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Literature summary for 2.7.4.22 extracted from

  • Labesse, G.; Bucurenci, N.; Douguet, D.; Sakamoto, H.; Landais, S.; Gagyi, C.; Gilles, A.M.; Barzu, O.
    Comparative modelling and immunochemical reactivity of Escherichia coli UMP kinase (2002), Biochem. Biophys. Res. Commun., 294, 173-179.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Escherichia coli

Protein Variants

Protein Variants Comment Organism
D168N as stable as wild-type Escherichia coli
D174N as stable as wild-type, impairs the function of the enzyme Escherichia coli
D201N impairs the function of the enzyme Escherichia coli
D77N affects enzyme activity and especially the allosteric regulation Escherichia coli
L226Q more insoluble than wild-type, impairs the stability of the enzyme Escherichia coli
P141L affects enzyme activity and especially the allosteric regulation Escherichia coli
P141Q more soluble than wild-type Escherichia coli
R62H as stable as wild-type, affects enzyme activity and especially the allosteric regulation Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + UMP Escherichia coli
-
ADP + UDP
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A7E9
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + UMP
-
Escherichia coli ADP + UDP
-
?
ATP + UMP 30°C, pH 7.4, 2 mM MgCl2 Escherichia coli ADP + UDP
-
?

Synonyms

Synonyms Comment Organism
UMP kinase
-
Escherichia coli