thermolysin การใช้

• Thermolysin has a molecular weight of 34, 600 Da.
• It is a known reversible inhibitor of thermolysin and is expected to inhibit other metalloproteinases.
• However thermolysin is also widely used for peptide bond formation through the reverse reaction of hydrolysis.
• Insulin B chain cleavage pattern identical to that of thermolysin, but specificity differs in other respects
• These enzymes are also termed'neutral'proteinases or thermolysin-like proteinases ( TLPs ).
• :Cleavage of insulin B chain with specificity similar to that of thermolysin, preferring hydrophobic P1'residue.
• Thermolysin is the most stable member of a family of metalloproteinases produced by various " Bacillus " species.
• However, commercially available thermolysin is dependent on calcium ions for activity and denatures itself just above 85 degrees Celsius.
• It is an inhibitor of the enzyme thermolysin, a membrane metallo-endopeptidase inhibitor, and an endothelin converting enzyme inhibitor.
• The catalytic site is contained within a thermolysin-like region found in many metallopeptidases and located in the domain near the floor of the channel.
• Examples of enzymes that ilomastat inhibit include thermolysin, and anthrax lethal factor endopeptidase ( LF ) produced by the bacterium " Bacillus anthracis ".
• In particular a phenylalanine ( F ) at amino acid position 63 and a proline ( P ) at amino acid position 69 contribute significantly to thermolysin stability.
• Alternatively, it has been shown for thermolysin ( another metalloproteinase ) that the amide product can be released in its neutral ( R-NH2 ) form.
• He also solved early structures of the thermophilic bacterial enzyme thermolysin, the helix-turn-helix DNA-binding transcription factor lambda Cro repressor, and the light-antenna bacteriochlorophyll protein.
• Papain as well as other proteases, including bromelain, collagenase, trypsin and thermolysin, have also been tried or used according to other reports on the use of proteases for debridement of wounds and burns without damaging healthy tissue.
• The peptidase M13 family believed to activate or inactivate oligopeptide ( pro )-hormones such as opioid peptides, Thermolysin complexed with the inhibitor ( " S " )-thiorphan are isomeric thiol-containing inhibitors of endopeptidase EC 24-11 ( also called " enkephalinase " ).
• In contrast to many proteins that undergo conformational changes upon heating and mutation of its binding site, reduced thermolysin stability by 7 癈 . However, while calcium binding makes a significant contribution to stabilising thermolysin, more crucial to stability is a small cluster of N-terminal domain amino acids located at the proteins surface.
• In contrast to many proteins that undergo conformational changes upon heating and mutation of its binding site, reduced thermolysin stability by 7 癈 . However, while calcium binding makes a significant contribution to stabilising thermolysin, more crucial to stability is a small cluster of N-terminal domain amino acids located at the proteins surface.
• Changing these amino acids to threonine ( T ) and alanine ( A ) respectively in a less stable thermolysin-like proteinase produced by " Bacillus stearothermophillus " ( TLP-ste ), results in individual reductions in stability of 7 癈 ( F63?! T ) and 6.3 癈 ( P69?! A ) and when combined a reduction in stability of 12.3 癈.