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Literature summary extracted from

  • Lence, E.; van der Kamp, M.W.; Gonzalez-Bello, C.; Mulholland, A.J.
    QM/MM simulations identify the determinants of catalytic activity differences between type II dehydroquinase enzymes (2018), Org. Biomol. Chem., 16, 4443-4455 .
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

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

Organism

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
-
-

Synonyms

EC Number Synonyms Comment Organism
4.2.1.10 AroQ
-
Helicobacter pylori
4.2.1.10 AroQ
-
Mycobacterium tuberculosis