α-Amylase has been studied extensively from various sides. This enzyme is used in many industries .Many applications of this enzyme have encouraged us for greater attempts on the study of α-amylase and to search for more effective processes. In this investigation, the structure of nanotube - catalytic site of bacillus subtilis α- amylase was optimized by hype...

Between 8 to 14 calcium-calmodulin (Ca(2+)/CaM) dependent protein kinase-II (CaMKII) subunits form a complex that modulates synaptic activity. In living cells, the autoinhibited holoenzyme is organized as catalytic-domain pairs distributed around a central oligomerization-domain core. The functional significance of catalytic-domain pairing is not known. In a provocative model, catalytic-domain ...

The Bacillus circulans ATCC 31382 β-galactosidase (BgaD) is a retaining-type glycosidase of glycoside hydrolase family 2 (GH2). Its commercial enzyme preparation, Biolacta N5, is used for commercial-scale production of galacto-oligosaccharides (GOS). The BgaD active site and catalytic amino acid residues have not been studied. Using bioinformatic routines we identified two putative catalytic gl...

Acetylcholinesterase (AChE) and butyrylcholinesterase (BuChE) catalyze the hydrolysis of the neurotransmitter acetylcholine and, thereby, function as coregulators of cholinergic neurotransmission. For both enzymes, hydrolysis takes place near the bottom of a 20 Å deep active site gorge. A number of amino acid residues within the gorge have been identified as important in facilitating efficient ...

Enzymes from different species that have identical catalytic activities are usually very similar in their amino-acid sequences and three-dimensional structures. This is particularly true at the catalytic site, where the amino acids that form the active site and participate in catalysis are highly conserved. The similarities between homologous enzymes have hampered the design of species-specific...