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. 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. Contents3D Structures of ThermolysinUpdated on 24-September-2014 Thermolysin2whz, 3fvp, 3dnz, 3do0, 3do1, 3do2, 2g4z, 2a7g, 1gxw, 1kei, 1l3f, 1tlx, 2tlx, 8tln, 3p7p, 3p7q, 3p7r, 3p7s, 3p7t, 3p7u, 3p7v, 3p7w, 3zi6 – 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 09:11, 24 September 2014.