Literature summary for 1.1.1.282 extracted from

H�ppner, A.; Schomburg, D.; Niefind, K.
Enzyme-substrate complexes of the quinate/shikimate dehydrogenase from Corynebacterium glutamicum enable new insights in substrate and cofactor binding, specificity, and discrimination (2013), Biol. Chem., 394, 1505-1516.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
purified enzyme with bound NAD+ in a binary complex, and as ternary complexes with NADH plus either shikimate or quinate, sitting drop vapour diffusion method, for the ternary complexes: mixing of 0.002 ml of 10 mg/ml protein in 50 mM Tris-HCl, pH 7.5, 500 mM NaCl, 20% v/v glycerol, with 1 mM NAD+/NADH or additonally with 35 mM of either quinate or shikimate, with 0.002 ml of crystallization solution containing for the QSDH-NAD+ crystals 1.6 M trisodium citrate, pH 6.5-6.9, 25-62 mM CoCl2, or for crystals of the QSDH-quinate-NADH and QSDH-shikimate-NADH 24% w/v polyethylene glycol 6000, 360-400 mM CaCl2, 100 mM Tris-HCl, pH 8.0-9.5. Crystals are soaked in a cryoprotectant containing 30% w/v polyethylene glycol 6000, 25% v/v glycerol, 100 mM Tris-HCl, pH 8.5, for 1 h, X-ray diffraction structure determination and analysis at 1.0-1.6 A resolution, structure modelling	Corynebacterium glutamicum

Crystallization (Comment)

Organism

purified enzyme with bound NAD+ in a binary complex, and as ternary complexes with NADH plus either shikimate or quinate, sitting drop vapour diffusion method, for the ternary complexes: mixing of 0.002 ml of 10 mg/ml protein in 50 mM Tris-HCl, pH 7.5, 500 mM NaCl, 20% v/v glycerol, with 1 mM NAD+/NADH or additonally with 35 mM of either quinate or shikimate, with 0.002 ml of crystallization solution containing for the QSDH-NAD+ crystals 1.6 M trisodium citrate, pH 6.5-6.9, 25-62 mM CoCl2, or for crystals of the QSDH-quinate-NADH and QSDH-shikimate-NADH 24% w/v polyethylene glycol 6000, 360-400 mM CaCl2, 100 mM Tris-HCl, pH 8.0-9.5. Crystals are soaked in a cryoprotectant containing 30% w/v polyethylene glycol 6000, 25% v/v glycerol, 100 mM Tris-HCl, pH 8.5, for 1 h, X-ray diffraction structure determination and analysis at 1.0-1.6 A resolution, structure modelling

Corynebacterium glutamicum

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism
0.13	-	NAD+	pH 7.5, 30°C, with quinate	Corynebacterium glutamicum
0.28	-	NAD+	pH 9.0-9.5, 30°C, with quinate	Corynebacterium glutamicum
0.46	-	NAD+	pH 10.0-10.5, 30°C, with shikimate	Corynebacterium glutamicum
0.87	-	NAD+	pH 7.5, 30°C, with shikimate	Corynebacterium glutamicum
1.56	-	L-quinate	pH 7.5, 30°C, with NAD+	Corynebacterium glutamicum
2.38	-	L-quinate	pH 9.0-9.5, 30°C, with NAD+	Corynebacterium glutamicum
10.16	-	shikimate	pH 7.5, 30°C, with NAD+	Corynebacterium glutamicum
55.88	-	shikimate	pH 10.0-10.5, 30°C, with NAD+	Corynebacterium glutamicum

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.
L-quinate + NAD+	Corynebacterium glutamicum	-	3-dehydroquinate + NADH + H+	-	?
additional information	Corynebacterium glutamicum	the enzyme CglQSDH shows a substrate preference for quinate compared with shikimate both at the pH optimum and in a physiological pH range, which is a remarkable contrast to closely related SDH/QDH enzymes	?	-	?
additional information	Corynebacterium glutamicum ATCC 13032	the enzyme CglQSDH shows a substrate preference for quinate compared with shikimate both at the pH optimum and in a physiological pH range, which is a remarkable contrast to closely related SDH/QDH enzymes	?	-	?
shikimate + NAD+	Corynebacterium glutamicum	-	3-dehydroshikimate + NADH + H+	-	?
shikimate + NAD+	Corynebacterium glutamicum ATCC 13032	-	3-dehydroshikimate + NADH + H+	-	?

Organism

Organism	UniProt	Comment	Textmining
Corynebacterium glutamicum	Q9X5C9	-	-
Corynebacterium glutamicum ATCC 13032	Q9X5C9	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
L-quinate + NAD+	-	Corynebacterium glutamicum	3-dehydroquinate + NADH + H+	-	?
additional information	the enzyme CglQSDH shows a substrate preference for quinate compared with shikimate both at the pH optimum and in a physiological pH range, which is a remarkable contrast to closely related SDH/QDH enzymes	Corynebacterium glutamicum	?	-	?
additional information	the enzyme CglQSDH shows a substrate preference for quinate compared with shikimate both at the pH optimum and in a physiological pH range, which is a remarkable contrast to closely related SDH/QDH enzymes	Corynebacterium glutamicum ATCC 13032	?	-	?
shikimate + NAD+	-	Corynebacterium glutamicum	3-dehydroshikimate + NADH + H+	-	?
shikimate + NAD+	-	Corynebacterium glutamicum ATCC 13032	3-dehydroshikimate + NADH + H+	-	?

Subunits

Subunits	Comment	Organism
More	enzyme three-dimensional structure determination, analysis, and comparisons, overview. The N-terminal or catalytic domain comprises residues 1 to 113 and 256 to 283, whereas the C-terminal or nucleotide-binding domain is build up of residues 114 to 255. The catalytic domain forms an open alpha/beta sandwich, which is characteristic for enzymes of the SDH/QDH family. The substrate-binding site is located in the N-terminal domain, close to the nicotinamide ring of the cofactor	Corynebacterium glutamicum

Synonyms

Synonyms	Comment	Organism
cgl0424	-	Corynebacterium glutamicum
QSDH	-	Corynebacterium glutamicum
qsuD	-	Corynebacterium glutamicum
quinate/shikimate 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
30.13	-	shikimate	pH 7.5, 30°C, with NAD+	Corynebacterium glutamicum
43.67	-	NAD+	pH 7.5, 30°C, with quinate	Corynebacterium glutamicum
50.82	-	L-quinate	pH 7.5, 30°C, with NAD+	Corynebacterium glutamicum
61.12	-	NAD+	pH 7.5, 30°C, with shikimate	Corynebacterium glutamicum
104.9	-	L-quinate	pH 9.0-9.5, 30°C, with NAD+	Corynebacterium glutamicum
105.8	-	NAD+	pH 10.0-10.5, 30°C, with shikimate	Corynebacterium glutamicum
214.1	-	shikimate	pH 10.0-10.5, 30°C, with NAD+	Corynebacterium glutamicum
223.1	-	NAD+	pH 9.0-9.5, 30°C, with quinate	Corynebacterium glutamicum

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
9	9.5	quinate oxidation	Corynebacterium glutamicum
10	10.5	shikimate oxidation	Corynebacterium glutamicum

Cofactor

Cofactor	Comment	Organism
additional information	CglQSDH is strictly NAD(H)-dependent due to structural features	Corynebacterium glutamicum
NAD+	-	Corynebacterium glutamicum
NADH	-	Corynebacterium glutamicum

General Information

General Information	Comment	Organism
additional information	substrate binding site structure, overview. Quinate binding causes a slight closure of the N- and C-terminal domain of CglQSDH. Shikimate binding causes a alternative side-chain conformation of Lys73	Corynebacterium glutamicum

kcat/KM [mM/s]

kcat/KM Value [1/mMs^-1]	kcat/KM Value Maximum [1/mMs^-1]	Substrate	Comment	Organism
3.1	-	shikimate	pH 7.5, 30°C, with NAD+	Corynebacterium glutamicum
4.24	-	shikimate	pH 10.0-10.5, 30°C, with NAD+	Corynebacterium glutamicum
33.3	-	L-quinate	pH 7.5, 30°C, with NAD+	Corynebacterium glutamicum
44.05	-	L-quinate	pH 9.0-9.5, 30°C, with NAD+	Corynebacterium glutamicum
71.58	-	NAD+	pH 7.5, 30°C, with shikimate	Corynebacterium glutamicum
329.1	-	NAD+	pH 7.5, 30°C, with quinate	Corynebacterium glutamicum
464.7	-	NAD+	pH 10.0-10.5, 30°C, with shikimate	Corynebacterium glutamicum
826.6	-	NAD+	pH 9.0-9.5, 30°C, with quinate	Corynebacterium glutamicum