Any feedback?
Information on EC 2.7.7.43 - N-acylneuraminate cytidylyltransferase and Organism(s) Mus musculus and UniProt Accession Q99KK2
for references in articles please use BRENDA:EC2.7.7.43Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.7.7.43 N-acylneuraminate cytidylyltransferaseIUBMB Comments
Acts on N-acetyl- and N-glycolyl- derivatives.
Specify your search results
Word Map
- 2.7.7.43
-
sialylation
-
sialyltransferase
- meningitidis
-
polysialic
- lipooligosaccharide
- n-acetylmannosamine
- ducreyi
-
sialoglycoconjugates
- synthesis
- kdn
- mannac
- neu5gc
- medicine
- agriculture
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
Synonyms
cmp-sialic acid synthetase, cmp-neu5ac synthetase, cmp-neuac synthetase, cmp-neunac synthetase, cmp-n-acetylneuraminic acid synthetase, nmcss, cmp-sia synthetase, dmcss, cmp-sia-syn, dmcsas, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acylneuraminate cytidyltransferase
-
-
-
-
CMP sialate pyrophosphorylase
-
-
-
-
CMP-N-acetylneuraminate synthase
-
-
-
-
CMP-N-acetylneuraminate synthetase
-
-
-
-
CMP-N-acetylneuraminic acid synthase
-
-
-
-
CMP-N-acetylneuraminic acid synthetase
-
-
-
-
CMP-NANA synthetase
-
-
-
-
CMP-Neu5Ac synthetase
CMP-NeuAc synthetase
-
-
-
-
CMP-NeuNAc synthetase
-
-
-
-
CMP-Sia synthetase
CMP-sialate synthase
-
-
-
-
CMP-sialate synthetase
-
-
-
-
CMP-sialic acid synthetase
CMP-sialic synthetase
-
-
-
-
CMPsialate pyrophosphorylase
-
-
-
-
CMPsialate synthase
-
-
-
-
CSS
cytidine 5'-monophospho-N-acetylneuraminic acid synthetase
-
-
-
-
cytidine 5'-monophosphosialic acid synthetase
-
-
-
-
cytidine 5-monophosphate N-acetylneuraminic acid synthetase
-
-
-
-
cytidine monophosphate-N-acetylneuraminic acid synthetase
-
-
-
-
cytidine monophospho-sialic acid synthetase
-
-
-
-
cytidine monophosphoacetylneuraminic synthetase
-
-
-
-
cytidine monophosphosialate pyrophosphorylase
-
-
-
-
cytidine monophosphosialate synthetase
-
-
-
-
cytidyltransferase, acylneuraminate
-
-
-
-
cytidylyltransferase, acetylneuraminate
-
-
-
-
sialate cytidylyltransferase
-
-
-
-
CMP-Neu5Ac synthetase
-
-
-
-
CMP-Sia synthetase
-
-
-
-
CMP-sialic acid synthetase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nucleotidyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
CTP:N-acylneuraminate cytidylyltransferase
Acts on N-acetyl- and N-glycolyl- derivatives.
CAS REGISTRY NUMBER
COMMENTARY
9067-82-7
-
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 + 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 + 3-deoxy-D-glycero-D-galacto-nononate
diphosphate + CMP-3-deoxy-D-glycero-D-galacto-nononate
-
reaction of EC 2.7.7.92
-
?
CTP + N-acetylneuraminic acid
diphosphate + CMP-N-acetylneuraminic acid
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
-
-
-
?
CTP + N-acylneuraminate
diphosphate + CMP-N-acylneuraminate
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
-
-
?
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
production of CMP-N-acetylneuraminate is required for the synthesis of sialylated glycoconjugates
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.043
CTP
N-terminal domain and C-terminal domain of CMP-sialic acid synthetase
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
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.87
CTP
N-terminal domain and C-terminal domain of CMP-sialic acid synthetase
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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
a small, but significant population of the mouse CMP-sialic acid synthetase is also present in cytoplasm
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
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
the enzyme is involved in the biosynthesis of sialoglycoconjugates in vertebrates, overview
physiological function
malfunction
cells lacking functional enzyme display increased viability during reovirus infection
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
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). NEUA_MOUSE
432
0
48058
Swiss-Prot
other Location (Reliability: 3)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
175800
tetramer, CMP-sialic acid synthetase, determined by gel filtration
56600
dimer, N-terminal domain of CMP-sialic acid synthetase, determined by gel filtration
87000
tetramer, C-terminal domain of CMP-sialic acid synthetase, determined by gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the structure of the C-terminal domain of CMP-sialic acid synthetase is solved to 1.9 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
additional information
additional information
by deletion mutant analysis it is demonstrated that mouse CSS contains two nuclear export signals which regulate the transport of the protein from nucleus towards cytosol
additional information
-
by deletion mutant analysis it is demonstrated that mouse CSS contains two nuclear export signals which regulate the transport of the protein from nucleus towards cytosol
additional information
the two nuclear export signals of mouse CSS are conserved among mammals and fish CSSs but they are not present in bacteria or insect CSS
additional information
-
the two nuclear export signals of mouse CSS are conserved among mammals and fish CSSs but they are not present in bacteria or insect CSS
additional information
generation of mouse embryonic stem cell (mESC) lines that lack CMP-Sia synthetase (CMAS) and thereby the ability to activate Sia to CMP-Sia, phenotype, overview. The Cmas targeting strategy uses a targeting vector with diphtheria toxin cassette (DT) to increase homologous recombination. Cmas-/- mESC accumulate intracellular Neu5Ac. alpha2,3- and alpha2,6-Sialylated N-glycans are absent in Cmas-/- mESCs
additional information
-
generation of mouse embryonic stem cell (mESC) lines that lack CMP-Sia synthetase (CMAS) and thereby the ability to activate Sia to CMP-Sia, phenotype, overview. The Cmas targeting strategy uses a targeting vector with diphtheria toxin cassette (DT) to increase homologous recombination. Cmas-/- mESC accumulate intracellular Neu5Ac. alpha2,3- and alpha2,6-Sialylated N-glycans are absent in Cmas-/- mESCs
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nakata, D.; Munster, A.K.; Gerardy-Schahn, R.; Aoki, N.; Matsuda, T.; Kitajima, K.
Molecular cloning of a unique CMP-sialic acid synthetase that effectively utilizes both deaminoneuraminic acid (KDN) and N-acetylneuraminic acid (Neu5Ac) as substrates
Glycobiology
11
685-692
2001
Oncorhynchus mykiss (Q90WG6), Oncorhynchus mykiss, Mus musculus (Q99KK2), Mus musculus
Munster, A.K.; Eckhardt, M.; Potvin, B.; Muhlenhoff, M.; Stanley, P.; Gerardy-Schahn, R.
Mammalian cytidine 5'-monophosphate N-acetylneuraminic acid synthetase: a nuclear protein with evolutionarily conserved structural motifs
Proc. Natl. Acad. Sci. USA
95
9140-9145
1998
Mus musculus (Q99KK2), Mus musculus
Fujita, A.; Sato, C.; Munster-Kuhnel, A.K.; Gerardy-Schahn, R.; Kitajima, K.
Development of a simple and efficient method for assaying cytidine monophosphate sialic acid synthetase activity using an enzymatic reduced nicotinamide adenine dinucleotide/oxidized nicotinamide adenine dinucleotide converting system
Anal. Biochem.
337
12-21
2005
Mus musculus, Oncorhynchus mykiss
Fujita, A.; Sato, C.; Kitajima, K.
Identification of the nuclear export signals that regulate the intracellular localization of the mouse CMP-sialic acid synthetase
Biochem. Biophys. Res. Commun.
355
174-180
2007
Mus musculus (Q99KK2), Mus musculus
Oschlies, M.; Dickmanns, A.; Haselhorst, T.; Schaper, W.; Stummeyer, K.; Tiralongo, J.; Weinhold, B.; Gerardy-Schahn, R.; von Itzstein, M.; Ficner, R.; Muenster-Kuehnel, A.K.
A C-terminal phosphatase module conserved in vertebrate CMP-sialic acid synthetases provides a tetramerization interface for the physiologically active enzyme
J. Mol. Biol.
393
83-97
2009
Mus musculus (Q99KK2), Mus musculus
Abeln, M.; Borst, K.M.; Cajic, S.; Thiesler, H.; Kats, E.; Albers, I.; Kuhn, M.; Kaever, V.; Rapp, E.; Muenster-Kuehnel, A.; Weinhold, B.
Sialylation is dispensable for early murine embryonic development in vitro
ChemBioChem
18
1305-1316
2017
Mus musculus (Q99KK2), Mus musculus
Di, W.; Fujita, A.; Hamaguchi, K.; Delannoy, P.; Sato, C.; Kitajima, K.
Diverse subcellular localizations of the insect CMP-sialic acid synthetases
Glycobiology
27
329-341
2017
Aedes aegypti, Aedes aegypti (Q0IG96), Tribolium castaneum, Tribolium castaneum (A0A2Z5TXA4), Mus musculus (A0A0R4J0B4), Drosophila melanogaster (Q8IQV0), Drosophila melanogaster
Urbanek, K.; Sutherland, D.M.; Orchard, R.C.; Wilen, C.B.; Knowlton, J.J.; Aravamudhan, P.; Taylor, G.M.; Virgin, H.W.; Dermody, T.S.
Cytidine monophosphate N-acetylneuraminic acid synthetase and solute carrier family 35 member A1 are required for reovirus binding and infection
J. Virol.
95
e01571-20
2020
Mus musculus (Q99KK2), Mus musculus
EXTERNAL LINKS (specific for EC-Number 2.7.7.43)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
