Endothia

Endothall [45-73-2] Endothelins Endothia parasitica Endothion [2778-04-3] Endotoxin... 

Fig. 10. The effects of chestnut blight (Endothia parasitica) on a deciduous forest ecosystem (after Day Monk, 1974).

The carboxyl proteases are so called because they have two catalytically essential aspartate residues. They were formerly called acid proteases because most of them are active at low pH. The best-known member of the family is pepsin, which has the distinction of being the first enzyme to be named (in 1825, by T. Schwann). Other members are chymosin (rennin) cathepsin D Rhizopus-pepsin (from Rhizopus chinensis) penicillinopepsin (from Penicillium janthinel-lum) the enzyme from Endothia parasitica and renin, which is involved in the regulation of blood pressure. These constitute a homologous family, and all have an Mr of about 35 000. The aspartyl proteases have been thrown into prominence by the discovery of a retroviral subfamily, including one from HIV that is the target of therapy for AIDS. These are homodimers of subunits of about 100 residues.156,157 All the aspartyl proteases contain the two essential aspartyl residues. Their reaction mechanism is the most obscure of all the proteases, and there are no simple chemical models for guidance. 

This aspartic proteinase [EC 3.4.23.22], from the ascomy-cete Endothia parasitica, catalyzes the hydrolysis of proteins with broad specificity similar to that of pepsin A, with preferential action on substrates containing hydrophobic residues at PI and PI. ... 

Alais, C. and Novak, G. 1968. Study of a microbial coagulating enzyme produced by Endothia parasitica. I. Biochemical properties of Pfizer coagulating enzyme (1) and rheological properties of curds formed in the milk. Lait 48, 393-418. 

Reps, A., Poznanski, S. and Kowalska, W. 1970. Characteristics of milk-coagulating proteases obtained from Byssochlamys fulua and Endothia parasitica. Milchwissenschaft. 25, 146-150. 

Reps, A., Poznanski, S., Rymaszewski, J., Jakubowski, J. and Jarmul, I. 1973. Production of milk-clotting enzymes by Byssochlamys fluva and Endothia parasitica moulds. Roczniki Instytutu Przemyslu Mleczarskiego 15, 73-85. 

Thomasow, J., Mrowetz, G. and Schmanke, E. 1970. Experimental cheesemaking with rennet from Endothia parasitica. Milchwissenschaft 25, 211-217. 

Tam, J.T., Whitaker, J.R. 1972. Rates and extents of hydrolysis of several caseins by pepsin, rennin, Endothia parasitica and Mucor pusillus proteinase. J. Dairy Sci. 55, 1523-1531. 

Rennet, Microbial (Endothia parasitica) Produced as an off white to tan, amorphous powder or as a liquid by controlled fermentation using nonpathogenic strains of Endothia parasitica. The powder is soluble in water (the solution is usually tan to dark brown), but practically insoluble in alcohol, in chloroform, and in ether. Major active principle protease. Typical application used in the manufacture of cheese. 

Rennet protease (1) fourth stomach of ruminant animals (2) Endothia parasitica (3) Rhizomucor miehei (4) Rhizomucor pusillus (Lindt) (5) Bacillus cereus none 3.4.23.1 3.4.23.4 3.4.23.22 3.4.23.23... 

Standard Preparation Use a standard-strength rennet, bovine rennet, microbial rennet (Endothia parasitica), or microbial rennet (Mucor species), as appropriate for the preparation to be assayed. Such standards, which are available from commercial coagulant manufacturers, should be of known activity. Dilute the standard-strength material 1 to 200 with water, and mix. Equilibrate to 300 before use, and prepare no more than 2 h before use. 

Rennet, Microbial (nonpathogenic strain of Bacillus cereus), 21 Rennet, Microbial (Endothia parasitica), 21... 

S3)21 Rennet, Microbial (Endothia parasitica), 132, 788, (S3)21 Rennet, Microbial (Rhizomucor (Mucor) sp.), 132, (S3)21 Rennet, Microbial (nonpathogenic strain of Bacillus cereus), 132,... 

Endothia acid protease Other Plants Lotus acid protease Nepenthes acid protease Protozoan Tetrahyniena... 

Endothia parasitica acid protease Rhodotorida glutinis acid protease... 

A number of chemical approaches have been used in the design of renin inhibitors. In the absence of the purified enzyme, most of the early search for inhibitors was carried out using crude renin preparations. The amino acid sequences of mouse, rat and human renin were obtained later on using either the traditional isolation and sequencing techniques or cDNA methodology. Various three-dimensional models of renin were constructed in the early stages, based on the x ray structures of other similar aspartyl proteases, for example endothia-pepsin and penicillopepsin. Later on, the X ray crystal structure of recombinant human renin was reported. The inhibitor design process has been based on some of these models. 

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