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Literature summary for 3.5.1.5 extracted from

  • Heyl, K.A.; Fischer, A.; Goebel, U.B.; Henklein, P.; Heimesaat, M.M.; Bereswill, S.
    Inhibition of Helicobacter pylori urease activity in vivo by the synthetic nickel binding protein Hpn (2013), Eur. J. Microbiol. Immunol. (Bp.), 3, 77-80.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.5.1.5

Application

Application Comment Organism
drug development urease is considered a first line target for drug development and vaccination against Helicobacter pylori infection Helicobacter pylori

Inhibitors

Inhibitors Comment Organism Structure
Hpn protein synthesis and purifcation of the 7 kDa protein, the synthetic nickel-binding histidine-rich protein designated Hpn is capable of abrogating urease activity of live Heicobacter pylori in liquid cultures due to inhibition of nickel uptake into cells Helicobacter pylori

Metals/Ions

Metals/Ions Comment Organism Structure
Ni2+ the catalytic activity of urease is mediated by nickel ions Helicobacter pylori

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
urea + H2O Helicobacter pylori
-
 CO2 + 2 NH3
-
 ?

Organism

Organism UniProt Comment Textmining
Helicobacter pylori
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
urea + H2O
-
 Helicobacter pylori CO2 + 2 NH3
-
 ?

General Information

General Information Comment Organism
physiological function neutralization of acid by ammonia is essential for gastric Helicobacter pylori colonization Helicobacter pylori