosylation mutant LEC29.Lec32, the mutation resides in either the structural gene encoding CMP-NeuAc synthetase or in a gene that regulates the prpduction of the active enzyme
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
robust expression in the entire central nervous system, the somites, the notochord, and the developing pronephric duct
brenda
more or less ubiquitously expressed from the end of gastrula through segmentation
brenda
-
DmCSAS gene is greatly enriched in adult head, suggesting a possible role in the central nervous system
brenda
robust expression in the entire central nervous system, the somites, the notochord, and the developing pronephric duct
brenda
robust expression in the entire central nervous system, the somites, the notochord, and the developing pronephric duct
brenda
additional information
during the pharyngula stage, expression is restricted to the brain
brenda
additional information
not detected in skeletal muscle, liver, or kidney
brenda
additional information
not detected in skeletal muscle, liver, or kidney
brenda
additional information
-
not detected in skeletal muscle, liver, or kidney
brenda
additional information
-
DmCSAS gene is developmentally regulated, with expression first appearing at 12-24 h of embryogenesis, low expression through larval and pubal stages
brenda
additional information
-
no activity in skeletal muscle. The expression the enzyme is tissue-dependent and does not seem to be embryonically determined. 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
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
a small, but significant population of the mouse CMP-sialic acid synthetase is also present in cytoplasm
brenda
the N-terminal hydrophobic regions of AaCSS functions as a signalpeptide to render it soluble in the endoplasmic reticulum
brenda
the N-terminal hydrophobic regions of TcCSS functions as a signal peptide to render it soluble in the endoplasmic reticulum
brenda
-
unlike all vertebrate CSAS that localize to the nucleus, the DmCSAS is localized to the Golgi compartment
brenda
vertebrate CSS are usually localised in the nucleus due to a nuclear localisation signal, however in mouse a small proportion of CSS is also present in cytoplasm due to two nuclear export signals
brenda
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
-
brenda
additional information
no localization in the nucleus. The N-terminus of DmCSS functions as a membrane-spanning region of type II transmembrane proteins whose cytosolic KLK sequence functions as an endoplasmic reticulum export signal
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brenda
additional information
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no localization in the nucleus. The N-terminus of DmCSS functions as a membrane-spanning region of type II transmembrane proteins whose cytosolic KLK sequence functions as an endoplasmic reticulum export signal
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brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
the enzyme is involved in the biosynthesis of sialoglycoconjugates in vertebrates, overview
physiological function
evolution
enzyme AaCSS shares a common overall structure with Drosophila melanogaster CSS in terms of evolutionarily conserved motifs and the absence of the C-terminal domain typical to vertebrate CSSs
evolution
enzyme DmCSS shows a structure with evolutionarily conserved motifs and the absence of the C-terminal domain typical to vertebrate CSSs. The most prominent feature of Drosophila melanogaster CMP-Sia synthetase (DmCSS) is its Golgi-localization, contrasted with nuclear localization of vertebrate CSSs
evolution
enzyme TcCSS shares a common overall structure with Drosophila melanogaster CSS in terms of evolutionarily conserved motifs and the absence of the C-terminal domain typical to vertebrate CSSs
malfunction
cells lacking functional enzyme display increased viability during reovirus infection
malfunction
cleavage of the N-terminal hydrophobic region of the CSSs is critical for the enzyme activity
malfunction
cleavage of the N-terminal hydrophobic region of the CSSs is critical for the enzyme activity
malfunction
mouse embryonic stem cell (mESC) lines that lack CMP-Sia synthetase (CMAS) and thereby the ability to activate Sia to CMP-Sia show that loss of CMAS activity results in an asialo cell surface accompanied by an increase in glycoconjugates with terminal galactosyl and oligo-LacNAc residues, as well as intracellular accumulation of free Sia. These changes do not impact intracellular metabolites or the morphology and transcriptome of pluripotent mESC lines. Moreover, the capacity of Cmas-/- mESCs for undirected differentiation into embryoid bodies, germ layer formation and even the generation of beating cardiomyocytes provides first and conclusive evidence that pluripotency and differentiation of mESC in vitro can proceed in the absence of (poly)sialoglycans. Genetic ablation of CMAS results in complete loss of cellsurface sialylation with concomitant increase in LacNAc structures. Intracellular Neu5Ac accumulation alters neither associated metabolites nor intracellular glycosylation
physiological function
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CMP-sialic acid synthetase is a key enzyme in the biosynthesis of the capsular polysaccharides required for bacterial infection
physiological function
CMAS activity is essential for maintaining cellular homeostasis of sialic acid biosynthesis
physiological function
the enzyme gene is required for serotype 3 reovirus binding and infection of microglial cells
physiological function
the enzyme plays an important role in triple-negative breast cancer tumor formation and invasivity
Show AA Sequence and Transmembrane Helices (3577 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
175800
tetramer, CMP-sialic acid synthetase, determined by gel filtration
25440
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2 * 25440, dimer or larger oligomer, electrospray mass spectrometry