| Thermolysin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Crystallographic structure of Bacillus thermoproteolyticus thermolysin.[1] | |||||||||
| Identifiers | |||||||||
| EC no. | 3.4.24.27 | ||||||||
| CAS no. | 9073-78-3 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Thermolysin (EC 3.4.24.27, Bacillus thermoproteolyticus neutral proteinase, thermoase, thermoase Y10, TLN) is a thermostable neutral metalloproteinase enzyme produced by the Gram-positive bacteria Bacillus thermoproteolyticus.[2] It requires one zinc ion for enzyme activity and four calcium ions for structural stability.[3] 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.[4] 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).
- ^ PDB: 3TMN; Holden HM, Matthews BW (March 1988). "The binding of L-valyl-L-tryptophan to crystalline thermolysin illustrates the mode of interaction of a product of peptide hydrolysis". J. Biol. Chem. 263 (7): 3256–60. doi:10.2210/pdb3tmn/pdb. PMID 3343246.
- ^ 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. doi:10.1111/j.1432-1033.1976.tb10293.x. 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. doi:10.1016/S0168-1656(03)00024-5. PMID 12697393.