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

BRENDA support

Literature summary for 4.2.1.10 extracted from

  • Light, S.H.; Minasov, G.; Shuvalova, L.; Duban, M.E.; Caffrey, M.; Anderson, W.F.; Lavie, A.
    Insights into the mechanism of type I dehydroquinate dehydratases from structures of reaction intermediates (2011), J. Biol. Chem., 286, 3531-3539.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.2.1.10

Crystallization (Commentary)

Crystallization (Comment) Organism
wild-type enzyme post-dehydration covalent intermediate, from 100 mM Tris, pH 8.5, 30% w/v PEG 500, X-ray diffraction structure determination and analysis at 2.20 A resolution Clostridioides difficile
wild-type enzyme pre-dehydration covalent intermediate, and mutant K170M in complex with 3-dehydroquinate, crystallization of the wild-type enzyme from 170 mM NH4OAc, pH 4.6, 25.5% w/v PEG 4000, 15% v/v glycerol, the mutant is crystallized from 50 mM K2PO4, pH 6.0, 20% w/v PEG 8000, X-ray diffraction structure determination and analysis at 1.6-1.95 A resolution Salmonella enterica

Protein Variants

Protein Variants Comment Organism
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 Salmonella enterica

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.021
-
 3-dehydroquinate wild-type enzyme, pH 7.5, 37°C Salmonella enterica
0.033
-
 3-dehydroquinate mutant K170M, pH 7.5, 37°C Salmonella enterica
0.036
-
 3-dehydroquinate wild-type enzyme, pH 7.5, 37°C Clostridioides difficile

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3-dehydroquinate Clostridioides difficile
-
 3-dehydroshikimate + H2O
-
 ?
3-dehydroquinate Salmonella enterica
-
 3-dehydroshikimate + H2O
-
 ?
3-dehydroquinate Clostridioides difficile 630
-
 3-dehydroshikimate + H2O
-
 ?
3-dehydroquinate Salmonella enterica LT2
-
 3-dehydroshikimate + H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Clostridioides difficile
-
-
-
Clostridioides difficile 630
-
-
-
Salmonella enterica P58687
-
-
Salmonella enterica LT2 P58687
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-dehydroquinate
-
 Clostridioides difficile 3-dehydroshikimate + H2O
-
 ?
3-dehydroquinate
-
 Salmonella enterica 3-dehydroshikimate + H2O
-
 ?
3-dehydroquinate
-
 Clostridioides difficile 630 3-dehydroshikimate + H2O
-
 ?
3-dehydroquinate
-
 Salmonella enterica LT2 3-dehydroshikimate + H2O
-
 ?
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 Clostridioides difficile ?
-
 ?
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 Salmonella enterica ?
-
 ?
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 Clostridioides difficile 630 ?
-
 ?
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 Salmonella enterica LT2 ?
-
 ?

Synonyms

Synonyms Comment Organism
dehydroquinate dehydratase
-
 Clostridioides difficile
dehydroquinate dehydratase
-
 Salmonella enterica
DHQD
-
 Clostridioides difficile
DHQD
-
 Salmonella enterica
type I dehydroquinate dehydratase
-
 Clostridioides difficile
type I dehydroquinate dehydratase
-
 Salmonella enterica
type I DHQD
-
 Clostridioides difficile
type I DHQD
-
 Salmonella enterica

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Clostridioides difficile
37
-
 assay at Salmonella enterica

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.015
-
 3-dehydroquinate mutant K170M, pH 7.5, 37°C Salmonella enterica
125
-
 3-dehydroquinate wild-type enzyme, pH 7.5, 37°C Clostridioides difficile
210
-
 3-dehydroquinate wild-type enzyme, pH 7.5, 37°C Salmonella enterica

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Clostridioides difficile
7.5
-
 assay at Salmonella enterica

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.00000045
-
 3-dehydroquinate mutant K170M, pH 7.5, 37°C Salmonella enterica
0.001
-
 3-dehydroquinate wild-type enzyme, pH 7.5, 37°C Salmonella enterica
0.0035
-
 3-dehydroquinate wild-type enzyme, pH 7.5, 37°C Clostridioides difficile