1.1.1.24: quinate/shikimate dehydrogenase (NAD+)
This is an abbreviated version!
For detailed information about quinate/shikimate dehydrogenase (NAD+), go to the full flat file.
Word Map on EC 1.1.1.24
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1.1.1.24
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crassa
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neurospora
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dehydratase
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dehydroquinate
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dehydroshikimate
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qa
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nidulans
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gluconobacter
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quinoproteins
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calcoaceticus
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3-dehydroquinase
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protocatechuate
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carrot
- 1.1.1.24
- crassa
-
neurospora
- dehydratase
- dehydroquinate
- dehydroshikimate
- qa
- nidulans
- gluconobacter
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quinoproteins
- calcoaceticus
- 3-dehydroquinase
- protocatechuate
- carrot
Reaction
Synonyms
cgl0424, CglQSDH, dehydrogenase, quinate, More, NAD+-dependent QDH, NAD+-dependent quinate dehydrogenase, PoptrQDH2, QDH, QDH2, quinate 5-dehydrogenase, quinate dehydrogenase, quinate/shikimate dehydrogenase, quinate: oxidoreductase, quinate:NAD oxidoreductase, quinate:NAD+ 5-oxidoreductase, quinic dehydrogenase
ECTree
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Substrates Products
Substrates Products on EC 1.1.1.24 - quinate/shikimate dehydrogenase (NAD+)
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REACTION DIAGRAM
L-quinate + NADP+
3-dehydroquinate + NADPH + H+
low activity
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r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
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QDH plays a key role in the quinate-degradation pathway
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r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
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Thr88 and Thr221 are involved in quinate binding
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r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
the enzyme is involved in the catabolic quinate metabolism required for the degradation of lignin
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r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
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
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r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
the enzyme is involved in the catabolic quinate metabolism required for the degradation of lignin
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r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
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
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r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
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r
protocatechuic acid + H2O
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overview substrate specificity, some strains are using the substrate, some are not
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?
p-hydroxybenzoate + O2
protocatechuic acid + H2O
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overview substrate specificity, some strains are using the substrate, some are not
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?
quinate + NAD+
5-dehydroquinate + NADH + H+
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first reaction in inducible quinic acid catabolic pathway
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quinate + NAD+
5-dehydroquinate + NADH + H+
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overview substrate specificity, some strains are using the substrate, some are not
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?
shikimate + NAD+
3-dehydroshikimate + NADH + H+
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
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r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
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
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r
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addition of either shikimate or quinate to the assay does not increase the reaction rate when the other substrate is present alone
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additional information
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the enzyme is involved in the quinate and shikimate metabolism, regulation, overview
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additional information
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the bifunctional enzyme shows quinate and shikimate dehydrogenase activities
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additional information
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the bifunctional enzyme shows quinate and shikimate dehydrogenase activities, interconversion of 5-dehydroquinate and 5-dehydroshikimate by dehydroquinase, EC 4.2.1.10, favouring 5-dehydroshikimate formation
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additional information
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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
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?
additional information
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product analysis by GC-MS
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additional information
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product analysis by GC-MS
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