2.7.7.43: N-acylneuraminate cytidylyltransferase

This is an abbreviated version!
For detailed information about N-acylneuraminate cytidylyltransferase, go to the full flat file.

Reaction

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, CMP-N-acylneuraminic acid synthetase, CMP-NANA synthetase, CMP-Neu5Ac synthetase, CMP-NeuAc synthetase, CMP-NeuNAc synthetase, CMP-SA synthase, CMP-Sia synthetase, CMP-Sia-syn, CMP-sialate synthase, CMP-sialate synthetase, CMP-sialic acid synthetase, CMP-sialic acid synthetase (CSS), CMP-sialic synthetase, CMPsialate pyrophosphorylase, CMPsialate synthase, CNS, CSAS, CSS, cytidine 5'-monophosphate N-acetylneuraminic acid synthetase, 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 monophosphate sialic acid synthetase, cytidine monophosphate-N-acetylneuraminic acid synthetase, cytidine monophosphate-sialic acid synthetase, cytidine monophospho-sialic acid synthetase, cytidine monophosphoacetylneuraminic synthetase, cytidine monophosphosialate pyrophosphorylase, cytidine monophosphosialate synthetase, cytidyltransferase, acylneuraminate, cytidylyltransferase, acetylneuraminate, DmCSAS, DmCSS, hCSS, mCSS, N-Acetyl-neuraminic acid cytidylyltransferase, NmCSS, SaV CSS, sialate cytidylyltransferase, sialic acid cytidylyltransferase, TcCSS

ECTree

     2 Transferases

         2.7 Transferring phosphorus-containing groups

             2.7.7 Nucleotidyltransferases

                2.7.7.43 N-acylneuraminate cytidylyltransferase

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Results	in table
13	Activating Compound
3864	AA Sequence
8	Application
1	CAS Registry Number
35	Cloned(Commentary)
4	Crystallization (Commentary)
14	Disease/ Diagnostics
1	Expression
12	General Information
9	General Stability
10	IC50 Value
100	Inhibitors
30	kcat/KM [mM/s]
2	Ki Value [mM]
129	KM Value [mM]
30	Localization
64	Metals/Ions
43	Molecular Weight [Da]
37	Natural Substrates/ Products (Substrates)
121	Organism
7	Pathway
17	PDB ID
28	pH Optimum
12	pH Range
3	pH Stability
5	pI Value
8	Posttranslational Modification
53	Protein Variants
26	Purification (Commentary)
6	Reaction
3	Reaction Type
95	Reference
65	Source Tissue
20	Specific Activity [micromol/min/mg]
13	Storage Stability
228	Substrates and Products (Substrate)
39	Subunits
139	Synonyms
1	Systematic Name
21	Temperature Optimum [°C]
6	Temperature Range [°C]
16	Temperature Stability [°C]
44	Turnover Number [1/s]

General Information

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General Information on EC 2.7.7.43 - N-acylneuraminate cytidylyltransferase

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GENERAL INFORMATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

evolution

3 entries

malfunction

4 entries

metabolism

Mus musculus

Q99KK2

the enzyme is involved in the biosynthesis of sialoglycoconjugates in vertebrates, overview

760882

physiological function

4 entries

evolution

Aedes aegypti

Q0IG96

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

761215

evolution

Drosophila melanogaster

Q8IQV0

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

761215

evolution

Tribolium castaneum

A0A2Z5TXA4

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

761215

malfunction

Mus musculus

Q99KK2

cells lacking functional enzyme display increased viability during reovirus infection

761773

malfunction

Aedes aegypti

Q0IG96

cleavage of the N-terminal hydrophobic region of the CSSs is critical for the enzyme activity

761215

malfunction

Drosophila melanogaster

Q8IQV0

cleavage of the N-terminal hydrophobic region of the CSSs is critical for the enzyme activity

761215

malfunction

Mus musculus

Q99KK2

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

760882

physiological function

Neisseria meningitidis

-

CMP-sialic acid synthetase is a key enzyme in the biosynthesis of the capsular polysaccharides required for bacterial infection

706038

physiological function

Mus musculus

Q99KK2

CMAS activity is essential for maintaining cellular homeostasis of sialic acid biosynthesis

760882

physiological function

Mus musculus

Q99KK2

the enzyme gene is required for serotype 3 reovirus binding and infection of microglial cells

761773

physiological function

Homo sapiens

Q8NFW8

the enzyme plays an important role in triple-negative breast cancer tumor formation and invasivity

762081