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Literature summary for 1.1.1.25 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

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

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis A5U5Q2
-
-
Mycobacterium tuberculosis H37Rv A5U5Q2
-
-

Reaction

Reaction Comment Organism Reaction ID
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

Substrates and Products (Substrate)

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

Turnover Number [1/s]

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