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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
-
ducreyi
-
sialoglycoconjugates
- n-acetylmannosamine
- synthesis
- neu5gc
- kdn
- mannac
- medicine
- agriculture
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
acylneuraminate cytidyltransferase, Cmas1, Cmas2, CMP sialate pyrophosphorylase, CMP-N-acetylneuraminate synthase, CMP-N-acetylneuraminate synthetase, CMP-N-acetylneuraminic acid synthase, CMP-N-acetylneuraminic acid synthetase, CMP-N-acylneuraminic acid synthetase, CMP-NANA synthetase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acylneuraminate cytidyltransferase
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CMP sialate pyrophosphorylase
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CMP-N-acetylneuraminate synthase
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CMP-N-acetylneuraminate synthetase
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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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-
-
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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 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-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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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
CTP + N-acetylneuraminate = diphosphate + CMP-N-acylneuraminate
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CTP + N-acetylneuraminate = diphosphate + CMP-N-acylneuraminate
typical ordered-sequential kinetic behaviour, enzyme does not bind N-acetylneuraminate in the absence of CTP
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CTP + N-acylneuraminate = 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
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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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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nucleotidyl group transfer
nucleotidyl group transfer
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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
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-
-
-
?
CTP + (N-4-O-)diacetylneuraminic acid
diphosphate + CMP-N-4-O-diacetylneuraminate
-
(N-4-O-)diacetylneuraminic acid is 46% effective compared to N-acylneuraminate
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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
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
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-
-
-
?
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
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CDP + N-acetylneuraminate
phosphate + CMP-N-acetylneuraminate
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-
-
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?
CDP + N-acetylneuraminate
phosphate + CMP-N-acetylneuraminate
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-
-
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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
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-
?
CTP + 3-deoxy-D-glycero-D-galacto-nononate
diphosphate + CMP-3-deoxy-D-glycero-D-galacto-nononate
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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
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reaction of EC 2.7.7.92
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?
CTP + N-acetylneuraminate
diphosphate + CMP-N-acetylneuraminate
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-
-
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?
CTP + N-acetylneuraminate
diphosphate + CMP-N-acetylneuraminate
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-
-
-
?
CTP + N-acetylneuraminate
diphosphate + CMP-N-acetylneuraminate
-
-
-
-
?
CTP + N-acetylneuraminate
diphosphate + CMP-N-acetylneuraminate
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-
-
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?
CTP + N-acetylneuraminate
diphosphate + CMP-N-acetylneuraminate
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-
-
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?
CTP + N-acetylneuraminate
diphosphate + CMP-N-acetylneuraminate
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-
-
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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
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?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
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-
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?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
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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
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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
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-
-
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?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
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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
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?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
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CMP-NeuAc is essential for the formation of capsule polysialylate for strain K1
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?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
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CMP-NeuAc is essential for the formation of capsule polysialylate for strain K1
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?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
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-
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?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
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reaction is freely reversible and the ratio of the velocities in synthesis and degradation direction is 3:1
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r
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
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the enzyme produces CMP-N-acetylneuraminate, the nucleotide sugar donor used by sialyltransferase
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-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
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-
-
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CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
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the enzyme produces CMP-N-acetylneuraminate, the nucleotide sugar donor used by sialyltransferase
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?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
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-
-
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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
-
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
-
-
-
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-
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
-
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?
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
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
-
ir
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
-
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
-
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 methyl ester
diphosphate + CMP-N-acylneuraminate methyl ester
-
-
-
-
?
CTP + N-acylneuraminate methyl ester
diphosphate + CMP-N-acylneuraminate methyl ester
-
-
-
-
?
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
-
-
-
-
?
CTP + N-glycolylneuraminate
diphosphate + CMP-N-glycolylneuraminate
-
-
-
-
?
CTP + N-glycolylneuraminate
diphosphate + CMP-N-glycolylneuraminate
-
-
-
r
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
-
no activity with UTP
-
-
-
UTP + N-acylneuraminate
diphosphate + UMP-N-acylneuraminate
-
no activity with UTP
-
-
-
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 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 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-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
-
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
-
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 + 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
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
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
Fe2+
Mg2+
Mn2+
Zn2+
-
62% as effective as Mn2+; can replace Mn2+, 62% as effective as Mn2+ at 10 mM
Ca2+
-
divalent metal ion is strictly required, with 20 mM Ca2+ 13% of the activation compared to activation by Mg2+
Co2+
-
66% as effective as Mn2+; can replace Mn2+, 66% as effective as Mn2+ at 10 mM
Co2+
-
divalent metal ion is strictly required, with 20 mM Mn2+ 27% of the activation compared to activation by Mg2+
Mg2+
-
absolutely required for activity, 20 mM Mg2+ gives the most activity
Mg2+
-
20 mM; 57% as effective as Mn2+; can replace Mn2+, 57% as effective as Mn2+ at 10 mM
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
Mn2+
-
required for activity, Mn2+ is only 40% as effective as Mg2+ at 20 mM
Mn2+
-
absolute requirement for a divalent cation for activity, maximum activity at 10 mM 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+
-
required for activity, can be replaced by Mg2+, Co2+, and Zn2+ in decreasing order
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
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
saturated sulfo-UDP ester
-
1 mM, 37°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
-
dithiothreitol has little effect on enzyme activity
-
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+
-
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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
DTT has no effect on enzyme activity
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
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.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.3
N-acetylneuraminate methyl ester
-
pH 9.0, 37°C, reaction with CTP
0.043
CTP
-
N-terminal domain and C-terminal domain of CMP-sialic acid synthetase
0.24
CTP
-
; at 50°C, 10 mM MnCl2, 50 mM Tris buffer (pH 9.5)
2.6
CTP
-
pH 9.0, 37°C, reaction with N-acetylneuraminate methyl ester
1.9
N-acetylneuraminate
-
pH 9.0, 37°C, reaction with UDP; pH 9.0, 37°C, reaction with UTP
0.13
N-acylneuraminate
-
at 50°C, 10 mM MnCl2, 50 mM Tris buffer (pH 9.5)
0.16
N-glycolylneuraminic acid
-
at 50°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
2.25
N-acylneuraminate
-
at 50°C, 10 mM MnCl2, 50 mM Tris buffer (pH 9.5)
3.33
CTP
-
; at 50°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
1.66
N-glycolylneuraminic acid
-
at 50°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
additional information
CDP
Neisseria meningitidis
-
1 mM, 37°C, pH 8.5, 15 min, 14% inhibition
additional information
saturated sulfo-CDP
Neisseria meningitidis
-
1 mM, 37°C, pH 8.5, 15 min, 55% inhibition
additional information
saturated sulfo-UDP
Neisseria meningitidis
-
1 mM, 37°C, pH 8.5, 15 min, 35% inhibition
additional information
saturated sulfo-UDP ester
Neisseria meningitidis
-
1 mM, 37°C, pH 8.5, 15 min, 24% inhibition
additional information
sulfo-CDP
Neisseria meningitidis
-
1 mM, 37°C, pH 8.5, 15 min, 47% inhibition
additional information
sulfo-CTP
Neisseria meningitidis
-
1 mM, 37°C, pH 8.5, 15 min, 39% inhibition
additional information
sulfo-UDP
Neisseria meningitidis
-
1 mM, 37°C, pH 8.5, 15 min, 6% inhibition
additional information
sulfo-UTP
Neisseria meningitidis
-
1 mM, 37°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
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
-
enzyme is active between pH 8-13; in Tris-HCl buffer
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
40 - 60
-
immobilized enzyme yields maximal activity at 40°C which is maintained up to 60°C, whereas the activity of the soluble enzyme decreases sharply above 40°C
50
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 42
-
4°C: activity is undetectable, 25-37°C: maximal activity, 42°C: 12% of maximal activity
30 - 50
-
30°C: about 40% of maximal activity, 50°C: about 90% of maximal activity
37 - 60
-
enzyme is active between 37°C - 60°C; in the presence of 0.2 mM dithiothreitol
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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
-
unlike all vertebrate CSAS that localize to the nucleus, the DmCSAS is localized to the Golgi compartment
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
-
; a small, but significant population of the mouse CMP-sialic acid synthetase is also present in cytoplasm
brenda
-
mostly localized in nucleus; 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
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
CMP-sialic acid synthetase is a key enzyme in the biosynthesis of the capsular polysaccharides required for bacterial infection
Show AA Sequence and Transmembrane Helices (1069 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25440
-
2 * 25440, dimer or larger oligomer, electrospray mass spectrometry
43000
48200
or pentamer, 4 * 48200, calculated; or tetramer, 5 * 48200, calculated
56600
-
dimer, N-terminal domain of CMP-sialic acid synthetase, determined by gel filtration
69000
-
SDS-PAGE, recombinant thioredoxin fusion protein; x * 69000, SDS-PAGE
87000
-
tetramer, C-terminal domain of CMP-sialic acid synthetase, determined by gel filtration
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
tetramer
trimer
?
-
x * 24892, calculation from nucleotide sequence; x * 24893, mass spectrometry
dimer
-
2 * 25440, dimer or larger oligomer, electrospray mass spectrometry; 2 * 25600, dimer or larger oligomer, SDS-PAGE
dimer
-
2 * 25440, dimer or larger oligomer, electrospray mass spectrometry; 2 * 25600, dimer or larger oligomer, SDS-PAGE
-
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the structure of the C-terminal domain of CMP-sialic acid synthetase is solved to 1.9 A resolution
-
modeling of the closed conformation. Enzyme forms a dimer complex. Amino acids involved in the Neu5Ac binding pocket are Glu162 and Arg165 from monomer B and Gln104, Ser82, Val86, Tyr179, and Phe192 from monomer A
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
D209A
-
almost complete loss of activity. Residue involved in metal binding
K142A
-
10000fold reduction in kcat with an insignificant, fourfold, rise in Km for CTP; dramatic loss of activity. Residue involved in metal binding
N175A
-
16fold increases in the Km value for CTP and 23fold 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
additional information
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; 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; 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 1–229. The C-terminal half consisting of amino acids 228–418 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 1–229. The C-terminal half consisting of amino acids 228–418 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; 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
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
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 12.5
-
activity is drastically reduced below pH 7.0 and above pH 12.5
690583
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
37
37 - 70
-
complete loss of activity above 70°C, no loss of activity after 24 h incubation at 37°C and 50°C
40
40 - 45
-
the enzyme loses complete activity after 50 and 10 min when stored at 40°C and 45°C, respectively
45
25
enzyme is more stable at lower temperatures, 55% of enzyme activity remains after 24 h incubation at 25°C
37
enzyme is not stable at 37°C, incubation for 1 h decreases enzyme activity by 50%, incubation for 24 h at 37°C completely inactivates enzyme activity
37
-
reaction rate is proportional to enzyme concentration and constant for at least 45 min. At high enzyme concentrations the reaction rate decreases 10-15% between 45 and 60 min
40
-
50 min, complete inactivation without stabilizer, completely stable in presence of 1.0 M NaCl, 0.5 M Na2HPO4 or 25% v/v glycerol
45
-
60 min, 65% loss of activity, less than 10% loss of activity in presence of 20% w/v glycerol
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
not stable to freezing and thawing, addition of substrates partially stabilizes the purified enzyme to freezing and thawing
-
stabilized against thermal inactivation by some salts, NaCl, Na2SO4 or Na2HPO4, or by glycerol
-
stable in the frozen state, each cycle of freezing and thawing leads to a 15% decrease in activity
-
the enzyme is equally stable with or without the presence of glycerol at different temperatures
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C or -80°C, the relatively crude preparation is stable to storage as a 50% glycerol solution for at least several months
-
-20°C, partially purified enzyme can be stored in 43% glycerol or in 50 mM Tris/HCl or potassium phosphate, pH 7.5, for several months without loss of activity
-
-20°C, stable for at least 1 year
4°C, 7 months, a magnetic nanoparticle-CSS preparation retains almost 100% activity
-
4°C, the relatively crude preparation is stable to storage as a 65% ammonium sulfate suspension or 20% glycerol solution for at least several months
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by column chromatography on Sephacryl S-200 (gel filtration), Yellow-86-Agarose (affinity) and Phenyl-Sepharose (hydrophobic affinity)
-
C-His6-tagged CSS is purified using a nickel-nitrilotriacetic acid-agarose (Ni2+-NTA-agarose) affinity column
partial
recombinant proteins are expressed in Escherichia coli BL21DE3 cells and purified by affinity chromatography utilizing the StrepII-Tag, further purified on a Superdex 200 HR 10/30 columnn
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
a series of deletions from the 3'-end of the CMP-NeuAc synthetase coding region is constructed and expressed in Escherichia coli
-
cloned in Escherichia coli XL-10; expressed in Escherichia coli strain BL21
-
cloning is achieved by complementation of the Chineses hamster ovary lec32 mutation that causes a deficiency in CMP-N-acetylneuraminate synthetase activity, it also causes polysialic acid to be expressed in the capsule of the CMP-Neu5Ac synthetase negative Escherichia coli mutant EV5; expression in CHO cells or Escherichia coli
-
DmCSAS is cloned into the baculovirus vector pBlueBac4.5 (pBlueBac-DmCSAS4) which is used to transfect LEC29.Lec32 cells
-
expressed in CHO cells, HeLa cells, and NIH-3T3 cells; expression in CHO cells
-
expression in Escherichia coli
expression in Escherichia coli, enzyme can function in K1 capsular polysaccharide biosynthesis in Escherichia coli
-
human CMP-N-acetylneuraminic acid synthetase is expressed in tobacco BY2 suspension-cultured cells, enzyme is demonstrated to be active
-
the enzyme is subcloned for overexpression in Escherichia coli K12 using the expression vector pKK233-3
-
the gene is cloned into a T7 expression vector, the protein is expressed in Escherichia coli
-
the N-terminal domain, residues 39-267, and the C-terminal domain, residues 267-432, of CMP-sialic acid synthetase, and CMP-sialic acid synthetase, residues 39-432, are cloned into a pET22b-Strep vector
-
transfection of NIH-3T3 and EPC cells; transfection of NIH-3T3 and EPC cells
transformation of the CMP-NeuNAc defective Escherichia coli K1 strain EV5 with CMP-NeuNAc synthetase from Neisseria meningitidis can complement the defect in Escherichia coli
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
-
this approach enables plant cells to produce glycoproteins with mammalian-type N-glycans
medicine
-
the enzyme is involved in the production of activated sialic acids. Sialic acids are virulence factors in a variety of bacterial species, e.g. Neisseria menigitidis. As such, the identification of the bacterial CMP-NeuAc synthetase active site can serve as a starting point for rational drug design strategies
synthesis
synthesis
-
since CMP-N-acylneuraminate is unstable and relatively expensive, the enzyme is valuable for the preparative enzymatic synthesis of silylated oligosaccharides
synthesis
-
the enzyme is used for preparative synthesis of CMP-N-acylneuraminate. Optimization of the culture conditions for the production of the enzyme and the detection of a colony variant of Escherichia coli K-235 that is an even better producer of the synthetase
synthesis
-
the high expressivity of the recombinant production clone, the high catalytic efficiency of the enzyme, and its broad substrate tolerance make this enzyme the preferred catalyst for the enzymatic synthesis of CMP-Neu5Ac
synthesis
-
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
synthesis
-
the enzyme is used for preparative synthesis of CMP-N-acylneuraminate. Optimization of the culture conditions for the production of the enzyme and the detection of a colony variant of Escherichia coli K-235 that is an even better producer of the synthetase
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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, Homo sapiens, Ovis aries, Sus scrofa
brenda
Kolisis, F.N.
Studies on acylneuraminate cytidylytransferase from human placenta
Arch. Int. Physiol. Biochim.
92
179-184
1984
Homo sapiens
brenda