Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Höppner, 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.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.24 expression in Escherichia coli Corynebacterium glutamicum

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.1.24 vapor diffusion sitting-drop method at 20°C. Atomic resolution crystal structures of the enzyme in different functional states: with bound NAD+ (binary complex) and as ternary complexes with NADH plus either shikimate or quinate Corynebacterium glutamicum
1.1.1.282 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.24 0.13
-
NAD+ 30°C, pH 7.5 Corynebacterium glutamicum
1.1.1.24 0.28
-
NAD+ 30°C, pH 9.0-9.5, cosubstrate: quinate Corynebacterium glutamicum
1.1.1.24 0.46
-
NAD+ 30°C, pH 10.0-10.5, cosubstrate: shikimate Corynebacterium glutamicum
1.1.1.24 0.87
-
NAD+ 30°C, pH 7.5 Corynebacterium glutamicum
1.1.1.24 1.6
-
L-quinate 30°C, pH 7.5 Corynebacterium glutamicum
1.1.1.24 2.4
-
L-quinate 30°C, pH 9.0-9.5 Corynebacterium glutamicum
1.1.1.24 10.2
-
shikimate 30°C, pH 7.5 Corynebacterium glutamicum
1.1.1.24 53.9
-
shikimate 30°C, pH 10.0-10.5 Corynebacterium glutamicum
1.1.1.282 0.13
-
NAD+ pH 7.5, 30°C, with quinate Corynebacterium glutamicum
1.1.1.282 0.28
-
NAD+ pH 9.0-9.5, 30°C, with quinate Corynebacterium glutamicum
1.1.1.282 0.46
-
NAD+ pH 10.0-10.5, 30°C, with shikimate Corynebacterium glutamicum
1.1.1.282 0.87
-
NAD+ pH 7.5, 30°C, with shikimate Corynebacterium glutamicum
1.1.1.282 1.56
-
L-quinate pH 7.5, 30°C, with NAD+ Corynebacterium glutamicum
1.1.1.282 2.38
-
L-quinate pH 9.0-9.5, 30°C, with NAD+ Corynebacterium glutamicum
1.1.1.282 10.16
-
shikimate pH 7.5, 30°C, with NAD+ Corynebacterium glutamicum
1.1.1.282 55.88
-
shikimate pH 10.0-10.5, 30°C, with NAD+ Corynebacterium glutamicum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.24 L-quinate + NAD+ Corynebacterium glutamicum the enzyme is involved in the catabolic quinate metabolism required for the degradation of lignin 3-dehydroquinate + NADH + H+
-
r
1.1.1.24 L-quinate + NAD+ Corynebacterium glutamicum ATCC 13032 the enzyme is involved in the catabolic quinate metabolism required for the degradation of lignin 3-dehydroquinate + NADH + H+
-
r
1.1.1.282 L-quinate + NAD+ Corynebacterium glutamicum
-
3-dehydroquinate + NADH + H+
-
?
1.1.1.282 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 ?
-
?
1.1.1.282 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 ?
-
?
1.1.1.282 shikimate + NAD+ Corynebacterium glutamicum
-
3-dehydroshikimate + NADH + H+
-
?
1.1.1.282 shikimate + NAD+ Corynebacterium glutamicum ATCC 13032
-
3-dehydroshikimate + NADH + H+
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.24 Corynebacterium glutamicum Q9X5C9
-
-
1.1.1.24 Corynebacterium glutamicum ATCC 13032 Q9X5C9
-
-
1.1.1.282 Corynebacterium glutamicum Q9X5C9
-
-
1.1.1.282 Corynebacterium glutamicum ATCC 13032 Q9X5C9
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.24
-
Corynebacterium glutamicum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.24 L-quinate + NAD+ the enzyme is involved in the catabolic quinate metabolism required for the degradation of lignin Corynebacterium glutamicum 3-dehydroquinate + NADH + H+
-
r
1.1.1.24 L-quinate + NAD+ the enzyme also shows activity with shikimate. Clear substrate preference of the enzyme for quinate compared with shikimate both at the pH optimum and in a physiological pH range. The enzyme is strictly NAD(H) dependent Corynebacterium glutamicum 3-dehydroquinate + NADH + H+
-
r
1.1.1.24 L-quinate + NAD+ the enzyme is involved in the catabolic quinate metabolism required for the degradation of lignin Corynebacterium glutamicum ATCC 13032 3-dehydroquinate + NADH + H+
-
r
1.1.1.24 L-quinate + NAD+ the enzyme also shows activity with shikimate. Clear substrate preference of the enzyme for quinate compared with shikimate both at the pH optimum and in a physiological pH range. The enzyme is strictly NAD(H) dependent Corynebacterium glutamicum ATCC 13032 3-dehydroquinate + NADH + H+
-
r
1.1.1.24 shikimate + NAD+ the enzyme also shows high activity with quinate. Clear substrate preference of the enzyme for quinate compared with shikimate both at the pH optimum and in a physiological pH range. The enzyme is strictly NAD(H) dependent Corynebacterium glutamicum 3-dehydroshikimate + NADH + H+
-
r
1.1.1.24 shikimate + NAD+ the enzyme also shows high activity with quinate. Clear substrate preference of the enzyme for quinate compared with shikimate both at the pH optimum and in a physiological pH range. The enzyme is strictly NAD(H) dependent Corynebacterium glutamicum ATCC 13032 3-dehydroshikimate + NADH + H+
-
r
1.1.1.282 L-quinate + NAD+
-
Corynebacterium glutamicum 3-dehydroquinate + NADH + H+
-
?
1.1.1.282 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 ?
-
?
1.1.1.282 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 ?
-
?
1.1.1.282 shikimate + NAD+
-
Corynebacterium glutamicum 3-dehydroshikimate + NADH + H+
-
?
1.1.1.282 shikimate + NAD+
-
Corynebacterium glutamicum ATCC 13032 3-dehydroshikimate + NADH + H+
-
?

Subunits

EC Number Subunits Comment Organism
1.1.1.282 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

EC Number Synonyms Comment Organism
1.1.1.24 cgl0424
-
Corynebacterium glutamicum
1.1.1.24 CglQSDH
-
Corynebacterium glutamicum
1.1.1.24 quinate/shikimate dehydrogenase the enzyme also shows activity with shikimate Corynebacterium glutamicum
1.1.1.282 cgl0424
-
Corynebacterium glutamicum
1.1.1.282 QSDH
-
Corynebacterium glutamicum
1.1.1.282 qsuD
-
Corynebacterium glutamicum
1.1.1.282 quinate/shikimate dehydrogenase
-
Corynebacterium glutamicum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.24 30
-
assay at Corynebacterium glutamicum
1.1.1.282 30
-
assay at Corynebacterium glutamicum

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.24 30.1
-
shikimate 30°C, pH 7.5 Corynebacterium glutamicum
1.1.1.24 43.7
-
NAD+ 30°C, pH 7.5 Corynebacterium glutamicum
1.1.1.24 50.8
-
L-quinate 30°C, pH 7.5 Corynebacterium glutamicum
1.1.1.24 61.1
-
NAD+ 30°C, pH 7.5 Corynebacterium glutamicum
1.1.1.24 104.9
-
L-quinate 30°C, pH 9.0-9.5 Corynebacterium glutamicum
1.1.1.24 205.8
-
NAD+ 30°C, pH 10.0-10.5, cosubstrate: shikimate Corynebacterium glutamicum
1.1.1.24 214.1
-
shikimate 30°C, pH 10.0-10.5 Corynebacterium glutamicum
1.1.1.24 223.1
-
NAD+ 30°C, pH 9.0-9.5, cosubstrate: quinate Corynebacterium glutamicum
1.1.1.282 30.13
-
shikimate pH 7.5, 30°C, with NAD+ Corynebacterium glutamicum
1.1.1.282 43.67
-
NAD+ pH 7.5, 30°C, with quinate Corynebacterium glutamicum
1.1.1.282 50.82
-
L-quinate pH 7.5, 30°C, with NAD+ Corynebacterium glutamicum
1.1.1.282 61.12
-
NAD+ pH 7.5, 30°C, with shikimate Corynebacterium glutamicum
1.1.1.282 104.9
-
L-quinate pH 9.0-9.5, 30°C, with NAD+ Corynebacterium glutamicum
1.1.1.282 105.8
-
NAD+ pH 10.0-10.5, 30°C, with shikimate Corynebacterium glutamicum
1.1.1.282 214.1
-
shikimate pH 10.0-10.5, 30°C, with NAD+ Corynebacterium glutamicum
1.1.1.282 223.1
-
NAD+ pH 9.0-9.5, 30°C, with quinate Corynebacterium glutamicum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.24 9 9.5 substrate: L-quinate Corynebacterium glutamicum
1.1.1.24 10 10.5 substrate: shikimate Corynebacterium glutamicum
1.1.1.282 9 9.5 quinate oxidation Corynebacterium glutamicum
1.1.1.282 10 10.5 shikimate oxidation Corynebacterium glutamicum

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.24 NAD+ strictly dependent on Corynebacterium glutamicum
1.1.1.24 NADH strictly dependent on Corynebacterium glutamicum
1.1.1.282 additional information CglQSDH is strictly NAD(H)-dependent due to structural features Corynebacterium glutamicum
1.1.1.282 NAD+
-
Corynebacterium glutamicum
1.1.1.282 NADH
-
Corynebacterium glutamicum

General Information

EC Number General Information Comment Organism
1.1.1.282 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]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.1.1.24 3.1
-
shikimate 30°C, pH 7.5 Corynebacterium glutamicum
1.1.1.24 4.2
-
shikimate 30°C, pH 10.0-10.5 Corynebacterium glutamicum
1.1.1.24 33.3
-
L-quinate 30°C, pH 7.5 Corynebacterium glutamicum
1.1.1.24 44.05
-
L-quinate 30°C, pH 9.0-9.5 Corynebacterium glutamicum
1.1.1.24 71.6
-
NAD+ 30°C, pH 7.5 Corynebacterium glutamicum
1.1.1.24 329.1
-
NAD+ 30°C, pH 7.5 Corynebacterium glutamicum
1.1.1.24 464.7
-
NAD+ 30°C, pH 10.0-10.5, cosubstrate: shikimate Corynebacterium glutamicum
1.1.1.24 826.6
-
NAD+ 30°C, pH 9.0-9.5, cosubstrate: quinate Corynebacterium glutamicum
1.1.1.282 3.1
-
shikimate pH 7.5, 30°C, with NAD+ Corynebacterium glutamicum
1.1.1.282 4.24
-
shikimate pH 10.0-10.5, 30°C, with NAD+ Corynebacterium glutamicum
1.1.1.282 33.3
-
L-quinate pH 7.5, 30°C, with NAD+ Corynebacterium glutamicum
1.1.1.282 44.05
-
L-quinate pH 9.0-9.5, 30°C, with NAD+ Corynebacterium glutamicum
1.1.1.282 71.58
-
NAD+ pH 7.5, 30°C, with shikimate Corynebacterium glutamicum
1.1.1.282 329.1
-
NAD+ pH 7.5, 30°C, with quinate Corynebacterium glutamicum
1.1.1.282 464.7
-
NAD+ pH 10.0-10.5, 30°C, with shikimate Corynebacterium glutamicum
1.1.1.282 826.6
-
NAD+ pH 9.0-9.5, 30°C, with quinate Corynebacterium glutamicum