EC Number | Crystallization (Comment) | Organism |
---|---|---|
4.2.1.10 | molecular dynamics simulations and comparison of DHQ2 enzymes from Mycobacterium tuberculosis and Helicobacter pylori. The rate-determining step involves the formation of an enolate intermediate. The enolate and transition state of the key step is more efficiently stabilized in Mycobacterium tuberculosis DHQ2, mainly by the essential residues Tyr24 and Arg19. A water molecule, which is absent in Mycobacterium tuberculosis DHQ2 but involved in generation of the catalytic Tyr22 tyrosinate in Helicobacter pylori DHQ2, destabilizes both the transition state and the enolate intermediate | Helicobacter pylori |
4.2.1.10 | molecular dynamics simulations and comparison of DHQ2 enzymes from Mycobacterium tuberculosis and Helicobacter pylori. The rate-determining step involves the formation of an enolate intermediate. The enolate and transition state of the key step is more efficiently stabilized in Mycobacterium tuberculosis DHQ2, mainly by the essential residues Tyr24 and Arg19. A water molecule, which is absent in Mycobacterium tuberculosis DHQ2 but involved in generation of the catalytic Tyr22 tyrosinate in Helicobacter pylori DHQ2, destabilizes both the transition state and the enolate intermediate | Mycobacterium tuberculosis |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
4.2.1.10 | Helicobacter pylori | Q48255 | - |
- |
4.2.1.10 | Helicobacter pylori ATCC 700392 | Q48255 | - |
- |
4.2.1.10 | Mycobacterium tuberculosis | P9WPX7 | - |
- |
4.2.1.10 | Mycobacterium tuberculosis H37Rv | P9WPX7 | - |
- |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
4.2.1.10 | AroQ | - |
Helicobacter pylori |
4.2.1.10 | AroQ | - |
Mycobacterium tuberculosis |