EC Number   |
General Information |
Reference |
|---|
   3.4.24.27 | evolution |
thermolysin and pseudolysin belong to subclan MA(E) of peptidases, also known as the Glu-zincins, of the matrix metalloproteinases family of zinc-containing endoproteinases with broad substrate specificity and extracellular matrix components are among the substrates |
733787 |
| 3.4.24.27 | more |
a thermostable neutral protease |
733899 |
| 3.4.24.27 | more |
autodegradation at position 154155 |
717113 |
| 3.4.24.27 | more |
development and evaluation of a method providing information at the surface of the outer envelope membrane, based on specific tagging with biotin or proteolysis using thermolysin, a non-membrane permeable protease. Envelope, thylakoid, and stroma proteins are separated by two-dimensional electrophoresis and analyzed by immunostaining and mass spectrometry, overview |
733917 |
| 3.4.24.27 | more |
life cycle of the thermolysin-like protease from Bacillus stearothermophilus in light of the calcium-dependent stability and instability of the N-terminal domain. |
718367 |
| 3.4.24.27 | more |
proposed mechanism of action for the thermolysin-catalyzed synthesis of aspartame precursor carbobenzoxy-L-aspartyl-L-phenylalanine methyl ester, overview. Residues E143, Y157, and H231 represent the catalytic triad, enzyme active site structure analysis |
732993 |
| 3.4.24.27 | more |
structure analsis using enzyme structure PDB ID 8TLN. Catalytically important residues Glu143 and His231. Important role of Asn116 in the activity and stability of thermolysin presumably by stabilizing the beta-hairpin structure. In the N-terminal domain of thermolysin, two antiparallel beta-strands, Asn112-Ala113-Phe114-Trp115 and Ser118-Gln119-Met120-Val121-Tyr122 are connected by an Asn116-Gly117 turn to form a beta-hairpin structure |
734109 |
| 3.4.24.27 | more |
the glutamic acid of the HEXXH motif is catalytically important |
733787 |
| 3.4.24.27 | more |
the peptide products from hydrolysis of elastin and collagen by the enzyme have an inhibitory effect on angiotensin I-converting enzyme and antihypertensive activity, overview |
-, 733529 |
| 3.4.24.27 | physiological function |
thermolysin family proteases are related to various diseases such as bacterial infections, cholera, gastritis and peptic ulcers, and gastric carcinoma |
734411 |
