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
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2-deoxystreptamine-containing
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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 (Substrates Products
Substrates Products on EC 4.2.1.10 - 3-dehydroquinate dehydratase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2R)-2-methyl-3-dehydroquinic acid
?
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compound is a reversible competive inhibitor of type 1 enzymes and a weak substrate of type 2 enzymes
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-
?
3-deoxy-D-arabino-heptulosonate 7-phosphate
3-dehydroquinate + phosphate
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-
-
-
?
3-dehydroquinate
3-dehydroshikimate + H2O
B7DR33
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-
-
?
3-dehydroquinate
3-dehydroshikimate + H2O
-
-
-
?
3-dehydroquinate
3-dehydroshikimate + H2O
-
-
-
?
3-dehydroquinate
3-dehydroshikimate + H2O
-
-
-
?
3-dehydroquinate
3-dehydroshikimate + H2O
-
-
-
-
?
3-dehydroquinate
3-dehydroshikimate + H2O
-
-
-
-
r
3-dehydroquinate
3-dehydroshikimate + H2O
-
-
?
3-dehydroquinate
3-dehydroshikimate + H2O
WP_003413001
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-
-
?
3-dehydroquinate
3-dehydroshikimate + H2O
-
-
-
?
3-dehydroquinate
3-dehydroshikimate + H2O
-
-
-
?
3-dehydroquinate
3-dehydroshikimate + H2O
-
-
-
-
?
3-dehydroquinate
3-dehydroshikimate + H2O
-
-
-
?
3-dehydroquinate
3-dehydroshikimate + H2O
-
-
-
?
3-dehydroquinate
3-dehydroshikimate + H2O
-
-
-
-
?
3-dehydroquinate
3-dehydroshikimate + H2O
-
-
-
?
3-dehydroquinate
?
-
the enzyme is involved in both the catabolism of quinate and the biosynthesis of aromatic amino acids
-
-
?
3-dehydroquinate
?
-
type II dehydroquinase is involved in the quinate pathway
-
-
?
3-dehydroquinate
?
-
type I dehydroquinase is involved in the biosynthetic shikimate pathway
-
-
?
3-dehydroquinate
?
-
the enzyme catalyzes the third of the seven step shikimate pathway
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-
?
3-dehydroquinate
?
-
the enzyme catalyzes the third of the seven step shikimate pathway
-
-
?
3-dehydroquinate
?
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the enzyme is likely to function in the shikimate pathway
-
-
?
5-dehydroquinate
?
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enzyme catalyzes the third step in the biosynthesis of chorismate
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-
?
5-dehydroquinate
?
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enzyme is involved in the biosynthesis of aromatic amino acids
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-
?
5-dehydroquinate
?
-
2 isoenzymes: the catabolic dehydroquinase is produced by the qa-2 gene and the biosynthetic dehydroquinase is produced by the constitutive aro cluster
-
-
?
additional information
?
-
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the intermediate state structures reveal a reaction state-dependent behavior of His143 in which the residue adopts a conformation proximal to the site of catalytic dehydration only when the leaving group is present. His143 is likely to assume differing catalytic roles in each of its observed conformations. One conformation of His143 positions the residue for the formation/hydrolysis of the covalent Schiff base intermediates, whereas the other conformation positions the residue for a role in the catalytic dehydration event, role of His143 in type I DHQD-catalyzed reaction, reaction mechanism, overview
-
-
?
additional information
?
-
-
the intermediate state structures reveal a reaction state-dependent behavior of His143 in which the residue adopts a conformation proximal to the site of catalytic dehydration only when the leaving group is present. His143 is likely to assume differing catalytic roles in each of its observed conformations. One conformation of His143 positions the residue for the formation/hydrolysis of the covalent Schiff base intermediates, whereas the other conformation positions the residue for a role in the catalytic dehydration event, role of His143 in type I DHQD-catalyzed reaction, reaction mechanism, overview
-
-
?
additional information
?
-
active-site binding of 3-dehydroshikimate, catalytic loop in the MtDHQase-1 structure, comparison with the incomplete structure of apo-MtDHQase, PDB code 2DHQ, overview
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-
?
additional information
?
-
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active-site binding of 3-dehydroshikimate, catalytic loop in the MtDHQase-1 structure, comparison with the incomplete structure of apo-MtDHQase, PDB code 2DHQ, overview
-
-
?
additional information
?
-
active-site binding of 3-dehydroshikimate, catalytic loop in the MtDHQase-1 structure, comparison with the incomplete structure of apo-MtDHQase, PDB code 2DHQ, overview
-
-
?
additional information
?
-
the enzyme also shows shikimate dehydrogenase activity, EC 1.1.1.25
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-
?
additional information
?
-
the enzyme also shows shikimate dehydrogenase activity, EC 1.1.1.25
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-
?
additional information
?
-
-
the enzyme also shows shikimate dehydrogenase activity, EC 1.1.1.25
-
-
?
additional information
?
-
functionality of a surface loop that closes over the active site following substrate binding, both direct and indirect mechanisms of involvement of the loop in substrate binding exist, overview. To establish a direct interaction with the substrate, closure of the loop necessitates a conformational change of a key active site arginine, which in turn positions the substrate productively. Loop closure induces a conformational change in Arg213. Specifically the side chain of Gln236, may be critical for inducing the change in the conformation of Arg213
-
-
?
additional information
?
-
-
functionality of a surface loop that closes over the active site following substrate binding, both direct and indirect mechanisms of involvement of the loop in substrate binding exist, overview. To establish a direct interaction with the substrate, closure of the loop necessitates a conformational change of a key active site arginine, which in turn positions the substrate productively. Loop closure induces a conformational change in Arg213. Specifically the side chain of Gln236, may be critical for inducing the change in the conformation of Arg213
-
-
?
additional information
?
-
the intermediate state structures reveal a reaction state-dependent behavior of His143 in which the residue adopts a conformation proximal to the site of catalytic dehydration only when the leaving group is present. His143 is likely to assume differing catalytic roles in each of its observed conformations. One conformation of His143 positions the residue for the formation/hydrolysis of the covalent Schiff base intermediates, whereas the other conformation positions the residue for a role in the catalytic dehydration event, role of His143 in type I DHQD-catalyzed reaction, reaction mechanism, overview
-
-
?
additional information
?
-
-
the intermediate state structures reveal a reaction state-dependent behavior of His143 in which the residue adopts a conformation proximal to the site of catalytic dehydration only when the leaving group is present. His143 is likely to assume differing catalytic roles in each of its observed conformations. One conformation of His143 positions the residue for the formation/hydrolysis of the covalent Schiff base intermediates, whereas the other conformation positions the residue for a role in the catalytic dehydration event, role of His143 in type I DHQD-catalyzed reaction, reaction mechanism, overview
-
-
?
additional information
?
-
the intermediate state structures reveal a reaction state-dependent behavior of His143 in which the residue adopts a conformation proximal to the site of catalytic dehydration only when the leaving group is present. His143 is likely to assume differing catalytic roles in each of its observed conformations. One conformation of His143 positions the residue for the formation/hydrolysis of the covalent Schiff base intermediates, whereas the other conformation positions the residue for a role in the catalytic dehydration event, role of His143 in type I DHQD-catalyzed reaction, reaction mechanism, overview
-
-
?
additional information
?
-
-
role in shikimate pathway for the biosynthesis of aromatic compounds
-
?
additional information
?
-
role in shikimate pathway
-
?
