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Papain

Papain is a cysteine protease enzyme present in papaya and mountain papaya. Papain belongs to a family of related proteins with a wide variety of activities, including endopeptidases, aminopeptidases, dipeptidyl peptidases and enzymes with both exo- and endo-peptidase activity. It consists of 212 amino acids stabilized by 3 disulfide bridges. Its 3D structure consists of 2 distinct structural domains with a cleft between them. This cleft contains the active site, which contains a catalytic triad that has been likened to that of chymotrypsin. Its catalytic triad is made up of 3 amino acids cysteine-25, histidine-159, and asparagine-158. Papain breaks peptide bonds involve deprotonation of Cys-25 by His-15. It is also used as an ingredient in various enzymatic debriding preparations, notably Accuzyme. It can also be found as an ingredient in some toothpastes or mints as teeth-whitener. Its whitening effect in toothpastes and mints however is minimal, because the papain is present in low concentrations. Papain is the main ingredient of Papacarie, a gel used for chemomechanical dental caries removal.

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Pectinase

Pectinase is a general term for enzymes, such as pectolyase, pectozyme and polygalacturonase, commonly referred to in brewing as pectic enzymes. These break down pectin, a polysaccharide substrate that is found in the cell walls of plants. pectinases have an optimum temperature and pH at which they are most active. For example, a commercial pectinase might typically be activated at 45 to 55 °C and work well at a pH of 4.5 to 5.5

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Pelitinib

Pelitinib is a 3-cyanoquinoline pan-ErbB tyrosine kinase inhibitor with potential antineoplastic activity. Pelitinib irreversibly binds covalently to epidermal growth factor receptors (EGFR) ErbB-1, -2 and -4, thereby inhibiting receptor phosphorylation and signal transduction and resulting in apoptosis and suppression of proliferation in tumor cells that overexpress these receptors. Pelitinib inhibits EGF-induced phosphorylation of EGF-R and the growth of tumors that overexpress EGF-R in animal models.

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Penicillin G Acylase

Penicillin G Acylase (EC 3.5.1.11) is a enzyme derived from Escherichia coli.Penicillin G acylase has many applications, from the hydrolysis of penicillin G (production of 6-aminopenicillanic acid) to the synthesis of semi-synthetic antibiotics.It is widely used in synthesis of antibiotics such as ampicillin, amoxicillin, cloxacillin, cephalexin, and cefatoxime.

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Peptide-methionine (R)-S-oxide reductase

Peptide-methionine (R)-S-oxide reductase (EC 1.8.4.12) is an enzyme that belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with a disulfide as acceptor. The systematic name of this enzyme class is peptide-methionine:thioredoxin-disulfide S-oxidoreductase.

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Peptidyl transferase

Peptidyl transferase is an aminoacyltransferase (EC 2.3.2.12) as well as the primary enzymatic function of the ribosome which forms peptide links between adjacent amino acids using tRNAs during the translation process of protein biosynthesis. Peptidyl transferases are not limited to translation but there are relatively few enzymes with this function.

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Perillyl-alcohol dehydrogenase

Perillyl-alcohol dehydrogenase (EC 1.1.1.144) is an enzyme that belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is perillyl-alcohol:NAD+ oxidoreductase .This enzyme participates in limonene and pinene degradation.

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Phenylacetaldehyde dehydrogenase

Phenylacetaldehyde dehydrogenase (EC 1.2.1.39) is an enzyme that belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is phenylacetaldehyde:NAD+ oxidoreductase. This enzyme participates in phenylalanine metabolism and styrene degradation.

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Phenylacetyl-Coenzyme A

Phenylacetyl-Coenzyme A is an enzyme that catalyzes the chemical reaction.

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Phenylalanine dehydrogenase

Phenylalanine dehydrogenase (EC 1.4.1.20) is an enzyme that belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-phenylalanine:NAD+ oxidoreductase (deaminating). This enzyme participates in phenylalanine metabolism and phenylalanine, tyrosine and tryptophan biosynthesis.

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