Literature summary for 1.1.1.25 extracted from

Gan, J.; Wu, Y.; Prabakaran, P.; Gu, Y.; Li, Y.; Andrykovitch, M.; Liu, H.; Gong, Y.; Yan, H.; Ji, X.
Structural and biochemical analyses of shikimate dehydrogenase AroE from Aquifex aeolicus: implications for the catalytic mechanism (2007), Biochemistry, 46, 9513-9522.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli in native and His-tagged form	Aquifex aeolicus

Crystallization (Commentary)

Crystallization (Comment)	Organism
apo-enzyme and in complex with both shikimate and NADP+, which assumes the closed conformation	Aquifex aeolicus

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.0424	-	NADP+	25°C, pH 9.0	Aquifex aeolicus
0.0424	-	shikimate	25°C, pH 9.0	Aquifex aeolicus

Organism

Organism	UniProt	Comment	Textmining
Aquifex aeolicus	O67049	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
shikimate + NADP+ = 3-dehydroshikimate + NADPH + H+	the active enzyme for dehydrogenation of shikimate contains a deprotonated K70 residue, a deprotonated D106, and a protonated Y216. The hydride transfer and the deprotonation of the 3-hydroxyl group of shikimate proceed in a concerted manner. K70 functions as a general base and becomes protonated in the dehydrogenation reaction. The proton is then transferred to the bulk solvent via the short proton-conducting wire. D106 plays a critical role in the transfer of the proton to the bulk solvent	Aquifex aeolicus	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
shikimate + NADP+	-	Aquifex aeolicus	3-dehydroshikimate + NADPH + H+	-	?

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
55	-	shikimate	25°C, pH 9.0	Aquifex aeolicus

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Release 2023.1 (January 2023)