220.127.116.11 - 3-dehydroquinate dehydratase
There are no alternative names for this Enzyme
3-dehydroquinate = 3-dehydroshikimate + H2O
There are no Cofactors for this Enzyme
|AA||Uniprot||Uniprot Resid||PDB||PDB Resid|
overall reactant used, proton transfer, unimolecular elimination by the conjugate base, overall product formed, enzyme-substrate complex formation, bimolecular nucleophilic addition, intramolecular elimination, assisted tautomerisation (not keto-enol), intermediate formation, dehydration, schiff base formed, intermediate terminated, native state of enzyme regenerated, inferred reaction step, proton relay, intermediate collapse, enzyme-substrate complex cleavage
There are no kinetic parameters information for this Enzyme
- in Silico Docking and Molecular Dynamic Simulation of 3-Dehydroquinate Dehydratase from Mycobacterium Tuberculosis Through Virtual Screening and Pharmacokinetics Studies
- Functional Analysis of 3-Dehydroquinate Dehydratase/Shikimate Dehydrogenases Involved in Shikimate Pathway in Camellia sinensis.
- Development of machine learning models to predict inhibition of 3-dehydroquinate dehydratase.
- Prioritization of natural compounds against mycobacterium tuberculosis 3-dehydroquinate dehydratase: A combined in-silico and in-vitro study.
- Binding studies and structure determination of the recombinantly produced type-II 3-dehydroquinate dehydratase from Acinetobacter baumannii.
- Identification of polyketide inhibitors targeting 3-dehydroquinate dehydratase in the shikimate pathway of Enterococcus faecalis.
- Structure-based virtual screening as a tool for the identification of novel inhibitors against Mycobacterium tuberculosis 3-dehydroquinate dehydratase.
- Discovery of Potential Noncovalent Inhibitors of Dehydroquinate Dehydratase from Methicillin-Resistant Staphylococcus aureus through Computational-Driven Drug Design.
- Overexpression of a type II 3-dehydroquinate dehydratase enhances the biotransformation of quinate to 3-dehydroshikimate in Gluconobacter oxydans.
- The MADS-box protein SlTAGL1 regulates a ripening-associated SlDQD/SDH2 involved in flavonoid biosynthesis and resistance against Botrytis cinerea in post-harvest tomato fruit.
- In-silico identification of phytocompounds as inhibitors to two key enzymes of Shikimate pathway of Mycobacterium tuberculosis for discovery of new lead molecule(s) for treatment of Tuberculosis.