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Literature summary extracted from

  • Fonseca, I.O.; Silva, R.G.; Fernandes, C.L.; de Souza, O.N.; Basso, L.A.; Santos, D.S.
    Kinetic and chemical mechanisms of shikimate dehydrogenase from Mycobacterium tuberculosis (2007), Arch. Biochem. Biophys., 457, 123-133.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.25 NADP+ product inhibition, competitive versus NADPH, noncompetitive versus 3-dehydroshikimate Mycobacterium tuberculosis
1.1.1.25 shikimate product inhibition, noncompetitive versus NADPH, competitive versus 3-dehydroshikimate Mycobacterium tuberculosis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.25 0.034
-
 NADPH 25°C, pH 7.3 Mycobacterium tuberculosis
1.1.1.25 0.044
-
 3-dehydroshikimate 25°C, pH 7.3 Mycobacterium tuberculosis

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.25 Mycobacterium tuberculosis A5U5Q2
-
-
1.1.1.25 Mycobacterium tuberculosis H37Rv A5U5Q2
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.1.1.25 shikimate + NADP+ = 3-dehydroshikimate + NADPH + H+ steady-state ordered bi-bi kinetic mechanism. The hydride transferred from NADPH and protons transferred from the solvent in the catalytic cycle are not significantly rate limiting in the overall reaction. Both hydride and proton transfers are concerted, and acid/base chemistry takes place in catalysis and substrate binding Mycobacterium tuberculosis
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.25 3-dehydroshikimate + NADPH
-
 Mycobacterium tuberculosis shikimate + NADP+
-
 ?
1.1.1.25 3-dehydroshikimate + NADPH
-
 Mycobacterium tuberculosis H37Rv shikimate + NADP+
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.25 0.078
-
 3-dehydroshikimate 25°C, pH 7.3 Mycobacterium tuberculosis