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Literature summary for 2.7.7.43 extracted from

  • Liu, G.; Jin, C.
    CMP-N-acetylneuraminic acid synthetase from Escherichia coli K1 is a bifunctional enzyme: identification of minimal catalytic domain for synthetase activity and novel functional domain for platelet-activating factor acetylhydrolase activity (2004), J. Biol. Chem., 279, 17738-17749.
    View publication on PubMed
Search for more literature for 2.7.7.43

Cloned(Commentary)

Cloned (Comment) Organism
a series of deletions from the 3'-end of the CMP-NeuAc synthetase coding region is constructed and expressed in Escherichia coli Escherichia coli

Protein Variants

Protein Variants Comment Organism
DELTA1-227 mutant enzyme shows no CMP-N-acetylneuraminic acid synthetase activity, mutant enzyme is able to hydrolyze platelet activating factor Escherichia coli
DELTA1-229 mutant enzyme shows no CMP-N-acetylneuraminic acid synthetase activity, mutant enzyme is not able to hydrolyze platelet activating factor Escherichia coli
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 Escherichia coli
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 Escherichia coli
DELTA340-418 mutant enzyme shows 65% of the wild-type activity with CTP and N-acylneuraminate as substrates, as stable as wild-type enzyme Escherichia coli
DELTA384-418 mutant enzyme shows 31% of the wild-type activity with CTP and N-acylneuraminate as substrates, as stable as wild-type enzyme Escherichia coli
DELTA396-418 mutant enzyme shows 38% of the wild-type activity with CTP and N-acylneuraminate as substrates, as stable as wild-type enzyme Escherichia coli
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 Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
CTP + N-acylneuraminate Escherichia coli CMP-NeuAc is essential for the formation of capsule polysialylate for strain K1 diphosphate + CMP-N-acylneuraminate
-
 ?
CTP + N-acylneuraminate Escherichia coli K1 CMP-NeuAc is essential for the formation of capsule polysialylate for strain K1 diphosphate + CMP-N-acylneuraminate
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
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-
-
Escherichia coli K1
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-
-

Purification (Commentary)

Purification (Comment) Organism
wild-type enzyme and mutant enzymes Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.0017
-
 mutant enzyme DELTA1-227 Escherichia coli
0.0113
-
 wild-type enzyme Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
CTP + N-acylneuraminate
-
 Escherichia coli diphosphate + CMP-N-acylneuraminate
-
 ?
CTP + N-acylneuraminate CMP-NeuAc is essential for the formation of capsule polysialylate for strain K1 Escherichia coli diphosphate + CMP-N-acylneuraminate
-
 ?
CTP + N-acylneuraminate
-
 Escherichia coli K1 diphosphate + CMP-N-acylneuraminate
-
 ?
CTP + N-acylneuraminate CMP-NeuAc is essential for the formation of capsule polysialylate for strain K1 Escherichia coli K1 diphosphate + CMP-N-acylneuraminate
-
 ?

Synonyms

Synonyms Comment Organism
CMP-N-acetylneuraminic acid synthetase
-
 Escherichia coli
CMP-NeuAc synthetase
-
 Escherichia coli