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Literature summary for 2.7.7.43 extracted from

  • Karwaski, M.F.; Wakarchuk, W.W.; Gilbert, M.
    High-level expression of recombinant Neisseria CMP-sialic acid synthetase in Escherichia coli (2002), Protein Expr. Purif., 25, 237-240.
    View publication on PubMed
Search for more literature for 2.7.7.43

Application

Application Comment Organism
synthesis since CMP-N-acylneuraminate is unstable and relatively expensive, the enzyme is valuable for the preparative enzymatic synthesis of silylated oligosaccharides Neisseria meningitidis

Cloned(Commentary)

Cloned (Comment) Organism
high-level expression in Escherichia coli Neisseria meningitidis

Localization

Localization Comment Organism GeneOntology No. Textmining
soluble
-
 Neisseria meningitidis
-
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
24892
-
 x * 24892, calculation from nucleotide sequence Neisseria meningitidis
24893
-
 x * 24893, mass spectrometry Neisseria meningitidis

Organism

Organism UniProt Comment Textmining
Neisseria meningitidis P0A0Z8 406Y
-
Neisseria meningitidis 406Y P0A0Z8 406Y
-

Purification (Commentary)

Purification (Comment) Organism
-
 Neisseria meningitidis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
CTP + N-acylneuraminate
-
 Neisseria meningitidis diphosphate + CMP-N-acylneuraminate
-
 ?
CTP + N-acylneuraminate
-
 Neisseria meningitidis 406Y diphosphate + CMP-N-acylneuraminate
-
 ?

Subunits

Subunits Comment Organism
? x * 24892, calculation from nucleotide sequence Neisseria meningitidis
? x * 24893, mass spectrometry Neisseria meningitidis