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Fig. 4 | BMC Systems Biology

Fig. 4

From: Investigation and identification of functional post-translational modification sites associated with drug binding and protein-protein interactions

Fig. 4

A case study of the Lys217 carboxylation site associated with drug binding on urease subunit alpha (URE1). Urease is responsible for hydrolyzing urea into carbon dioxide and ammonia. The active site of all known ureases is composed of a bis-μ-hydroxo dimeric nickel center, located in the alpha (α)-subunit, and has an interatomic distance of ~3.5 Å. Our analysis shows that acetohydroxamic acid might inhibit urease activity by competing with nickel atoms in the enzyme to form a chelate. This could potentially interrupt the hydrolysis (Lys217 carboxylation) of urea, which reduces the concentration of urinary ammonia and lowers urine pH

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BMC Systems Biology

ISSN: 1752-0509

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