Crystal structure of the first plant urease from jack bean: 83 years of journey from its first crystal to molecular structure
A Balasubramanian, K Ponnuraj - Journal of molecular biology, 2010 - Elsevier
Urease, a nickel-dependent metalloenzyme, is synthesized by plants, some bacteria, and
fungi. It catalyzes the hydrolysis of urea into ammonia and carbon dioxide. Although the …
fungi. It catalyzes the hydrolysis of urea into ammonia and carbon dioxide. Although the …
[HTML][HTML] A new proposal for urease mechanism based on the crystal structures of the native and inhibited enzyme from Bacillus pasteurii: why urea hydrolysis costs …
Background: Urease catalyzes the hydrolysis of urea, the final step of organic nitrogen
mineralization, using a bimetallic nickel centre. The role of the active site metal ions and …
mineralization, using a bimetallic nickel centre. The role of the active site metal ions and …
Interplay of metal ions and urease
EL Carter, N Flugga, JL Boer, SB Mulrooney… - Metallomics, 2009 - academic.oup.com
Urease, the first enzyme to be crystallized, contains a dinuclear nickel metallocenter that
catalyzes the decomposition of urea to produce ammonia, a reaction of great agricultural …
catalyzes the decomposition of urea to produce ammonia, a reaction of great agricultural …
Antifungal activity of plant and bacterial ureases
AB Becker-Ritt, AHS Martinelli, S Mitidieri, V Feder… - Toxicon, 2007 - Elsevier
Ureases (EC 3.5. 1.5) are nickel-dependent metalloenzymes that catalyze the hydrolysis of
urea to ammonia and carbon dioxide. Produced by plants, fungi and bacteria, but not by …
urea to ammonia and carbon dioxide. Produced by plants, fungi and bacteria, but not by …
[HTML][HTML] Ureases: Historical aspects, catalytic, and non-catalytic properties–A review
K Kappaun, AR Piovesan, CR Carlini… - Journal of advanced …, 2018 - Elsevier
Abstract Urease (urea amidohydrolase, EC 3.5. 1.5) is a nickel-containing enzyme produced
by plants, fungi, and bacteria that catalyzes the hydrolysis of urea into ammonia and …
by plants, fungi, and bacteria that catalyzes the hydrolysis of urea into ammonia and …
Structures of the Klebsiella aerogenes Urease Apoenzyme and Two Active-Site Mutants,
E Jabri, PA Karplus - Biochemistry, 1996 - ACS Publications
Urease from Klebsiella aerogenes [Jabri et al.(1995) Science 268, 998− 1004] is an (αβγ) 3
trimer with each α-subunit having an (αβ) 8-barrel domain containing a binickel active …
trimer with each α-subunit having an (αβ) 8-barrel domain containing a binickel active …
Proteus mirabilis urease: nucleotide sequence determination and comparison with jack bean urease
Proteus mirabilis, a common cause of urinary tract infection, produces a potent urease that
hydrolyzes urea to NH3 and CO2, initiating kidney stone formation. Urease genes, which …
hydrolyzes urea to NH3 and CO2, initiating kidney stone formation. Urease genes, which …
The complex of Bacillus pasteurii urease with β-mercaptoethanol from X-ray data at 1.65-Å resolution
The structure of β-mercaptoethanol-inhibited urease from Bacillus pasteurii, a highly
ureolytic soil micro-organism, was solved at 1.65 Å using synchrotron X-ray cryogenic …
ureolytic soil micro-organism, was solved at 1.65 Å using synchrotron X-ray cryogenic …
Inactivation of urease by catechol: Kinetics and structure
Urease is a Ni (II)-containing enzyme that catalyzes the hydrolysis of urea to yield ammonia
and carbamate at a rate 10 15 times higher than the uncatalyzed reaction. Urease is a …
and carbamate at a rate 10 15 times higher than the uncatalyzed reaction. Urease is a …
The structure of the elusive urease–urea complex unveils the mechanism of a paradigmatic nickel‐dependent enzyme
Urease, the most efficient enzyme known, contains an essential dinuclear NiII cluster in the
active site. It catalyzes the hydrolysis of urea, inducing a rapid pH increase that has negative …
active site. It catalyzes the hydrolysis of urea, inducing a rapid pH increase that has negative …