1.1.1.282: quinate/shikimate dehydrogenase [NAD(P)+]
This is an abbreviated version!
For detailed information about quinate/shikimate dehydrogenase [NAD(P)+], go to the full flat file.
Word Map on EC 1.1.1.282
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1.1.1.282
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3-dehydroquinate
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lignin
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corynebacterium
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nad+-dependent
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glutamicum
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cosubstrate
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drug development
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dehydrogenases
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agriculture
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synthesis
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medicine
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pharmacology
- 1.1.1.282
- 3-dehydroquinate
- lignin
-
corynebacterium
-
nad+-dependent
- glutamicum
-
cosubstrate
- drug development
- dehydrogenases
- agriculture
- synthesis
- medicine
- pharmacology
Reaction
Synonyms
cgl0424, cgR_0495, dehydroquinate dehydratase-shikimate dehydrogenase, More, NAD+ cofactor-specific QDH, NAD+-dependent enzyme quinate/shikimate dehydrogenase, NADP+ cofactor-specific QDH, NADP+-specific DHQD-QDH, PintaQDH, Poptr2, Poptr3, Poptr4, QDH, QSDH, qsuD, quinate dehydrogenase, quinate/shikimate 5-dehydrogenase, quinate/shikimate dehydrogenase, rifI, RifI2, SDH, SDH/QDH, sdhL, shikimate/quinate dehydrogenase, YdiB
ECTree
1.1.1.282 quinate/shikimate dehydrogenase [NAD(P)+]Advanced search results
results (
results (Engineering
Engineering on EC 1.1.1.282 - quinate/shikimate dehydrogenase [NAD(P)+]
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
S67A
site-directed mutagenesis, increased activity compared to wild type enzyme
N193Q
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
N193S
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
N193Q
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
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N193S
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
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additional information
additional information
construction of a gene qsuD deletion mutant. Cell cultures of the qsuD-deficient strain in glucose-containing medium are light yellow, whereas those of the wild-type in shikimate or quinate-containing medium are brown
additional information
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construction of a gene qsuD deletion mutant. Cell cultures of the qsuD-deficient strain in glucose-containing medium are light yellow, whereas those of the wild-type in shikimate or quinate-containing medium are brown
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additional information
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construction of an enzyme ydiB- knockout mutant JM101 strain. Fermentation processes for the production of shikimate in overproducing strains of Escherichia coli result in the simultaneous synthesis of quinic acid and 3-dehydroshikimic acid. The production of high amounts of these byproducts significantly reduces the yield of shikimate, and more importantly, the presence of quinate impairs the efficiency of shikimate extraction from supernatant cultures, reducing its purity and increasing downstream processing costs. The inactivation of the ydiB gene increases the molar proportion of shikimate and 3-dehydroshikimate with respect to quinate, showing a molar ratio of 0.81/0.05/0.14 (mol/mol/mol) of shikimate/quinate/3-dehydroshikimate. In this derivative strain, quinate production is 6.17% relative to shikimate (mol/mol), indicating that the inactivation of ydiB is a suitable strategy to reduce quinate production below 10% (mol/mol) relative to ahkimate in culture fermentations for shikimate production
additional information
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ydiB-encoded enzyme knockout in Escherichia coli strain PB12
additional information
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construction of an enzyme ydiB- knockout mutant JM101 strain. Fermentation processes for the production of shikimate in overproducing strains of Escherichia coli result in the simultaneous synthesis of quinic acid and 3-dehydroshikimic acid. The production of high amounts of these byproducts significantly reduces the yield of shikimate, and more importantly, the presence of quinate impairs the efficiency of shikimate extraction from supernatant cultures, reducing its purity and increasing downstream processing costs. The inactivation of the ydiB gene increases the molar proportion of shikimate and 3-dehydroshikimate with respect to quinate, showing a molar ratio of 0.81/0.05/0.14 (mol/mol/mol) of shikimate/quinate/3-dehydroshikimate. In this derivative strain, quinate production is 6.17% relative to shikimate (mol/mol), indicating that the inactivation of ydiB is a suitable strategy to reduce quinate production below 10% (mol/mol) relative to ahkimate in culture fermentations for shikimate production
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additional information
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ydiB-encoded enzyme knockout in Escherichia coli strain PB12
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