Thermolysin: Difference between revisions

Latest revision as of 12:49, 17 December 2023

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 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

Thermolysin 3D structures

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

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Alexander Berchansky, Michal Harel

[1] 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

[2] 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

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[2]

@@ Line 1: / Line 1: @@
-[[Image:3dnz.jpg|left|200px|thumb|Crystal Structure of Thermolysin [[3dnz]]]]
+<StructureSection load='2a7g'  size='350' side='right' scene= caption='Thermolysin complex with acetate, DMS, Zn+2 (grey) and Ca+2 (green) ions, [[2a7g]]'>
-{{STRUCTURE_3dnz|  PDB=3dnz  | SIZE=300| SCENE=Thermolysin/Cv/1 |right|CAPTION=Thermolysin [[3dnz]] }}
+== 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.
-Thermolysin (TML) is a thermostable metalloproteinase enzyme from ''Bacillus thermoproteolyticus''.  It catalyzes the hydrolysis of peptide bonds  containing hydrophobic residues. The images at the left and at the right correspond to one representative Thermolysin ([[3dnz]]).
+== 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>.
-{{TOC limit|limit=2}}
 == 3D Structures of Thermolysin ==
+[[Thermolysin 3D structures]]
+</StructureSection>
-=== Thermolysin ===
+== References ==
+<references/>
+[[Category: Topic Page]]
-[[2whz]], [[3fvp]], [[3dnz]], [[3do0]], [[3do1]], [[3do2]], [[2g4z]], [[2a7g]], [[1gxw]], [[1kei]], [[1l3f]], [[1tlx]], [[2tlx]], [[8tln]] – TML<br />
-[[1trl]] - TML residues 255-316 – NMR<br />
-[[3fxs]], [[3fbo]], [[3eim]], [[1lna]], [[1lnb]], [[1lnc]], [[1lnd]], [[1lne]], [[1lnf]] - TML residues 233-548+metal ion replacing Ca<br />
-=== TML+transition state analog ===
-[[1tlp]], [[1tmn]], [[2tmn]], [[4tmn]], [[5tmn]] – TML+transition state analog<br />
-=== TML+ dipeptide ===
-[[2wi0]], [[3tmn]] – TML+ dipeptide <br />
-[[3fgd]] - TML residues 233-548+dipeptide<br />
-=== TML+inhibitor ===
-[[1fjo]], [[1fj3]], [[1fjq]], [[1fjt]], [[1fju]], [[1fjv]], [[1fjw]], [[4tli]], [[5tli]], [[6tli]], [[7tli]], [[8tli]], [[1tli]], [[2tli]], [[3tli]] – TML soaked in organic solvents<br />
-[[3fv4]], [[3fxp]], [[3flf]], [[3fb0]], [[3fcq]], [[3f28]], [[3f2p]] – TML residues 233-548+inhibitor<br />
-[[3fwd]], [[3for]], [[1y3g]], [[1zdp]], [[1z9g]], [[1pes]], [[1pe7]], [[1pe8]], [[1os0]], [[1kto]], [[1ks7]], [[1kro]], [[1kr6]], [[1kkk]], [[1kjo]], [[1kjp]], [[1qf0]], [[1qf1]], [[1qf2]], [[1hyt]], [[1thl]], [[6tmn]], [[7tln]], [[4tln]], [[5tln]] – TML+inhibitor<br />