Thermolysin: Difference between revisions
Jump to navigation
Jump to search
New page: left|200px|thumb|Crystal Structure of Thermolysin [[3dnz]] {{STRUCTURE_3dnz| PDB=3dnz | SIZE=300| SCENE= |right|CAPTION=Thermolysin 3dnz }} |
Michal Harel (talk | contribs) No edit summary |
||
| (34 intermediate revisions by 2 users not shown) | |||
| Line 1: | Line 1: | ||
[[ | <StructureSection load='2a7g' size='350' side='right' scene= caption='Thermolysin complex with acetate, DMS, Zn+2 (grey) and Ca+2 (green) ions, [[2a7g]]'> | ||
== Function == | |||
[[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 == | |||
Thermolysin is a well researched [[metalloproteases|metalloprotease]] containing <scene name='User:Ralf_Stephan/Sandbox_2/Zinc/2'>zinc</scene> (click this!) and the amino acids His-Glu-X-His-His as its catalytic center. <scene name='User:Ralf_Stephan/Sandbox_2/Res_yellow/3'>Glu-166, His-142 and -146 are grouped around the zinc atom</scene>, holding it fast, while <scene name='User:Ralf_Stephan/Sandbox_2/Res/1'>Glu-143 holds the polarized water atom. Additionally, Tyr-157 and His-231</scene> stabilize the substrate protein which will be cleaved into two smaller proteins.<ref>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</ref><ref>PMID:11935352</ref>. | |||
== 3D Structures of Thermolysin == | |||
[[Thermolysin 3D structures]] | |||
</StructureSection> | |||
== References == | |||
<references/> | |||
[[Category: Topic Page]] | |||
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
|
| ||||||||||
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