Literature summary for 4.2.1.10 extracted from

Roszak, A.W.; Robinson, D.A.; Krell, T.; Hunter, I.S.; Fredrickson, M.; Abell, C.; Coggins, J.R.; Lapthorn, A.J.
The structure and mechanism of the type II dehydroquinase from Streptomyces coelicolor (2002), Structure, 10, 493-503.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
-	Streptomyces coelicolor

Protein Variants

Protein Variants	Comment	Organism
R23A	reduced catalytic activity, replacement of Arg23 results in Tyr28 adopting an alternative conformation, more favourable than the one required for catalysis	Streptomyces coelicolor

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
additional information	Streptomyces coelicolor	role in shikimate pathway	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Streptomyces coelicolor	P15474	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
3-dehydroquinate = 3-dehydroshikimate + H2O	mechanism	Streptomyces coelicolor	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
3-dehydroquinate	-	Streptomyces coelicolor	3-dehydroshikimate + H2O	-	?
additional information	role in shikimate pathway	Streptomyces coelicolor	?	-	?

Subunits

Subunits	Comment	Organism
dodecamer	-	Streptomyces coelicolor

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Release 2023.1 (January 2023)