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Literature summary extracted from

  • Kleanthous, C.; Deka, R.; Davis, K.; Kelly, S.M.; Cooper, A.; Harding, S.E.; Price, N.C.; Hawkins, A.R.; Coggins, J.R.
    A comparison of the enzymological and biophysical properties of two distinct classes of dehydroquinase enzymes (1992), Biochem. J., 282, 687-695.
    View publication on PubMedView publication on EuropePMC

General Stability

EC Number General Stability Organism
4.2.1.10 guanidine hydrochloride, the type II enzyme from Aspergillus nidulans unfolds at concentrations of denaturant 4fold greater than type I enzyme from E. coli and through a series of discrete transitions, while the type I enzyme from E. coli unfolds in a single transition Escherichia coli
4.2.1.10 guanidine hydrochloride, the type II enzyme from Aspergillus nidulans unfolds at concentrations of denaturant 4fold greater than type I enzyme from E. coli and through a series of discrete transitions, while the type I enzyme from E. coli unfolds in a single transition Aspergillus nidulans

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.2.1.10 diethyl dicarbonate
-
 Aspergillus nidulans
4.2.1.10 diethyl dicarbonate
-
 Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.2.1.10 0.015
-
 3-dehydroquinate
-
 Escherichia coli
4.2.1.10 0.15
-
 3-dehydroquinate
-
 Aspergillus nidulans

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.2.1.10 16505
-
 12 * 16505 Aspergillus nidulans
4.2.1.10 27466
-
 2 * 27466 Escherichia coli
4.2.1.10 44000 53000 sedimentation velocity determination and equilibrium sedimentation Escherichia coli
4.2.1.10 190000 200000 determination of sedimentation velocity and equilibrium sedimentation Aspergillus nidulans

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.2.1.10 3-dehydroquinate Aspergillus nidulans type II dehydroquinase is involved in the quinate pathway ?
-
 ?
4.2.1.10 3-dehydroquinate Escherichia coli type I dehydroquinase is involved in the biosynthetic shikimate pathway ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.10 Aspergillus nidulans
-
 type II dehydroquinase
-
4.2.1.10 Escherichia coli
-
 type I dehydroquinase
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.10 3-dehydroquinate
-
 Escherichia coli 3-dehydroshikimate + H2O
-
 ?
4.2.1.10 3-dehydroquinate
-
 Aspergillus nidulans 3-dehydroshikimate + H2O
-
 ?
4.2.1.10 3-dehydroquinate type II dehydroquinase is involved in the quinate pathway Aspergillus nidulans ?
-
 ?
4.2.1.10 3-dehydroquinate type I dehydroquinase is involved in the biosynthetic shikimate pathway Escherichia coli ?
-
 ?

Subunits

EC Number Subunits Comment Organism
4.2.1.10 dimer 2 * 27466 Escherichia coli
4.2.1.10 dodecamer 12 * 16505 Aspergillus nidulans

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
4.2.1.10 57
-
 Tm: 57°C, irreversible thermal denaturation Escherichia coli
4.2.1.10 70
-
 10 min, stable Aspergillus nidulans
4.2.1.10 70
-
 10 min, not stable Escherichia coli
4.2.1.10 82
-
 irreversible thermal denaturation involves at least three transitions. The first is a broad shoulder at approximately 82°C, the second is a shoarp doublet at 86°C and the final transition occurs at 95°C Aspergillus nidulans