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- W1570759873 abstract "Ureases are metalloproteins responsible for the one step hydrolysis of urea into ammonia and carbamate [1], the later then rapidly and spontaneously decomposes to form carbon di‐ oxide and a second molecule of ammonia [2]. Plant ureases hold a special place in science history, participating on some important landmarks of biochemistry. For instance, it was by the analysis of Canavalia ensiformis urease crystals that the proteinaceous nature of enzymes could be demonstrated [3], rendering a Chemistry Nobel Prize to James Sumner in 1946. Al‐ so by the studies carried out with the same protein it was obtained the first proof that Ni2+ actually exerts a biological role in living organisms [4]. Ureases usually present two Ni2+ in their active site, with a few exceptions reported [5, 6]. However, all this was only possible after Takeuchi’s observation that the crude extracts of soybean (Glycine max) seeds present high amounts of urease [7]. In those days, urease had been observed only in microorganisms and in algae, being Takeuchi’s finding the first evidence of the presence of ureases in higher plants. The importance of this discovery relays on the fact that it made urease largely availa‐ ble for any researcher on the globe, and many more works on ureases followed, utilizing the soybean seed urease with the objective of understanding enzyme functioning. Soybean ure‐ ase was also one of the key players on the development of enzymology, with studies on this enzyme leading to hypothesis that were essential to confirm the observations of Michaelis and Menten on the rate of reaction of enzymes and substrates [8]." @default.
- W1570759873 created "2016-06-24" @default.
- W1570759873 creator A5013343749 @default.
- W1570759873 creator A5076486808 @default.
- W1570759873 creator A5081780210 @default.
- W1570759873 date "2013-01-02" @default.
- W1570759873 modified "2023-10-14" @default.
- W1570759873 title "Soybean Urease: Over a Hundred Years of Knowledge" @default.
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