Thermolysin
From Proteopedia
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References
Created with the participation of Ralf Stephan.
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 zinc (click this!) and the amino acids His-Glu-X-His-His as its catalytic center. Glu-166, His-142 and -146 are grouped around the zinc atom, holding it fast, while Glu-143 holds the polarized water atom. Additionally, Tyr-157 and His-231 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 July 2012 Thermolysin2whz, 3fvp, 3dnz, 3do0, 3do1, 3do2, 2g4z, 2a7g, 1gxw, 1kei, 1l3f, 1tlx, 2tlx, 8tln, 3p7p, 3p7q, 3p7r, 3p7s, 3p7t, 3p7u, 3p7v, 3p7w – TML TML+transition state analog1tlp, 1tmn, 2tmn, 4tmn, 5tmn – TML+transition state analog TML+ amino acid1kl6 – TML+ alanine TML+ dipeptide2wi0, 3tmn – TML+ dipeptide TML+inhibitor1fjo, 1fj3, 1fjq, 1fjt, 1fju, 1fjv, 1fjw, 4tli, 5tli, 6tli, 7tli, 8tli, 1tli, 2tli, 3tli – TML soaked in organic solvents
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Created with the participation of Ralf Stephan.
This page was last modified 07:44, 3 July 2012.