Thermolysin

From Proteopedia

proteopedia linkproteopedia link

Revision as of 08:29, 18 June 2015 (edit) Michal Harel (Talk | contribs) ← Previous diff		Revision as of 07:54, 11 September 2016 (edit) (undo) Michal Harel (Talk | contribs) Next diff →
Line 43:		Line 43:
	**[[3t2j]] – TML + betaine<br />		**[[3t2j]] – TML + betaine<br />
	}}		}}
		+	== References ==
		+	<references/>
	[[Category: Topic Page]]		[[Category: Topic Page]]

---

Revision as of 07:54, 11 September 2016

spinqualitylabelsall models Thermolysin complex with acetate, DMS, Zn+2 (grey) and Ca+2 (green) ions, 2a7g Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image 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 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]. See Metalloproteases and Matrix metalloproteinase for discussion.

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