Elettra-Sincrotrone Trieste S.C.p.A. website uses session cookies which are required for users to navigate appropriately and safely. Session cookies created by the Elettra-Sincrotrone Trieste S.C.p.A. website navigation do not affect users' privacy during their browsing experience on our website, as they do not entail processing their personal identification data. Session cookies are not permanently stored and indeed are cancelled when the connection to the Elettra-Sincrotrone Trieste S.C.p.A. website is terminated.
More info

Structure of Jack Bean Urease Revealed 80 Years After it was Crystallized - Insecticidial Property of Plant Ureases Explained

Folding of the 10-kDa entomotoxic peptide region of JBU (Left) and the corresponding region in B. pasteurii bacterial urease (Right). The insecticidal region in bacterial urease is not intact and consists of two chains.

A. Balasubramanian et al., J. Mol. Biol. 400, 274 (2010)


The three dimensional structure of the historic enzyme, the Jack bean urease (JBU) has recently been unraveled. JBU was not only the first enzyme isolated as a crystalline protein by Sumner in 1926, which fetched him the Nobel Prize, but also the first example of a nickel metalloenzyme and the first protein which showed the presence of sulfhydryl groups. Surprisingly, JBU had to wait more than 80 years for its structural revelation Retrieve Article
Crystal structure of the first plant urease from jack bean: 83 years of journey from its first crystal to molecular structure; A. Balasubramanian and K. Ponnuraj, J. Mol. Biol. 400, 274 (2010); 10.1016/j.jmb.2010.05.009

Last Updated on Wednesday, 25 March 2015 17:46