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Literature summary for 6.3.4.2 extracted from

  • Weng, M.; Zalkin, H.
    Structural role for a conserved region in the CTP synthetase glutamine amide transfer domain (1987), J. Bacteriol., 169, 3023-3028.
    View publication on PubMedView publication on EuropePMC
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Protein Variants

Protein Variants Comment Organism
G351A mutation increases lability of the enzyme, mutant enzyme is not overproduced because of apparent instability and proteolytic degradation Escherichia coli
G352C mutation increases lability of the enzyme, mutation abolishes the capacity to form the covalent glutaminyl-cysteine379 catalytic intermediate, thus preventing glutamine amide transfer function, mutant enzyme is not overproduced because of apparent instability and proteolytic degradation Escherichia coli
G352P mutation increases lability of the enzyme, mutation abolishes the capacity to form the covalent glutaminyl-cysteine379 catalytic intermediate, thus preventing glutamine amide transfer function, mutant enzyme is not overproduced because of apparent instability and proteolytic degradation Escherichia coli
V349S mutation increases lability of the enzyme Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + UTP + NH4+
-
 Escherichia coli ADP + phosphate + CTP
-
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