Protease characterized

Subtilases comprise the second largest family of serine proteases characterized to date with members in Archaebacteria, eukaryotes, and even viruses. Surprisingly, the catalytic domains of subtilases display a high degree of sequence variability with... 

Kam CM, Hudig D, Powers JC. Granzymes (lymphocyte serine proteases) Characterization with natural and synthetic substrates and inhibitors. Biochim Biophys Acta 2000 1477 307-323. 

Metabolic Functions. Zinc is essential for the function of many enzymes, either in the active site, ie, as a nondialyzable component, of numerous metahoenzymes or as a dialyzable activator in various other enzyme systems (91,92). WeU-characterized zinc metahoenzymes are the carboxypeptidases A and B, thermolysin, neutral protease, leucine amino peptidase, carbonic anhydrase, alkaline phosphatase, aldolase (yeast), alcohol... 

Tetanus is a disease caused by the release of neurotoxins from the anaerobic, spore-forming rod Clostridium tetani. The clostridial protein, tetanus toxin, possesses a protease activity which selectively degrades the pre-synaptic vesicle protein synaptobrevin, resulting in a block of glycine and y-aminobutyric acid (GABA) release from presynaptic terminals. Consistent with the loss of neurogenic motor inhibition, symptoms of tetanus include muscular rigidity and hyperreflexia. The clinical course is characterized by increased muscle tone and spasms, which first affect the masseter muscle and the muscles of the throat, neck and shoulders. Death occurs by respiratory failure or heart failure. 

The serine proteases are the most extensively studied class of enzymes. These enzymes are characterized by the presence of a unique serine amino acid. Two major evolutionary families are presented in this class. The bacterial protease subtilisin and the trypsin family, which includes the enzymes trypsin, chymotrypsin, elastase as well as thrombin, plasmin, and others involved in a diverse range of cellular functions including digestion, blood clotting, hormone production, and complement activation. The trypsin family catalyzes the reaction ... 

NMR structural characterization of peptide inhibitors bound to the Hepatitis C virus NS3 protease design of a new P2 substituent. J Med Chem 47 123-132... 

CarriUo A, Stewart KD, Sham HL, Norbeck DW, Kohlbrenner WE, Leonard JM, Kempf DJ, Molla A (1998) In vitro selection and characterization of human immunodeficiency virus type 1 variants with increased resistance to ABT-378, a novel protease inhibitor. J Virol 72 7532-7541 Chambers TJ, Nestorowicz A, Amberg SM, Rice CM (1993) Mutagenesis of the yellow fever virus NS2B protein effects on proteolytic processing, NS2B-NS3 complex formation, and viral replication. J Virol 67 6797-6807... 

Lee TW, Chemey MM, Huitema C, Liu J, James KE, Powers JC, Eltis LD, James MN (2005) Crystal structures of the main peptidase from the SARS coronavirus inhibited by a substrate-fike aza-peptide epoxide. J Mol Biol 353 1137-1151 Liang PH (2006) Characterization and inhibition of SARS-coronavirus main protease. Curr Top Med Chem 6 361-376... 

Margosiak SA, Vanderpool DL, Sisson W, Pinko C, Kan CC (1996) Dimerization of the human cytomegalovirus protease kinetic and biochemical characterization of the catalytic homodimer. Biochemistry 35 5300-5307... 

Partaledis JA, Yamaguchi K, Tisdale M, Blair EE, Falcione C, Maschera B, Myers RE, Pazhanisamy S, Futer O, CuHinan AB et al (1995) In vitro selection and characterization of human immunodeficiency virus type 1 (HIV-1) isolates with reduced sensitivity to hydrox-yethylamino sulfonamide inhibitors of HIV-1 aspartyl protease. J Virol 69 5228-5235 Patick AK (2006) Rhinovirus chemotherapy. Antiviral Res 71 391-396... 

Bishop, P.D., Pearce, G., Bryant, J.E. Ryan, C.A. (1984). Isolation and characterization of the protease inhibitor-inducing factor from tomato leaves, identity and activity of poly- and oligogalacturonide fragments. Journal of Biological Chemistry, 259,13172-7. 

Mast cell protease A3 is less well characterized than tryptase and chymase in terms of physiological substrates. It is involved, among its other functions, in angiotensin metabolism. 

Some of the best investigated anti-nutrients are the enzyme inhibitors present in legumes and other plants. The Bowman-Birk and the Kunitz inhibitors of trypsin and other proteases are among the best characterized. In contrast to the non-specific and widespread influences of tannins and lectins (Carmona, 1996), the Bowman-Birk, Kunitz and other such inhibitors target specific enzymes. Corresponding with this, proteases and other digestive enzymes vary in sensitivity to the different inhibitors. 

Because of their very complex chemical structures and heterogeneity, melanins are difficult to extract, separate, and characterize from tissues. Eumelanins are insoluble in water and organic solvents. They can be extracted from tissues with strong chemicals that are capable of removing lipids, proteins, and other tissue components but also lead to the formation of degradation products. Enzymatic procedures were developed for the isolation of eumelanins from mammalian hair and irises. The first step is sequential digestion with protease, proteinase K, and papaine in the presence... 

Swadesh, J. K., Huang, I.-Y., and Budzynski, A. Z., Purification and characterization of hementin, a fibrinogenolytic protease from the leech Haementeria ghilianii,. Chromatogr. 502, 359, 1990. 

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