Preliminary crystallographic studies of urease from jack bean and from Klebsiella aerogenes
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Structural Biology
Reference19 articles.
1. Jack Bean Urease (EC 3.5.1.5.). A new purification and reliable rate assay;Blakeley;Biochemistry,1969
2. X-ray absorption spectroscopic evidence for binding of the competitive inhibitor 2-mercaptoethanol to the nickel sites of jack bean urease. A new NiNi interaction in the inhibited enzyme;Clark;Inorg. Chem,1990
3. Jack bean urease (EC 3.5.1.5). A metalloenzyme. A simple biological role for nickel?;Dixon;J. Amer. Chem. Soc,1975
4. Jack bean urease (EC 3.5.1.5). II. The relationship between nickel, enzymatic activity, and the “abnormal” ultraviolet spectrum;Dixon;Canad. J. Biochem,1980
5. Jack bean urease (EC 3.5.1.5). IV. The molecular mechanism of inhibition by hydroxamic acids. Spectrophotometric titration of enzymes with reversible inhibitors;Dixon;Canad. J. Biochem,1980
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