Literature summary for 4.2.3.4 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.

Search for more literature for 4.2.3.4

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Aspergillus nidulans

KM Value [mM]

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

Organism

Organism	UniProt	Comment	Textmining
Aspergillus nidulans	-	-	-

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Synonyms

Synonyms	Comment	Organism
dehydroquinate synthase	-	Aspergillus nidulans

Turnover Number [1/s]

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

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Release 2023.1 (January 2023)