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Literature summary extracted from

  • Light, S.H.; Minasov, G.; Shuvalova, L.; Peterson, S.N.; Caffrey, M.; Anderson, W.F.; Lavie, A.
    A conserved surface loop in type I dehydroquinate dehydratases positions an active site arginine and functions in substrate binding (2011), Biochemistry, 50, 2357-2363.
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
4.2.1.10 drug development the absence of DHQD in humans and its essentiality in many pathogenic bacteria make the enzyme a target for the development of nontoxic antimicrobials and design of type I DHQD inhibiting molecules Salmonella enterica

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.2.1.10 overexpression of His-tagged DHQD from MCSG7 expression vector in Escherichia coli strain BL21(DE3) Salmonella enterica

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.2.1.10 purified recombinant DHQD by sitting drop vaour diffusion method, generation of three different crystal forms, the protein solution contains 500 mM NaCl and 10 mM Tris-HCl, pH 8.3, mixing of protein and reservoir solution in a 1:1 ratio at room temperature, the reservoir solutions contain: 200 mM MgCl2 and 20% PEG 3350, or 170 mM NH4OAc, pH 4.6, 25.5% PEG 4000, and 15% glycerol, or 200 mM MgCl2, 100 mM Tris, pH 8.5, and 20% PEG 3350 for the wild-type enzyme in open or in closed conformation of for the mutant Q236A, X-ray diffraction structure determination and analysis at 1.03-1.93 A resolution. The Q236A enzyme crystallized in another crystal form that diffracts to a significantly higher resolution than any of the wild-type crystals Salmonella enterica

Protein Variants

EC Number Protein Variants Comment Organism
4.2.1.10 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 Salmonella enterica
4.2.1.10 S232A site-directed mutagenesis, substrate binding structure and kinetics compared to the wild-type enzyme, the mutant shows highly reduced catalytic activity Salmonella enterica

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.2.1.10 3-dehydroquinate Salmonella enterica
-
 3-dehydroshikimate + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.10 no activity in Homo sapiens
-
-
-
4.2.1.10 Salmonella enterica P58687
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.2.1.10 recombinant His-tagged DHQD from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Salmonella enterica

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.10 3-dehydroquinate
-
 Salmonella enterica 3-dehydroshikimate + H2O
-
 ?
4.2.1.10 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 Salmonella enterica ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.2.1.10 dehydroquinate dehydratase
-
 Salmonella enterica
4.2.1.10 DHQD
-
 Salmonella enterica
4.2.1.10 type I dehydroquinate dehydratase
-
 Salmonella enterica
4.2.1.10 type I DHQD
-
 Salmonella enterica

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.2.1.10 6.9
-
 3-dehydroquinate pH 8.3, temperature not specified in the publication, mutant Q236A Salmonella enterica
4.2.1.10 107
-
 3-dehydroquinate pH 8.3, temperature not specified in the publication, mutant S232A Salmonella enterica
4.2.1.10 210
-
 3-dehydroquinate pH 8.3, temperature not specified in the publication, wild-type enzyme Salmonella enterica

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.2.1.10 8.3
-
 assay at Salmonella enterica