Introduction
Enzymes are highly selective catalytic proteins which control and regulate all biochemical processes in the body. They are produced by living cells in order to accelerate both the rate and specificity of metabolic reactions. Enzymes are highly specific in their function because each enzyme is programmed to carry out one special task. Several million enzymes mediate chemical reactions occurring in a living system. Microbial enzymes play a major role in the diagnosis, curing, biochemical investigation, and monitoring of many dreaded diseases. Microorganisms represent an excellent source of many therapeutic enzymes owing to their broad biochemical diversity and their susceptibility to genetic manipulation. (AsANO, 1980)
In enzymology, an amidase (EC 3.5.1.4, acylamidase, acylase (misleading), amidohydrolase (ambiguous), deaminase (ambiguous), fatty acylamidase, N-acetylaminohydrolase (ambiguous) is an enzyme that catalyzes the hydrolysis of an amide:
Thus, the two substrates of this enzyme are monocarboxylic acid amide and H2O, whereas its two products are mono carboxylate and NH3.
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They are widespread, being found in both prokaryotes and eukaryotes. AS enzymes catalyse the hydrolysis of amide bonds (CO-NH2), although the family has diverged widely with regard to substrate specificity and function. Nonetheless, these enzymes maintain a core alpha/beta/alpha structure, where the topologies of the N- and C-terminal halves are similar. AS enzymes characteristically have a highly conserved C-terminal region rich in serine and glycine residues, but devoid of aspartic acid and histidine residues, therefore they differ from classical serine hydrolases. These enzymes possess a unique, highly conserved Ser-Ser-Lys catalytic triad used for amide hydrolysis, although the catalytic mechanism for acyl-enzyme intermediate formation can differ between enzymes. (Yun H et.