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Literature summary extracted from

  • Park, A.; Lamb, H.K.; Nichols, C.; Moore, J.D.; Brown, K.A.; Cooper, A.; Charles, I.G.; Stammers, D.K.; Hawkins, A.R.
    Biophysical and kinetic analysis of wild-type and site-directed mutants of the isolated and native dehydroquinate synthase domain of the AROM protein (2004), Protein Sci., 13, 2108-2119.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.2.3.4 expression in Escherichia coli Aspergillus nidulans

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.2.3.4 0.0019
-
 NAD+ cofactor NAD+ Aspergillus nidulans
4.2.3.4 0.014
-
 NAD+ mutant R130K, cofactor NAD+ Aspergillus nidulans
4.2.3.4 0.021
-
 3-deoxy-D-arabino-heptulosonate 7-phosphate
-
 Aspergillus nidulans
4.2.3.4 0.228
-
 3-deoxy-D-arabino-heptulosonate 7-phosphate mutant R130K Aspergillus nidulans

Organism

EC Number Organism UniProt Comment Textmining
4.2.3.4 Aspergillus nidulans
-
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.2.3.4 0.07
-
 mutant R130K Aspergillus nidulans
4.2.3.4 9.5
-
-
 Aspergillus nidulans

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.3.4 3-deoxy-arabino-heptulonate 7-phosphate
-
 Aspergillus nidulans 3-dehydroquinate + phosphate
-
 ?
4.2.3.4 3-deoxy-D-arabino-heptulosonate 7-phosphate
-
 Aspergillus nidulans 3-dehydroquinate + phosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.2.3.4 dehydroquinate synthase
-
 Aspergillus nidulans

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.2.3.4 6.8
-
 3-deoxy-D-arabino-heptulosonate 7-phosphate
-
 Aspergillus nidulans