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Literature summary for 2.4.2.17 extracted from

  • Read, B.J.; Cadzow, A.F.; Alphey, M.S.; Mitchell, J.B.O.; da Silva, R.G.
    Crystal structure, steady-state, and pre-steady-state kinetics of Acinetobacter baumannii ATP phosphoribosyltransferase (2024), Biochemistry, 63, 230-240.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop vapor diffusion method, using 0.2 M sodium nitrate, 0.1 M bis-Tris propane pH 8.5, and 20% (w/v) polyethylene glycol 3350 Acinetobacter baumannii

Inhibitors

Inhibitors Comment Organism Structure
L-histidine histidine allosterically inhibits the enzyme in a negative feedback control mechanism Acinetobacter baumannii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.096
-
5-phospho-alpha-D-ribose 1-diphosphate full length enzyme, with ADP as cosubstrate, in the presence of Mg2+, at pH 7.5 and 25°C Acinetobacter baumannii
0.14
-
5-phospho-alpha-D-ribose 1-diphosphate full length enzyme, with ATP as cosubstrate, in the presence of Mg2+, at pH 7.5 and 25°C Acinetobacter baumannii
0.19
-
ATP full length enzyme, in the presence of Mg2+, at pH 7.5 and 25°C Acinetobacter baumannii
0.36
-
ADP full length enzyme, in the presence of Mg2+, at pH 7.5 and 25°C Acinetobacter baumannii
0.39
-
ATP subunit HisGs, in the presence of Mn2+, at pH 7.5 and 25°C Acinetobacter baumannii
0.44
-
5-phospho-alpha-D-ribose 1-diphosphate subunit HisGs, with ADP as cosubstrate,in the presence of Mn2+, at pH 7.5 and 25°C Acinetobacter baumannii
0.6
-
5-phospho-alpha-D-ribose 1-diphosphate subunit HisGs, with ATP as cosubstrate, in the presence of Mg2+, at pH 7.5 and 25°C Acinetobacter baumannii
0.6
-
5-phospho-alpha-D-ribose 1-diphosphate subunit HisGs, with ATP as cosubstrate, in the presence of Mn2+, at pH 7.5 and 25°C Acinetobacter baumannii
0.83
-
ATP subunit HisGs, in the presence of Mg2+, at pH 7.5 and 25°C Acinetobacter baumannii
1.2
-
5-phospho-alpha-D-ribose 1-diphosphate subunit HisGs, with ADP as cosubstrate, in the presence of Mg2+, at pH 7.5 and 25°C Acinetobacter baumannii
1.5
-
ADP subunit HisGs, in the presence of Mg2+, at pH 7.5 and 25°C Acinetobacter baumannii
2.2
-
ADP subunit HisGs, in the presence of Mn2+, at pH 7.5 and 25°C Acinetobacter baumannii

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ dependent on Acinetobacter baumannii
Mn2+ Mn2+ enhances subunit HisGS catalysis at 25°C Acinetobacter baumannii

Natural Substrates/ Products (Substrates)

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

Organism

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

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
heterooctamer the catalytic subunit, HisGs, is allosterically activated upon binding of the regulatory subunit, HisZ, to form the heterooctameric holoenzyme Acinetobacter baumannii

Synonyms

Synonyms Comment Organism
ATPPRT
-
Acinetobacter baumannii

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.384
-
ATP subunit HisGs, in the presence of Mg2+, at pH 7.5 and 25°C Acinetobacter baumannii
0.48
-
ADP subunit HisGs, in the presence of Mg2+, at pH 7.5 and 25°C Acinetobacter baumannii
0.94
-
ATP subunit HisGs, in the presence of Mn2+, at pH 7.5 and 25°C Acinetobacter baumannii
3.3
-
ADP subunit HisGs, in the presence of Mn2+, at pH 7.5 and 25°C Acinetobacter baumannii
10.8
-
ATP full length enzyme, in the presence of Mg2+, at pH 7.5 and 25°C Acinetobacter baumannii
16.6
-
ADP full length enzyme, in the presence of Mg2+, at pH 7.5 and 25°C Acinetobacter baumannii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8 9.5
-
Acinetobacter baumannii

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.32
-
ADP subunit HisGs, in the presence of Mg2+, at pH 7.5 and 25°C Acinetobacter baumannii
0.4
-
5-phospho-alpha-D-ribose 1-diphosphate subunit HisGs, with ADP as cosubstrate, in the presence of Mg2+, at pH 7.5 and 25°C Acinetobacter baumannii
0.46
-
ATP subunit HisGs, in the presence of Mg2+, at pH 7.5 and 25°C Acinetobacter baumannii
0.64
-
5-phospho-alpha-D-ribose 1-diphosphate subunit HisGs, with ATP as cosubstrate, in the presence of Mg2+, at pH 7.5 and 25°C Acinetobacter baumannii
1.5
-
ADP subunit HisGs, in the presence of Mn2+, at pH 7.5 and 25°C Acinetobacter baumannii
1.6
-
5-phospho-alpha-D-ribose 1-diphosphate subunit HisGs, with ATP as cosubstrate, in the presence of Mn2+, at pH 7.5 and 25°C Acinetobacter baumannii
2.4
-
ATP subunit HisGs, in the presence of Mn2+, at pH 7.5 and 25°C Acinetobacter baumannii
8
-
5-phospho-alpha-D-ribose 1-diphosphate subunit HisGs, with ADP as cosubstrate,in the presence of Mn2+, at pH 7.5 and 25°C Acinetobacter baumannii
46
-
ADP full length enzyme, in the presence of Mg2+, at pH 7.5 and 25°C Acinetobacter baumannii
57
-
ATP full length enzyme, in the presence of Mg2+, at pH 7.5 and 25°C Acinetobacter baumannii
77
-
5-phospho-alpha-D-ribose 1-diphosphate full length enzyme, with ATP as cosubstrate, in the presence of Mg2+, at pH 7.5 and 25°C Acinetobacter baumannii
170
-
5-phospho-alpha-D-ribose 1-diphosphate full length enzyme, with ADP as cosubstrate, in the presence of Mg2+, at pH 7.5 and 25°C Acinetobacter baumannii