title: Molecular details of urease inhibition by boric acid: insights into the catalytic mechanism.
abstract: The structure of the complex of urease, a Ni-containing metalloenzyme, with boric acid was determined at 2.10 A resolution. The complex shows the unprecedented binding mode of the competitive inhibitor to the dinuclear metal center, with the B(OH)3 molecule bridging the Ni ions and leaving in place the bridging hydroxide. Boric acid can be considered a substrate analogue of urea, and the structure supports the proposal that the Ni-bridging hydroxide acts as the nucleophile in the enzymatic process of urea hydrolysis.
authors.affiliation: York Structural Biology Laboratory, University of York, York, UK.
authors.forename: Stefano
authors.initials: S
authors.lastname: Benini
authors.forename: Wojciech R
authors.initials: WR
authors.lastname: Rypniewski
authors.forename: Keith S
authors.initials: KS
authors.lastname: Wilson
authors.forename: Stefano
authors.initials: S
authors.lastname: Mangani
authors.forename: Stefano
authors.initials: S
authors.lastname: Ciurli
mesh_terms: D001665:Binding Sites; D001888:Boric Acids / Q000737:chemistry / Q000494:pharmacology*; D021902:Enterobacter aerogenes / Q000201:enzymology; D004791:Enzyme Inhibitors / Q000737:chemistry / Q000494:pharmacology*; D006860:Hydrogen Bonding; D015394:Molecular Structure; D011513:Proteus mirabilis / Q000201:enzymology; D014510:Urease / Q000037:antagonists & inhibitors* / Q000737:chemistry
chemical_list: D001888:Boric Acids; D004791:Enzyme Inhibitors; D014510:Urease; C032688:boric acid