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Literature summary extracted from

  • Shen, R.; Olcott, M.C.; Kim, J.; Rajagopal, I.; Mathews, C.K.
    Escherichia coli nucleoside diphosphate kinase interactions with T4 phage proteins of deoxyribonucleotide synthesis and possible regulatory functions (2004), J. Biol. Chem., 279, 32225-32232.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.4.6 expressed in Escherichia coli Tuner(DE3)pLysS Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.2.8 additional information Escherichia coli direct interaction between NDP kinase and dCMP hydroxymethylase ?
-
 ?
2.7.4.6 ATP + NDP Escherichia coli contributes to the maintenance of the cellular pools of all nucleosides triphosphates, enzyme is able to specifically interact with proteins encoded by the bacteriophage T4 ADP + NTP
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.1.2.8 Escherichia coli
-
-
-
2.7.4.6 Escherichia coli
-
 wild type and enzyme deficient strains
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.4.6 recombinant protein Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.2.8 additional information direct interaction between NDP kinase and dCMP hydroxymethylase Escherichia coli ?
-
 ?
2.7.4.6 ATP + NDP
-
 Escherichia coli ADP + NTP
-
 ?
2.7.4.6 ATP + NDP contributes to the maintenance of the cellular pools of all nucleosides triphosphates, enzyme is able to specifically interact with proteins encoded by the bacteriophage T4 Escherichia coli ADP + NTP
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.1.2.8 dCMP hydroxymethylase
-
 Escherichia coli
2.7.4.6 More enzyme is able to specifically interact with proteins encoded by the bacteriophage T4 Escherichia coli