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Literature summary for 4.2.3.4 extracted from

  • De Mendonca, J.; Adachi, O.; Rosado, L.; Ducati, R.; Santos, D.; Basso, L.
    Kinetic mechanism determination and analysis of metal requirement of dehydroquinate synthase from Mycobacterium tuberculosis H37Rv: An essential step in the function-based rational design of anti-TB drugs (2011), Mol. Biosyst., 7, 119-128.
    View publication on PubMed
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Inhibitors

Inhibitors Comment Organism Structure
EDTA 0.1 mM, complete loss of activity. Addition of Co2+, Zn2+ and Ca2+ leads to, respectively, full, 43% and 38% recovery of the enzyme activity Mycobacterium tuberculosis

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P9WPX9
-
-
Mycobacterium tuberculosis H37Rv P9WPX9
-
-

Reaction

Reaction Comment Organism Reaction ID
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate = 3-dehydroquinate + phosphate reaction follows a rapid-equilibrium random mechanism Mycobacterium tuberculosis
a

Cofactor

Cofactor Comment Organism Structure
NAD+ determination of constants of the cyclic reduction and oxidation of NAD+ and NADH. There is a transient increase in absorbance at 340 nm associated with NADH formation followed by its oxidation. The rates of NAD+ to NADH to NAD+ conversions are not rate limiting because they are larger than the kcat value Mycobacterium tuberculosis