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Thermolysin

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<StructureSection load='2a7g' size='400' side='right' scene= caption='Thermolysin complex with acetate, DMS, Zn+2 (grey) and Ca+2 (green) ions, [[2a7g]]'>
<StructureSection load='2a7g' size='400' side='right' scene= caption='Thermolysin complex with acetate, DMS, Zn+2 (grey) and Ca+2 (green) ions, [[2a7g]]'>
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== Function ==
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[[Thermolysin]] (TML) is a thermostable metalloproteinase enzyme from ''Bacillus thermoproteolyticus''. It catalyzes the hydrolysis of peptide bonds containing hydrophobic residues.
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[[Thermolysin]] (TML) is a thermostable metalloproteinase enzyme from ''Bacillus thermoproteolyticus''. It catalyzes the hydrolysis of peptide bonds containing hydrophobic residues. 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>. See [[Metalloproteases]] and [[Matrix metalloproteinase]] for discussion.
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== Structural highlights ==
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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>. See [[Metalloproteases]] and [[Matrix metalloproteinase]] for discussion.
</StructureSection>
</StructureSection>

Revision as of 07:56, 11 September 2016

Thermolysin complex with acetate, DMS, Zn+2 (grey) and Ca+2 (green) ions, 2a7g

Drag the structure with the mouse to rotate

3D Structures of Thermolysin

Updated on 11-September-2016

References

  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

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

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