Literature summary for 3.5.1.5 extracted from

Arora, R.; Issar, U.; Kakkar, R.
In silico study of the active site of Helicobacter pylori urease and its inhibition by hydroxamic acids (2018), J. Mol. Graph. Model., 83, 64-73 .

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Inhibitors

Inhibitors	Comment	Organism	Structure
hydroxamic acid	hydroxamic acids are strong inhibitors of urease due to their chelating ability. They bind the Ni(II) centers present in the active site of urease in their anionic form via the (O,O) coordination mode. The Ni(II) centers of the urease active site are electrophilic in nature. This is responsible for appreciable charge transfer from the nucleophilic oxygen centers of the hydroxamate ligand to the Ni(II) centers when they bind in the active site. Hydroxamic acids with hydrophobic groups attached to them are more potent inhibitors of urease because they can easily penetrate the hydrophobic environment surrounding the active site. The -CONHO-x01moiety of the hydroxamic acid is also found to be absolutely necessary for chelation and inhibition of urease	Helicobacter pylori

Organism

Organism	UniProt	Comment	Textmining
Helicobacter pylori	P14916	-	-
Helicobacter pylori ATCC 700392	P14916	-	-

Subunits

Subunits	Comment	Organism
dodecamer	the enzyme consists of a spherical assembly composed of four (alphabeta)3 units having three-fold symmetry. It has a dodecameric ((alphabeta)3)4 architecture	Helicobacter pylori

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Release 2023.1 (January 2023)