Thimet oligopeptidases

An endopeptidase that is incapable of cleaving proteins but can cleave small peptides. An example is thimet oligopeptidase (MEROPS M03.001). 

Thimet oligopeptidase Luteinizing hormone releasing Tyr5-Gly6... 

Further susceptibilities of the nonapeptide are shown in Fig. 6.34. Thus, the Pro7-Phe8 bond is also cleaved by neprilysin (EC 3.4.24.11) and endothelin-converting enzyme (EC 3.4.24.71) [149][165]. The C-terminal residue is susceptible to cleavage by several carboxypeptidases, particularly carboxypeptidase N. Thimet oligopeptidase (EC 3.4.24.15) is also able to act on bradykinin, which is cleaved at the Phe5-Ser6 bond [144],... 

LHRH (see Fig. 6.16) is highly sensitive to proteolytic degradation. Enzymes with particular activity toward LHRH include angiotensin-converting enzyme, neprilysin, and thimet oligopeptidase (see Sect. 6.4.2 and Table 6.6). D-Amino acid substitution in position 6, 7, or 10 has led to the de-... 

This zinc-dependent enzyme [EC 3.4.24.15], also referred to as thimet oligopeptidase and soluble metalloendopep-tidase, catalyzes the hydrolysis of peptide bonds with a preferential cleavage at positions with hydrophobic residues at PI, P2, and P3 and a small amino acid residue at PI. Substrates for this enzyme contain five to fifteen amino acid residues. 

Endopeptidase-24.15 (EC 3.4.24.15 thimet oligopeptidase) is a zinc-metalloproteinase found in soluble and membrane forms. Notable substrates include angiotensin I, angiotensin II, bradykinin, LH-RH, neurotensin and somatostatin. Inhibitors include CPP-Ala-Ala-Tyr-pAB CPE-Ala-Ala-Phe-pAB,... 

Several Zn metalloproteases play an important role in A 3 turnover in the CNS [156]. Insulin degrading enzyme (IDE), neprilysin (NEP), endothelin-converting enzyme, angiotensin-converting enzyme, thimet oligopeptidase and MMPs have all demonstrated A 3 cleavage activity in vitro and/or in vivo [156]. Numerous studies have examined in great detail how Zn modulates the protease activity of these enzymes [157]. Unfortunately, little is known... 

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