What is "thermolysin"

Thermolysin \Ther`mo*ly"sin\, n. [Thermo- + Gr. ly`ein to loose + -in.] (Biochem.) a proteolytic enzyme obtained from the bacterium Bacillus thermoproteolyticus, which hydrolyses the N-terminal amide bonds of hydrophobic amino acid residues in proteins. It is used in studies of protein structure. It has a molecular weight of about 37,500 and contains zinc and calcium in its active configuration.
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n. (context enzyme English) A thermostable neutral metalloproteinase enzyme produced by the gram-positive bacterium ''Bacillus thermoproteolyticus''.

Thermolysin (, Bacillus thermoproteolyticus neutral proteinase, thermoase, thermoase Y10, TLN) is a thermostable neutral metalloproteinase enzyme produced by the Gram-positive bacteria Bacillus thermoproteolyticus. It requires one zinc ion for enzyme activity and four calcium ions for structural stability. Thermolysin specifically catalyzes the hydrolysis of peptide bonds containing hydrophobic amino acids. However thermolysin is also widely used for peptide bond formation through the reverse reaction of hydrolysis. Thermolysin is the most stable member of a family of metalloproteinases produced by various Bacillus species. These enzymes are also termed 'neutral' proteinases or thermolysin -like proteinases (TLPs).