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Literature summary for 2.4.2.17 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

Activating Compound Comment Organism Structure
KCl dependent on Acinetobacter baumannii

Cloned(Commentary)

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

Protein Variants

Protein Variants Comment Organism
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]

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

Metals/Ions

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

Natural Substrates/ Products (Substrates)

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

Organism

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

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
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]

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

kcat/KM [mM/s]

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