Acyl aminoacyl peptidases are two-domain proteins composed by a C-terminal catalytic α/β-hydrolase domain and by an N-terminal β-propeller domain connected through a structural element that is at the N-terminus in sequence but participates in the 3D structure of the C-domain. We investigated about the structural and functional interplay between the two domains and the bridge structure (in this ...

Optical diffraction and computer image processing of electron micrographs were employed to analyze the structure of the regular surface layer of Sporosarcina ureae at high resolution. Negatively stained preparations of regular surface layer fragments showed two types of tetragonal pattern, each having p4 symmetry in projection with a = 12.8 nm. Although the two patterns differed greatly in over...

Urease belongs to a family of highly conserved urea-hydrolyzing enzymes. A common feature of these enzymes is the presence of two Lewis acid nickel ions and reactive cysteine residue in the active sites. In the current study we examined a series of biscoumarins 1-10 for their mechanisms of inhibition with the nickel containing active sites of Jack bean and Bacillus pasteurii ureases. All these ...

It is a universal fact that concrete one of the most employed construction materials and hence its exigency booming at rocket pace, which in turn, has resulted titanic demand ordinary Portland cement. Regrettably, production this essential binder not merely found to consume restricted natural resources but also be associated with emission carbon dioxide—a primary greenhouse gas (GHG) directly a...

Protease was isolated from Sporosarcina RRLJ1 which was collected from acid tea (Camellia sinensis) plantations. It showed potential for production of the enzyme for commercial purposes. The study revealed that optimum pH for growth of the organism was 6.5-7 and supplement of casein (1%) in the medium was required for production of protease. Enzyme production and enzyme activity was maximum in ...