Soybean (Glycine max) urease: Significance of sulfhydryl groups in urea catalysis

Kumar, Sandeep; Kayastha, Arvind M.

doi:10.1016/j.plaphy.2010.05.007

Cited by 15 publications

(7 citation statements)

References 27 publications

(23 reference statements)

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“…It may be due to unblocking of eSH groups by mercaptide exchange reaction. Such studies involving the inactivation of eSH groups of enzymes by p-CMB and subsequent reversal of inactivation by the addition of cysteine has been reported earlier (Srivastava and Kayastha, 2000;Kumar and Kayastha, 2010).…”

Section: Modification Of Sulfhydryl Groupsmentioning

confidence: 82%

Identification of active site residues of Fenugreek β-amylase: Chemical modification and in silico approach

Srivastava

Singh

Kayastha

2014

Plant Physiology and Biochemistry

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Section: Modification Of Sulfhydryl Groupsmentioning

confidence: 82%

Identification of active site residues of Fenugreek β-amylase: Chemical modification and in silico approach

Srivastava

Singh

Kayastha

2014

Plant Physiology and Biochemistry

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“…The binuclear nickel ions (Ni 2+ ) in the active site and sulfhydryl groups situated in the mobile flap are essential for urease’s catalytic activity 16 , 17 . Indeed, hydroxamic acids, phosphoramidates, and urea derivatives interacting with the metallocentre 18 – 20 , and quinones and polyphenols binding to the sulfhydryl groups of the urease active site 21 , 22 , constitute the current major structural classes of urease inhibitors.…”

Section: Introductionmentioning

confidence: 99%

Coptisine-induced inhibition ofHelicobacter pylori: elucidation of specific mechanisms by probing urease active site and its maturation process

Huang

Wong

et al. 2018

Journal of Enzyme Inhibition and Medicinal Chemistry

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In this study, we examined the anti-Helicobactor pylori effects of the main protoberberine-type alkaloids in Rhizoma Coptidis. Coptisine exerted varying antibacterial and bactericidal effects against three standard H. pylori strains and eleven clinical isolates, including four drug-resistant strains, with minimum inhibitory concentrations ranging from 25 to 50 μg/mL and minimal bactericidal concentrations ranging from 37.5 to 125 μg/mL. Coptisine’s anti-H. pylori effects derived from specific inhibition of urease in vivo. In vitro, coptisine inactivated urease in a concentration-dependent manner through slow-binding inhibition and involved binding to the urease active site sulfhydryl group. Coptisine inhibition of H. pylori urease (HPU) was mixed type, while inhibition of jack bean urease was non-competitive. Importantly, coptisine also inhibited HPU by binding to its nickel metallocentre. Besides, coptisine interfered with urease maturation by inhibiting activity of prototypical urease accessory protein UreG and formation of UreG dimers and by promoting dissociation of nickel from UreG dimers. These findings demonstrate that coptisine inhibits urease activity by targeting its active site and inhibiting its maturation, thereby effectively inhibiting H. pylori. Coptisine may thus be an effective anti-H. pylori agent.

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“…This CYS residue helps in positioning other residues in appropriate sites for catalysis. [47] It was also verified that the substitution of nickel ions with several other metals has little effect on urease activation. [48] 1.…”

Section: Active Site Structure Of Ureasementioning

confidence: 92%

Urease Inhibition and Structure‐Activity Relationship Study of Thiazolidinone‐, Triazole‐, and Benzothiazole‐Based Heterocyclic Derivatives: A Focus Review

et al. 2023

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Urease has a long and distinguished history in the development of enzymology since it was the first enzyme crystallized by Sumner in 1926. The present review article is focused on the urease inhibitory potential of thiazolidinone, triazole, and benzothiazole‐based heterocyclic derivatives. The study begins with the historical developments in the discovery of urease and its substrate, urea, along with the active site architecture of ureases of different origins. The two pathways for the urease‐catalyzed hydrolysis of urea are explained in detail. The urease inhibitory potential of the aforementioned heterocyclic derivatives is reviewed and arranged systematically. Structure‐activity relationships (SARs) study provided the substituents necessary for urease inhibition and will be useful for the researchers working in the field of anti‐ulcer agents. To a step further, important binding interactions were identified with the amino acid residues at the active site of the enzyme. The information gathered is anticipated to offer logical direction and an effective method for creating innovative, potent, and efficient urease inhibitors that will have greater practical uses in the future.

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Soybean (Glycine max) urease: Significance of sulfhydryl groups in urea catalysis

Cited by 15 publications

References 27 publications

Identification of active site residues of Fenugreek β-amylase: Chemical modification and in silico approach

Identification of active site residues of Fenugreek β-amylase: Chemical modification and in silico approach

Coptisine-induced inhibition ofHelicobacter pylori: elucidation of specific mechanisms by probing urease active site and its maturation process

Urease Inhibition and Structure‐Activity Relationship Study of Thiazolidinone‐, Triazole‐, and Benzothiazole‐Based Heterocyclic Derivatives: A Focus Review

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