A new proposal for urease mechanism based on the crystal structures of the native and inhibited enzyme from Bacillus pasteurii: why urea hydrolysis costs two nickels

Benini, Stefano; Rypniewski, W.; Wilson, K.S.; Miletti, Silvia; Ciurli, Stefano; Mangani, Stefano

doi:10.1016/s0969-2126(99)80026-4

Cited by 459 publications

(593 citation statements)

References 58 publications

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“…Other enzymes, which we have not alluded to, but which have comparable binuclear metal centers, include the Ni(II)-dependent ureases, 88,[298][299][300][301] phosphotriesterases, 302,303 and aminopeptidases [304][305][306][307][308] and nucleases such as the DNA double-strand break repair enzyme Mre11 246,309 and the UDPgalactose: -galactoside-R-1,3-galactosyltransferase. 310 In addition, global efforts into the sequencing and annotation of genomes are continually revealing other novel binuclear metalloenzymes.…”

Section: Discussionmentioning

confidence: 99%

The Catalytic Mechanisms of Binuclear Metallohydrolases

et al. 2006

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Section: Discussionmentioning

confidence: 99%

The Catalytic Mechanisms of Binuclear Metallohydrolases

et al. 2006

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“…shows that the two active site nickel ions are penta-and hexacoordinate (59). Co 3ϩ ions (and low spin d6 ions in general) greatly prefer octahedral geometry.…”

Section: Figmentioning

confidence: 98%

Crystal Structures of the Liganded and Unliganded Nickel-binding Protein NikA from Escherichia coli

Heddle

Scott

Unzai

et al. 2003

Journal of Biological Chemistry

114

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Bacteria have evolved a number of tightly controlled import and export systems to maintain intracellular levels of the essential but potentially toxic metal nickel. Nickel homeostasis systems include the dedicated nickel uptake system nik found in Escherichia coli, a member of the ABC family of transporters, that involves a periplasmic nickel-binding protein, NikA. This is the initial nickel receptor and mediator of the chemotactic response away from nickel. We have solved the crystal structure of NikA protein in the presence and absence of nickel, showing that it behaves as a "classical" periplasmic binding protein. In contrast to other binding proteins, however, the ligand remains accessible to the solvent and is not completely enclosed. No direct bonds are formed between the metal cation and the protein. The nickel binding site is apolar, quite unlike any previously characterized protein nickel binding site. Despite relatively weak binding, NikA is specific for nickel. Using isothermal titration calorimetry, the dissociation constant for nickel was found to be ϳ10 M and that for cobalt was approximately 20 times higher.

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“…According to B. Pasteurii, diamidophosphate inhibition involves inhibitor oxygen binding to nickel-1 and amide coordinates to nickel-2 mimicking the substrate bounded structure [6,7]. Several classes of compounds have been reported as the agents having anti-urease activity; among them hydroxamicacids are the best recognized urease inhibitors (8)(9)(10).…”

Section: Introductionmentioning

confidence: 99%

Benzamide Derivatives as Potential Candidates for Anti-Alzheimer, Anti-Fatigue, Anti-Urease and Anti-Oxidant Activity

Taj

Tirmizi

Raheel

et al. 2017

J. Chil. Chem. Soc.

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Benzamide derivatives were screened for their anti-alzheimer, anti-fatigue, anti-urease and anti-oxidant activity and their results were calculated in the form of %age inhibition and IC 50 value. Compounds 3a and 3g exhibited the highest anti alzheimer activity. Group of mice's treated by compounds 3f and 3g showed significantly longer swimming times than those of the treated with caffeine. The prominent urease inhibitory activity was shown by only one compound among seven benzamide derivatives. Controlled experiments suggest that benzamide derivatives (3a-3g) can be serve as the therapeutic agents

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A new proposal for urease mechanism based on the crystal structures of the native and inhibited enzyme from Bacillus pasteurii: why urea hydrolysis costs two nickels

Abstract: The mode of binding of the inhibitor, and a comparison between the native and inhibited urease structures, indicate a novel mechanism for enzymatic urea hydrolysis which reconciles the available structural and biochemical data.

Cited by 459 publications

References 58 publications

The Catalytic Mechanisms of Binuclear Metallohydrolases

The Catalytic Mechanisms of Binuclear Metallohydrolases

Crystal Structures of the Liganded and Unliganded Nickel-binding Protein NikA from Escherichia coli

Benzamide Derivatives as Potential Candidates for Anti-Alzheimer, Anti-Fatigue, Anti-Urease and Anti-Oxidant Activity

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