Literature summary for 1.1.1.24 extracted from

Schoepe, J.; Niefind, K.; Schomburg, D.
1.6 A structure of an NAD(+)-dependent quinate dehydrogenase from Corynebacterium glutamicum (2008), Acta Crystallogr. Sect. D, 64, 803-809.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
NAD+-dependent enzyme, X-ray diffraction structure determination and anaylsis at 1.64-8.0 A resolution, molecular replacement method, modelling of the ternary complexes, overview	Corynebacterium glutamicum

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
10.2	-	L-quinate	pH 9.0, 30°C	Corynebacterium glutamicum
46.6	-	shikimate	pH 10.0, 30°C	Corynebacterium glutamicum

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
L-quinate + NAD+	Corynebacterium glutamicum	QDH plays a key role in the quinate-degradation pathway	3-dehydroquinate + NADH + H+	-	r
shikimate + NAD+	Corynebacterium glutamicum	-	3-dehydroshikimate + NADH + H+	-	r

Organism

Organism	UniProt	Comment	Textmining
Corynebacterium glutamicum	-	ORF Cgl0424	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-quinate + NAD+	QDH plays a key role in the quinate-degradation pathway	Corynebacterium glutamicum	3-dehydroquinate + NADH + H+	-	r
L-quinate + NAD+	Thr88 and Thr221 are involved in quinate binding	Corynebacterium glutamicum	3-dehydroquinate + NADH + H+	-	r
additional information	structure of the potential binding site of quinate and shikimate includign the the completely conserved residues Lys92 and Asp102, overview. The crystal structure reveals that in contrast to shikimate, quinate forms a hydrogen bond to the NAD+. In addition, the hydroxyl group of a conserved active-site threonine hydrogen binds to quinate more effectively than to shikimate. Also, the hydroxyl group of a conserved tyrosine approaches the carboxylate group of quinate more closely than it does the carboxylate group of shikimate, active site structure, overview	Corynebacterium glutamicum	?	-	?
shikimate + NAD+	-	Corynebacterium glutamicum	3-dehydroshikimate + NADH + H+	-	r

Subunits

Subunits	Comment	Organism
More	seconfdary and tertiary enzyme structures, the enzyme is composed of two alphabetaalpha domains containing two discontinuous segments, Asp22-Asn127 and Gly287-Leu302, overview	Corynebacterium glutamicum

Synonyms

Synonyms	Comment	Organism
More	the enzyme belongs to a functional class of the shikimate/quinate dehydrogenase family	Corynebacterium glutamicum
NAD+-dependent QDH	-	Corynebacterium glutamicum
NAD+-dependent quinate dehydrogenase	-	Corynebacterium glutamicum

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
30	-	assay at	Corynebacterium glutamicum

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
61.9	-	L-quinate	pH 9.0, 30°C	Corynebacterium glutamicum
85.2	-	shikimate	pH 10.0, 30°C	Corynebacterium glutamicum

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
9	-	quinate dehydrogenase activity	Corynebacterium glutamicum
10	-	shikimate dehydrogenase activity	Corynebacterium glutamicum

Cofactor

Cofactor	Comment	Organism	Structure
NAD+	dependent on, 300fold higher activity compared to NADP+	Corynebacterium glutamicum
NADH	binding site structure, overview	Corynebacterium glutamicum

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Release 2023.1 (January 2023)