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Literature summary for 2.7.7.43 extracted from

  • 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 (2009), J. Mol. Biol., 393, 83-97.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
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 Mus musculus

Crystallization (Commentary)

Crystallization (Comment) Organism
the structure of the C-terminal domain of CMP-sialic acid synthetase is solved to 1.9 A resolution Mus musculus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.034
-
CTP CMP-sialic acid synthetase Mus musculus
0.042
-
CTP N-terminal domain of CMP-sialic acid synthetase Mus musculus
0.043
-
CTP N-terminal domain and C-terminal domain of CMP-sialic acid synthetase Mus musculus
0.045
-
sialic acid CMP-sialic acid synthetase, substrate N-acetylneuraminic acid Mus musculus
0.063
-
sialic acid N-terminal domain and C-terminal domain of CMP-sialic acid synthetase, substrate N-acetylneuraminic acid Mus musculus
0.07
-
sialic acid N-terminal domain of CMP-sialic acid synthetase, substrate N-acetylneuraminic acid Mus musculus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
18300
-
C-terminal domain of CMP-sialic acid synthetase, calculated Mus musculus
26400
-
N-terminal domain of CMP-sialic acid synthetase, calculated Mus musculus
44400
-
CMP-sialic acid synthetase, calculated Mus musculus
56600
-
dimer, N-terminal domain of CMP-sialic acid synthetase, determined by gel filtration Mus musculus
87000
-
tetramer, C-terminal domain of CMP-sialic acid synthetase, determined by gel filtration Mus musculus
175800
-
tetramer, CMP-sialic acid synthetase, determined by gel filtration Mus musculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
CTP + sialic acid Mus musculus
-
CMP-sialic acid + diphosphate
-
?

Organism

Organism UniProt Comment Textmining
Mus musculus Q99KK2
-
-

Purification (Commentary)

Purification (Comment) Organism
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 Mus musculus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
CTP + sialic acid
-
Mus musculus CMP-sialic acid + diphosphate
-
?

Subunits

Subunits Comment Organism
tetramer dimer of dimers Mus musculus

Synonyms

Synonyms Comment Organism
CMP-sialic acid synthetase
-
Mus musculus
CSS
-
Mus musculus
cytidine monophosphate-sialic acid synthetase
-
Mus musculus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
22
-
activity assay Mus musculus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.29
-
sialic acid CMP-sialic acid synthetase, substrate N-acetylneuraminic acid Mus musculus
2.57
-
CTP CMP-sialic acid synthetase Mus musculus
3.47
-
sialic acid N-terminal domain and C-terminal domain of CMP-sialic acid synthetase, substrate N-acetylneuraminic acid Mus musculus
3.56
-
sialic acid N-terminal domain of CMP-sialic acid synthetase, substrate N-acetylneuraminic acid Mus musculus
3.87
-
CTP N-terminal domain and C-terminal domain of CMP-sialic acid synthetase Mus musculus
3.89
-
CTP N-terminal domain of CMP-sialic acid synthetase Mus musculus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
activity assay Mus musculus