Thermolysin: Difference between revisions
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[[Image:2a7g.png|left|200px|thumb|Crystal Structure of Thermolysin [[2a7g]]]] | [[Image:2a7g.png|left|200px|thumb|Crystal Structure of Thermolysin [[2a7g]]]] | ||
Revision as of 13:21, 17 July 2013
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 (2a7g). 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 ThermolysinUpdate February 2013 Thermolysin2whz, 3fvp, 3dnz, 3do0, 3do1, 3do2, 2g4z, 2a7g, 1gxw, 1kei, 1l3f, 1tlx, 2tlx, 8tln, 3p7p, 3p7q, 3p7r, 3p7s, 3p7t, 3p7u, 3p7v, 3p7w – TML 3ls7 - TML residues 233-548 TML+transition state analog1tlp, 1tmn, 2tmn, 4tmn, 5tmn – TML+transition state analog TML+ amino acid1kl6 – TML+ alanine 3qgo – TML + phenylalanine methyl ester TML+ dipeptide3fgd - TML residues 233-548+dipeptide TML+inhibitor1fjo, 1fj3, 1fjq, 1fjt, 1fju, 1fjv, 1fjw, 4tli, 5tli, 6tli, 7tli, 8tli, 1tli, 2tli, 3tli – TML soaked in organic solvents 3fv4, 3fxp, 3flf, 3fb0, 3fcq, 3f28, 3f2p – TML residues 233-548+inhibitor
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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
Created with the participation of Ralf Stephan.