Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.24.27 (thermolysin)
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Neutral endopeptidase (EC 3.4.24.11) is a major constituent of kidney brush border membranes. It is also present in the brain where it has been shown to be involved in the inactivation of opioid peptides, methionine- and leucine-enkephalins. For this reason this enzyme is often called 'enkephalinase'. In order to characterize the primary structure of the enzyme, oligonucleotide probes were designed from partial amino acid sequences and used to isolate clones from kidney cDNA libraries. Sequencing of the cDNA inserts revealed the complete primary structure of the enzyme. Neutral endopeptidase consists of 750 amino acids. It contains a short N-terminal cytoplasmic domain (27 amino acids), a single membrane-spanning segment (23 amino acids) and an extracellular domain that comprises most of the protein mass. The comparison of the primary structure of neutral endopeptidase with that of thermolysin, a bacterial Zn-metallopeptidase, indicates that most of the amino acid residues involved in Zn coordination and catalytic activity in thermolysin are found within highly honmologous sequences in neutral endopeptidase.
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PMID:Amino acid sequence of rabbit kidney neutral endopeptidase 24.11 (enkephalinase) deduced from a complementary DNA. 244 Jun 77

Proteases with trypsin-, chymotrypsin- and thermolysin-like specificity were detected in Culex quinquefasciatus larval midguts. Their activities were monitored by N-terminal amino acid sequence analysis of the Bacillus thuringiensis subsp. israelensis CryIVD toxin proteolytic fragments. These proteases are located in the larval midgut and in different fractions obtained during the preparation of brush border membrane vesicles. The activity of the midgut proteases increased with an increase in pH. Both the chymotrypsin- and thermolysin-like activities are involved in the processing of solubilized CryIVD toxin, whereas an additional trypsin-like protease is necessary for the CryIVD parasporal inclusion processing. The solubilized CryIVD toxin was first cleaved between Thr347 and Phe348 and between Phe348 and Tyr349, generating a 40-kDa N-terminal fragment and a 32.5-kDa C-terminal fragment. The C-terminal domain was resistant to further processing, with only a small amount of a 31-kDa product appearing due to the action of a thermolysin-like protease. However, the N-terminal domain was very unstable, and was further degraded to about 30 kDa. Unlike the solubilized CryIVD toxin, the processing of the CryIVD parasporal inclusion was very slow at neutral pH. Three protease-resistant products were detected at pHs higher than 9.5 with an overnight incubation at 37 degrees C. The 30- and 28.5-kDa C-terminal peptides are proteolytic products of trypsin- and chymotrypsin-like proteases, respectively; while the 28-kDa N-terminal peptide has 27 amino acids deleted from the N-terminal end by a thermolysin-like protease.
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PMID:In vitro and in vivo proteolysis of the Bacillus thuringiensis subsp. israelensis CryIVD protein by Culex quinquefasciatus larval midgut proteases. 848 24