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Article

Kinetic and structural characterization of urease active site variants.

Biochemistry - 25 Jul 2000

Pearson M A, Park I S, Schaller R A, Michel L O, Karplus P A, Hausinger R P

Abstract excerpt

Klebsiella aerogenes urease uses a dinuclear nickel active site to catalyze urea hydrolysis at >10(14)-fold the spontaneous rate. To better define the enzyme mechanism, we examined the kinetics and structures for a suite of site-directed variants involving four residues at the active site: His320, His219, Asp221, and Arg336. Compared to wild-type urease, the H320A, H320N, and H320Q variants exhibit similar...

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PMID: 10913264
DOI: 10.1021/bi000613o

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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