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Literature summary extracted from

  • Li, J.; Wu, G.; Fu, Q.; Ge, H.; Liu, S.; Li, X.; Cheng, B.
    Exploring the influence of conserved lysine69 on the catalytic activity of the Helicobacter pylori shikimate dehydrogenase a combined QM/MM and MD simulations (2019), Comput. Biol. Chem., 83, 107098 .
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.25 K69A site-directed mutagenesis, the mutant shows significantly reduced the catalytic efficiency compared to wild-type enzyme Helicobacter pylori

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.25 shikimate + NADP+ Helicobacter pylori
-
3-dehydroshikimate + NADPH + H+
-
r

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.25 Helicobacter pylori
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.25 shikimate + NADP+
-
Helicobacter pylori 3-dehydroshikimate + NADPH + H+
-
r

Synonyms

EC Number Synonyms Comment Organism
1.1.1.25 SDH
-
Helicobacter pylori

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.25 NADP+
-
Helicobacter pylori
1.1.1.25 NADPH
-
Helicobacter pylori

General Information

EC Number General Information Comment Organism
1.1.1.25 malfunction mutation of Lys69 to alanine significantly reduces the catalytic efficiency of Helicobacter pylori SDH. Mutation of Lys69 triggers the movement of shikimate away from the active site of SDH, thereby disrupting the catalytic activity Helicobacter pylori
1.1.1.25 additional information the conserved Lys69 plays an important role in the catalytic activity of Helicobacter pylori SDH, structure-function analysis using the structure of SDH in complex with shikimate and NADP+ (PDB ID 3PHI). Two-layered ONIOM-based quantum mechanics/molecular mechanics (QM/MM) calculation and molecular dynamics (MD) simulations are performed to explore the role of Lys69 in SDH activity, overview. In addition to act as a catalytic base, the conserved Lys69 plays an additional, important role in the maintenance of the substrate shikimate in the active site, facilitating the catalytic reaction between the cofactor NADP+ and shikimate. Shikimate forms hydrogen bonds with Ser16, Ser18, and Tyr210. The C3-hydroxyl group of shikimate is hydrogen bonded to the side chain amide group of Gln237. The C4-hydroxyl group of shikimate donates hydrogen bonds with both the side chain amide group of Asn90 and the carboxylate group of Asp105. The C5-hydroxyl group of shikimate makes hydrogen bonds with the side chain hydroxyl group of Thr65 and the side chain ammonium group of Lys69. Comparison of active site structures of wild-type and mutant K69A enzymes Helicobacter pylori
1.1.1.25 physiological function shikimate dehydrogenase (SDH) catalyzes the reversible, NADPH-dependent reduction of 3-dehydroshikimate to shikimate, involved in the shikimate pathway Helicobacter pylori