Application | Comment | Organism |
---|---|---|
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 (Comment) | Organism |
---|---|
overexpression of His-tagged DHQD from MCSG7 expression vector in Escherichia coli strain BL21(DE3) | Salmonella enterica |
Crystallization (Comment) | Organism |
---|---|
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 | Comment | Organism |
---|---|---|
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 |
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 | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
3-dehydroquinate | Salmonella enterica | - |
3-dehydroshikimate + H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
no activity in Homo sapiens | - |
- |
- |
Salmonella enterica | P58687 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged DHQD from Escherichia coli strain BL21(DE3) by nickel affinity chromatography | Salmonella enterica |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
3-dehydroquinate | - |
Salmonella enterica | 3-dehydroshikimate + H2O | - |
? | |
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 | Comment | Organism |
---|---|---|
dehydroquinate dehydratase | - |
Salmonella enterica |
DHQD | - |
Salmonella enterica |
type I dehydroquinate dehydratase | - |
Salmonella enterica |
type I DHQD | - |
Salmonella enterica |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
6.9 | - |
3-dehydroquinate | pH 8.3, temperature not specified in the publication, mutant Q236A | Salmonella enterica | |
107 | - |
3-dehydroquinate | pH 8.3, temperature not specified in the publication, mutant S232A | Salmonella enterica | |
210 | - |
3-dehydroquinate | pH 8.3, temperature not specified in the publication, wild-type enzyme | Salmonella enterica |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8.3 | - |
assay at | Salmonella enterica |