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A protease is an enzyme that catalyzes proteolysis, breaking down proteins into smaller polypeptides or single amino acids, and spurring the formation of new protein products. They do this by cleaving the peptide bonds within proteins by hydrolysis, a reaction where water breaks bonds. Proteases are involved in many biological functions, including digestion of ingested proteins, protein catabolism, and cell signaling.
Tryptase is the most abundant secretory granule-derived serine proteinase contained in mast cells and has been used as a marker for mast cell activation. Club cells contain tryptase, which is believed to be responsible for cleaving the hemagglutinin surface protein of influenza A virus, thereby activating it and causing the symptoms of flu.
Cysteine proteases, also known as thiol proteases, are hydrolase enzymes that degrade proteins. These proteases share a common catalytic mechanism that involves a nucleophilic cysteine thiol in a catalytic triad or dyad.
Aspergillopepsin I is an enzyme. This enzyme catalyses the following chemical reaction
Microbial collagenase is an enzyme. This enzyme catalyses the following chemical reaction
Serine hydroxymethyltransferase (SHMT) is a pyridoxal phosphate (PLP) (Vitamin B6) dependent enzyme (EC 2.1.2.1) which plays an important role in cellular one-carbon pathways by catalyzing the reversible, simultaneous conversions of L-serine to glycine and tetrahydrofolate (THF) to 5,10-Methylenetetrahydrofolate (5,10-CH2-THF). This reaction provides the largest part of the one-carbon units available to the cell.
Actinidain is a type of cysteine protease enzyme found in fruits including kiwifruit, pineapple, mango, banana, figs, and papaya. This enzyme is part of the peptidase C1 family of papain-like proteases.
In molecular biology, Proteinase K is a broad-spectrum serine protease. The enzyme was discovered in 1974 in extracts of the fungus Parengyodontium album. Proteinase K is able to digest hair (keratin), hence, the name "Proteinase K". The predominant site of cleavage is the peptide bond adjacent to the carboxyl group of aliphatic and aromatic amino acids with blocked alpha amino groups. It is commonly used for its broad specificity. This enzyme belongs to Peptidase family S8 (subtilisin). The molecular weight of Proteinase K is 28,900 daltons.
Cathepsin X is an enzyme. This enzyme catalyses the following chemical reaction
α-L-Arabinofuranosidase is an enzyme with systematic name α-L-arabinofuranoside arabinofuranohydrolase. It catalyses the hydrolysis of terminal non-reducing α-L-arabinofuranoside residues in α-L-arabinosides
Cerevisin is an enzyme. This enzyme catalyses the following chemical reaction
Lysyl endopeptidase is an enzyme. This enzyme catalyses the following chemical reaction
Endopeptidase So is an enzyme. This enzyme catalyses the following chemical reaction
Zingibain, zingipain, or ginger protease is a cysteine protease enzyme found in ginger rhizomes. It catalyses the preferential cleavage of peptides with a proline residue at the P2 position. It has two distinct forms, ginger protease I (GP-I) and ginger protease II (GP-II).
Mucorpepsin is an enzyme. This enzyme catalyses the following chemical reaction
Candidapepsin is an enzyme. This enzyme catalyses the following chemical reaction
Serralysin is an enzyme. This enzyme catalyses the following chemical reaction
Bacillolysin is an enzyme. This enzyme catalyses the following chemical reaction
Trimerelysin I is an enzyme. This enzyme catalyses the following chemical reaction
The sedolisin family of peptidases are a family of serine proteases structurally related to the subtilisin (S8) family. Well-known members of this family include sedolisin ("pseudomonalisin") found in Pseudomonas bacteria, xanthomonalisin ("sedolisin-B"), physarolisin as well as animal tripeptidyl peptidase I. It is also known as sedolysin or serine-carboxyl peptidase. This group of enzymes contains a variation on the catalytic triad: unlike S8 which uses Ser-His-Asp, this group runs on Ser-Glu-Asp, with an additional acidic residue Asp in the oxyanion hole.
References
- ↑ Nakagawa, Y. (1970). "Alkaline proteinases from Aspergillus". Methods Enzymol. 19: 581–591. doi:10.1016/0076-6879(70)19046-x.
- ↑ Hayashi, K.; Terada, M. (1972). "Some characteristics of hydrolysis of synthetic substrates and proteins by the alkaline proteases from Aspergillus sojae". Agric. Biol. Chem. 36 (10): 1755–1765. doi: 10.1271/bbb1961.36.1755 .
- ↑ Turkovã J, Mikes O, Hayashi K, Danno G, Polgãr L (February 1972). "Alkaline proteinases of the genus Aspergillus". Biochimica et Biophysica Acta (BBA) - Protein Structure. 257 (2): 257–63. doi:10.1016/0005-2795(72)90277-2. PMID 4623338.
- ↑ Morihara K, Oka T, Tsuzuki H (November 1974). "Comparative study of various serine alkaline proteinases from microorganisms. Esterase activity against N-acylated peptide ester substrates". Archives of Biochemistry and Biophysics. 165 (1): 72–9. doi:10.1016/0003-9861(74)90143-x. PMID 4441086.
- ↑ Spadari S, Subramanian AR, Kalnitsky G (August 1974). "Highly restricted specificity of the serine proteinase aspergillopeptidase B". Biochimica et Biophysica Acta (BBA) - Protein Structure. 359 (2): 267–72. doi:10.1016/0005-2795(74)90224-4. PMID 4859351.
