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Literature summary extracted from

  • Ogbunude, P.O.; Lamour, N.; Barrett, M.P.
    Molecular cloning, expression and characterization of ribokinase of Leishmania major (2007), Acta Biochim. Biophys. Sin., 39, 462-466.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.1.15 overexpression in Escherichia coli Leishmania major

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.1.15 D-arabinose
-
Leishmania major
2.7.1.15 D-erythrose
-
Leishmania major
2.7.1.15 D-fructose
-
Leishmania major
2.7.1.15 D-glucose
-
Leishmania major
2.7.1.15 D-ribose 5-phosphate inhibits the phosphorylation of D-ribose Leishmania major
2.7.1.15 D-ribulose
-
Leishmania major
2.7.1.15 D-threose
-
Leishmania major
2.7.1.15 D-xylulose
-
Leishmania major

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.1.15 0.2
-
ATP
-
Leishmania major
2.7.1.15 0.3
-
D-ribose
-
Leishmania major

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.15 Leishmania major
-
-
-

Storage Stability

EC Number Storage Stability Organism
2.7.1.15 -70°C, in buffer/glycerol (1/1), the recombinant enzyme retains more than 50% of its activity after 1 year Leishmania major

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.15 ATP + D-ribose
-
Leishmania major 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 10.2
-
ATP 22°C, pH 8.5 Leishmania major

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.7.1.15 0.4
-
D-ribose 5-phosphate 22°C, pH 8.5 Leishmania major