4.2.1.10: 3-dehydroquinate dehydratase
This is an abbreviated version!
For detailed information about 3-dehydroquinate dehydratase, go to the full flat file.
Word Map on EC 4.2.1.10
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4.2.1.10
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quinic
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7-phosphate
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3-deoxy-d-arabino-heptulosonate
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chorismate
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pentafunctional
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dahp
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epsps
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2-deoxy-scyllo-inosose
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5-enolpyruvylshikimate
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2-deoxystreptamine-containing
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1.1.1.25
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2-deoxystreptamine
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drug development
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medicine
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analysis
- 4.2.1.10
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quinic
- 7-phosphate
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3-deoxy-d-arabino-heptulosonate
- chorismate
-
pentafunctional
- dahp
- epsps
- 2-deoxy-scyllo-inosose
-
5-enolpyruvylshikimate
-
2-deoxystreptamine-containing
-
1.1.1.25
- 2-deoxystreptamine
- drug development
- medicine
- analysis
Reaction
Synonyms
3-dehydroquinase, 3-dehydroquinate dehydratase, 3-dehydroquinate dehydratase /shikimate dehydrogenase isoform 1, 3-dehydroquinate dehydratase /shikimate dehydrogenase isoform 2, 3-dehydroquinate dehydratase/shikimate dehydrogenase, 3-DHQase, 5-dehydroquinase, 5-dehydroquinate dehydratase, 5-dehydroquinate hydro-lyase, AfDQ, aroD, AroQ, bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase, chloroplast, dehydratase, 3-dehydroquinate, dehydroquinase, dehydroquinate dehydratase, dehydroquinate dehydratase-shikimate dehydrogenase, dehydroquinate synthase, DHD/SHD, DHQ synthase, DHQ-SDH, DHQ-SDH protein, DHQ/SDH, DHQ1, DHQ2, DHQase, DHQase I, DHQase-SORase, DHQD, DHQS, DQD, EC 4.2.1.10, EcDQD/SDH1, EcDQD/SDH2, mDQD, membrane-bound 3-dehydroquinate dehydratase, More, MtDHQase, NtDHD/SHD-1, NtDHD/SHD-2, pDQD, sDQD, SVCR3, type I 3-dehydroquinate dehydratase, Type I dehydroquinase, type I dehydroquinate dehydratase, Type I DHQase, type I DHQD, type II 3-dehydroquinate dehydratase, Type II dehydroquinase, Type II DHQase
ECTree
4.2.1.10 3-dehydroquinate dehydrataseAdvanced search results
results (
results (Engineering
Engineering on EC 4.2.1.10 - 3-dehydroquinate dehydratase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D88N
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the mutant shows severely reduced activity compared to the wild type enzyme and is not active at pH 7.0 but pH 8.0
N12S
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the mutant shows severely reduced activity compared to the wild type enzyme
E86A
the mutant retains catalytic proficiency but is optimally active at more acidic conditions than the wild type enzyme (pH 5.7).The mutation reduces kcat 17fold
E86Q
the mutant retains catalytic proficiency and is optimally active at wild type conditions. The E86Q mutation rather modestly affects kcat, decreasing it by a factor of 4
K170M
Q236A
site-directed mutagenesis, substrate binding structure and kinetics compared to the wild-type enzyme, the mutant shows highly reduced catalytic activity. The loop mutant fails to induce a conformational change in Arg213
S232A
site-directed mutagenesis, substrate binding structure and kinetics compared to the wild-type enzyme, the mutant shows highly reduced catalytic activity
K170M
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site-directed mutagenesis, methionine is closest in shape to a lysine but cannot form a Schiff base, mutation of Lys170 results in a dramatic loss in reactivity. Comparison of mutant and wild-type crystal structures, the K170M substrate-bound structure reveals that His143 adopts partial occupancies of both of the conformations observed in the wild-type structures, overview
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R23A
reduced catalytic activity, replacement of Arg23 results in Tyr28 adopting an alternative conformation, more favourable than the one required for catalysis
additional information
K170M
site-directed mutagenesis, methionine is closest in shape to a lysine but cannot form a Schiff base, mutation of Lys170 results in a dramatic loss in reactivity. Comparison of mutant and wild-type crystal structures, the K170M substrate-bound structure reveals that His143 adopts partial occupancies of both of the conformations observed in the wild-type structures, overview
K170M
the mutant shows enhanced affinity towards quinate and shikimate
additional information
expression of endogenous DHD/SHD-1 is suppressed by RNAi in transgenic tobacco plants, the transgenic lines with less than 40% of wild-type activity display severe growth retardation and reduced content of aromatic amino acids and downstream products such as cholorogenic acid and lignin, but accumulation of dehydroquinate and shikimate, possibly due to existence of a parallel extra-plastidic shikimate pathway into which dehydroquinate is diverted with a second gene DHD/SHD-2 in tobacco lacking a plastidic targeting sequence, the cytosolic shikimate synthesis cannot complement loss of the plastidial pathway, phenotype, overview
additional information
expression of endogenous DHD/SHD-1 is suppressed by RNAi in transgenic tobacco plants, the transgenic lines with less than 40% of wild-type activity display severe growth retardation and reduced content of aromatic amino acids and downstream products such as cholorogenic acid and lignin, but accumulation of dehydroquinate and shikimate, possibly due to existence of a parallel extra-plastidic shikimate pathway into which dehydroquinate is diverted with a second gene DHD/SHD-2 in tobacco lacking a plastidic targeting sequence, the cytosolic shikimate synthesis cannot complement loss of the plastidial pathway, phenotype, overview
additional information
-
expression of endogenous DHD/SHD-1 is suppressed by RNAi in transgenic tobacco plants, the transgenic lines with less than 40% of wild-type activity display severe growth retardation and reduced content of aromatic amino acids and downstream products such as cholorogenic acid and lignin, but accumulation of dehydroquinate and shikimate, possibly due to existence of a parallel extra-plastidic shikimate pathway into which dehydroquinate is diverted with a second gene DHD/SHD-2 in tobacco lacking a plastidic targeting sequence, the cytosolic shikimate synthesis cannot complement loss of the plastidial pathway, phenotype, overview
