Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 4.2.3.4 extracted from

  • Hasan, N.; Nester, E.W.
    Dehydroquinate synthase in Bacillus subtilis. An enzyme associated with chorismate synthase and flavin reductase (1978), J. Biol. Chem., 253, 4999-5004.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
Cd2+
-
Bacillus subtilis
Cu2+
-
Bacillus subtilis
EDTA
-
Bacillus subtilis
NADH
-
Bacillus subtilis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.033 0.055 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate
-
Bacillus subtilis
0.055
-
NAD+ cofactor NAD+ Bacillus subtilis

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+
-
Bacillus subtilis
Mn2+
-
Bacillus subtilis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
24000
-
enzyme complex with chorismate synthase, SDS-PAGE Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
together with chorismate synthase Bacillus subtilis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
14.6
-
-
Bacillus subtilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate
-
Bacillus subtilis 3-dehydroquinate + phosphate
-
?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
-20
-
inactivation Bacillus subtilis
4
-
48 h, 65% activity Bacillus subtilis
55
-
inactivation Bacillus subtilis

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Bacillus subtilis