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Literature summary extracted from

  • Read, B.J.; Mitchell, J.B.O.; da Silva, R.G.
    Allosteric activation unveils protein-mass modulation of ATP phosphoribosyltransferase product release (2024), Commun. Chem., 7, 77.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.4.2.17 KCl dependent on Acinetobacter baumannii

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.2.17 expressed in Escherichia coli BL21(DE3) cells Acinetobacter baumannii

Protein Variants

EC Number Protein Variants Comment Organism
2.4.2.17 R70A the mutation causes an about 5fold decrease in kcat compared to the wild type enzyme and nullifies the higher enzyme kcat with ADP as substrate observed with the wild type variant at 25°C Acinetobacter baumannii

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.4.2.17 0.111
-
 1-(5-phospho-beta-D-ribosyl)-ATP at pH 8.5 and 5°C Acinetobacter baumannii
2.4.2.17 0.23
-
 ATP at pH 8.5 and 5°C Acinetobacter baumannii

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.4.2.17 Mg2+ dependent on Acinetobacter baumannii
2.4.2.17 Mn2+ kcat is enhanced when Mn2+ replaces Mg2+ as the divalent metal Acinetobacter baumannii

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.4.2.17 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate Acinetobacter baumannii
-
 ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
 r
2.4.2.17 ATP + 5-phospho-alpha-D-ribose 1-diphosphate Acinetobacter baumannii
-
 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
-
 r

Organism

EC Number Organism UniProt Comment Textmining
2.4.2.17 Acinetobacter baumannii A0A7U3XWM9 AND B2HWK9 subunits HisG and HisZ
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.2.17 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
-
 Acinetobacter baumannii ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
 r
2.4.2.17 ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
 Acinetobacter baumannii 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
-
 r

Synonyms

EC Number Synonyms Comment Organism
2.4.2.17 ATPPRT the enzyme is a multi-protein complex where the regulatory protein HisZ allosterically enhances catalysis by the catalytic protein HisGS Acinetobacter baumannii

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.4.2.17 2.95
-
 1-(5-phospho-beta-D-ribosyl)-ATP at pH 8.5 and 5°C Acinetobacter baumannii
2.4.2.17 2.95
-
 ATP at pH 8.5 and 5°C Acinetobacter baumannii

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.4.2.17 13
-
 ATP at pH 8.5 and 5°C Acinetobacter baumannii
2.4.2.17 27
-
 1-(5-phospho-beta-D-ribosyl)-ATP at pH 8.5 and 5°C Acinetobacter baumannii