Thermolysin: Difference between revisions
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<StructureSection load='2a7g' size='350' side='right' scene= caption='Thermolysin complex with acetate, DMS, Zn+2 (grey) and Ca+2 (green) ions, [[2a7g]]'> | <StructureSection load='2a7g' size='350' side='right' scene= caption='Thermolysin complex with acetate, DMS, Zn+2 (grey) and Ca+2 (green) ions, [[2a7g]]'> | ||
== Function == | == Function == | ||
[[Thermolysin]] (TML) is a thermostable metalloproteinase enzyme from ''Bacillus thermoproteolyticus''. It catalyzes the hydrolysis of peptide bonds containing hydrophobic residues. See [[Metalloproteases]] and [[Matrix metalloproteinase]] for discussion. | [[Thermolysin]] or '''thermostable neutral proteinase''' (TML) is a thermostable metalloproteinase enzyme from ''Bacillus thermoproteolyticus''. It catalyzes the hydrolysis of peptide bonds containing hydrophobic residues. See [[Metalloproteases]] and [[Matrix metalloproteinase]] for discussion. | ||
== Structural highlights == | == Structural highlights == | ||
Latest revision as of 12:49, 17 December 2023
FunctionThermolysin or thermostable neutral proteinase (TML) is a thermostable metalloproteinase enzyme from Bacillus thermoproteolyticus. It catalyzes the hydrolysis of peptide bonds containing hydrophobic residues. See Metalloproteases and Matrix metalloproteinase for discussion. Structural highlightsThermolysin is a well researched metalloprotease containing (click this!) and the amino acids His-Glu-X-His-His as its catalytic center. , holding it fast, while stabilize the substrate protein which will be cleaved into two smaller proteins.[1][2]. 3D Structures of Thermolysin
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ReferencesReferences
- ↑ Matthews, BW. (1988): Structural basis of the action of thermolysin and related zinc peptidases. In: Acc. Chem. Res. 21(9); 333–340; http://dx.doi.org/10.1021/ar00153a003
- ↑ Pelmenschikov V, Blomberg MR, Siegbahn PE. A theoretical study of the mechanism for peptide hydrolysis by thermolysin. J Biol Inorg Chem. 2002 Mar;7(3):284-98. Epub 2001 Sep 27. PMID:11935352 doi:http://dx.doi.org/10.1007/s007750100295