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14-September-2008 18:02:49 - Thermolysin Thermolysin EC 3.4.24.27 is a thermostable neutral metalloproteinase enzyme produced by the gram-positive bacteria Bacillus thermoproteolyticus.1 It requires one zinc ion for enzyme activity and four calcium ions ions for structural stability.2 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.3 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. Contents 1 Synthesis 2 Structure 3 References 4 External links Synthesis Like all bacterial extracellular proteases thermolysin is first synthesised by the bactrium as a pre-proenzyme.4 Thermolysin is synthesized as a pre-proenzyme consisting of a signal peptide 28 amino acids long, a pro-peptide 204 amino acids long and the mature enzyme itself 316 amino acids in length. The signal peptide acts as a signal for translocation of pre-prothermolysin to the bacterial cytoplasmic membrane. In the periplasm pre-prothermolysin is then processed into prothermolysin by a signal peptidase. The prosequence then acts as a molecular chaperone and leads to autocleavage of the peptide bond linking pro and mature sequences. The mature protein is then secreted into the extracellular medium.5 Structure Structure of thermolysin taken from pdb file 3TMN Structure of thermolysin taken from pdb file 3TMN Thermolysin consists of a beta pleated sheet rich N-terminal domain and a alpha helical rich C-terminal domain. These two domains are connected by a central alpha helix. References ^ Endo, S. 1962. Studies on protease produced by thermophilic bacteria. J. Ferment. Technol. 40: 346-353. ^ Tajima M, Urabe I. et al. 1976. Role of calcium ions in the thermostability of thermolysin and Bacillus subtilis var. amylosacchariticus neutral protease. Eur. J. Biochem. 64 1: 243-247. PMID 819262. ^ Trusek-Holownia A. 2003. Synthesis of ZAlaPheOMe, the precursor of bitter dipeptide in the two-phase ethyl acetate-water system catalysed by thermolysin. J. Biotechnol. 102 2: 153-163. PMID 12697393. ^ Yasukawa K, Kusano M, Inouye K. 2007. A new method for the extracellular production of recombinant thermolysin by co-expressing the mature sequence and pro-sequence in Escherichia coli. Protein Eng. Des. Sel. 20 8: 375-383. PMID 17616558. ^ Inouye K, Kusano M. et al. 2007. Engineering, expression, purification, and production of recombinant thermolysin. Biotechnol. Annu. Rev. 13: 43-64. PMID 17875473. External links MeSH Thermolysin This biochemistry article is a stub. v d e Proteases: metalloendopeptidases EC 3.4.24 ADAM proteins Alpha secretases ADAM9 · ADAM10 · ADAM17 · ADAM19 · ADAM2 · ADAM7 · ADAM8 · ADAM11 · ADAM12 · ADAM15 · ADAM18 · ADAM22 · ADAM23 · ADAM28 · ADAM33 · ADAMTS1 · ADAMTS2 · ADAMTS3 · ADAMTS4 · ADAMTS5 · ADAMTS8 · ADAMTS9 · ADAMTS10 · ADAMTS12 · ADAMTS13 Matrix metalloproteinase Collagenase · Gelatinase Other Neprilysin · Procollagen peptidase · Thermolysin · Pregnancy-associated plasma protein A · Bone morphogenetic protein 1 · Insulysin · Lysostaphin · Insulin degrading enzyme Retrieved from http://en..org/wiki/Thermolysin Categories: Biochemistry stubs | Enzymes Views Article Discussion this page History Personal tools Log in / create account Navigation Main page Contents Featured content Current events Random article Search Go Search Interaction Community portal Recent changes Contact Donate to Help Toolbox What links here Related changes Upload file Special pages Printable version Permanent link Cite this page Languages Deutsch Svenska This page was last modified on 23 June 2008, at 21:49
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