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Literature summary extracted from

  • Quiroga-Roger, D.; Babul, J.; Guixe, V.
    Role of monovalent and divalent metal cations in human ribokinase catalysis and regulation (2015), Biometals, 28, 401-413.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.1.15 expression in Escherichia coli Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
2.7.1.15 E202L mutation in NXXE motif, increase in the Km for MgATP of 52fold, and a decrease in the kcat value of around 200fold Homo sapiens
2.7.1.15 N199L mutation in NXXE motif, increase in the Km for MgATP- by about 68fold, a decrease in the kcat between 573- and 1036fold and almost no change in the Km for D-ribose. No substrate inhibition by D-ribose Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.1.15 ATP
-
Homo sapiens
2.7.1.15 D-ribose substrate inhibition Homo sapiens
2.7.1.15 EDTA complete inhibition Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.1.15 0.029
-
ATP wild-type, presence of Mn2+, pH 7.2, 37°C Homo sapiens
2.7.1.15 0.08
-
D-ribose mutant E202L, presence of Mg2+, pH 7.2, 37°C Homo sapiens
2.7.1.15 0.12
-
D-ribose mutant N199L, presence of Mg2+, pH 7.2, 37°C Homo sapiens
2.7.1.15 0.12
-
D-ribose wild-type, presence of Mg2+, pH 7.2, 37°C Homo sapiens
2.7.1.15 0.16
-
ATP wild-type, presence of Mg2+, pH 7.2, 37°C Homo sapiens
2.7.1.15 5.73
-
ATP mutant E202L, presence of Mg2+, pH 7.2, 37°C Homo sapiens
2.7.1.15 7.48
-
ATP mutant N199L, presence of Mg2+, pH 7.2, 37°C Homo sapiens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.1.15 Cd2+ may partly support activity Homo sapiens
2.7.1.15 Co2+ about 60% of the activity with Mn2+ Homo sapiens
2.7.1.15 Mg2+ about 70% of the activity with Mn2+ Homo sapiens
2.7.1.15 Mn2+ best activator, optimum concentration 0.1 mM Homo sapiens
2.7.1.15 Ni2+ may partly support activity Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.15 Homo sapiens Q9H477
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.15 ATP + D-ribose
-
Homo sapiens ADP + D-ribose 5-phosphate
-
?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.7.1.15 0.01
-
ATP mutant N199L, presence of Mg2+, pH 7.2, 37°C Homo sapiens
2.7.1.15 0.01
-
D-ribose mutant N199L, presence of Mg2+, pH 7.2, 37°C Homo sapiens
2.7.1.15 0.04
-
ATP mutant E202L, presence of Mg2+, pH 7.2, 37°C Homo sapiens
2.7.1.15 0.04
-
D-ribose mutant E202L, presence of Mg2+, pH 7.2, 37°C Homo sapiens
2.7.1.15 7.3
-
ATP wild-type, presence of Mn2+, pH 7.2, 37°C Homo sapiens
2.7.1.15 9.8
-
ATP wild-type, presence of Mg2+, pH 7.2, 37°C Homo sapiens
2.7.1.15 10.4
-
D-ribose wild-type, presence of Mg2+, pH 7.2, 37°C Homo sapiens

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.7.1.15 10.3
-
ATP wild-type, presence of Mn2+, pH 7.2, 37°C Homo sapiens
2.7.1.15 16.9
-
ATP wild-type, presence of Mg2+, pH 7.2, 37°C Homo sapiens

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.7.1.15 0.0013
-
ATP mutant N199L, presence of Mg2+, pH 7.2, 37°C Homo sapiens
2.7.1.15 0.007
-
ATP mutant E202L, presence of Mg2+, pH 7.2, 37°C Homo sapiens
2.7.1.15 0.08
-
D-ribose mutant N199L, presence of Mg2+, pH 7.2, 37°C Homo sapiens
2.7.1.15 0.5
-
D-ribose mutant E202L, presence of Mg2+, pH 7.2, 37°C Homo sapiens
2.7.1.15 60
-
ATP wild-type, presence of Mg2+, pH 7.2, 37°C Homo sapiens
2.7.1.15 90
-
D-ribose wild-type, presence of Mg2+, pH 7.2, 37°C Homo sapiens
2.7.1.15 250
-
ATP wild-type, presence of Mn2+, pH 7.2, 37°C Homo sapiens