Thermolysin
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FunctionThermolysin or thermostable neutral proteinase (TML) is a thermostable metalloproteinase enzyme from Bacillus thermoproteolyticus. It catalyzes the hydrolysis of peptide bonds containing hydrophobic residues. See Metalloproteases and Matrix metalloproteinase for discussion. Structural highlightsThermolysin 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]. 3D Structures of Thermolysin
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This page was last modified 09:03, 13 August 2026.