Papain-like cysteine proteases.
The name "cysteine protease" refers to the protease's nucleophilic cysteine residue that forms a covalent bond with the carbonyl group of the scissile peptide bond in substrates. The papain-like cysteine proteases, classified as the "C1 family" are the most predominant cysteine proteases. These proteases are found in viruses, plants, primitive parasites, invertebrates, and vertebrates alike. Mammalian papain-like cysteine proteases are also known as cathepsins. This unit discusses cathepsins, and their subcellular and tissue localization, catalytic mechanism, and substrate specificity. Several tables illustrate the properties of the various cathepsins.
Brömme
D
D
Mount Sinai School of Medicine, New York, New York, USA.
D000595:Amino Acid Sequence; D000818:Animals; D002384:Catalysis; D002403:Cathepsins / Q000145:classification / Q000235:genetics* / Q000378:metabolism*; D003546:Cysteine Endopeptidases / Q000145:classification / Q000235:genetics / Q000378:metabolism; D004721:Endoplasmic Reticulum / Q000201:enzymology; D019143:Evolution, Molecular; D016326:Extracellular Matrix Proteins / Q000378:metabolism; D006801:Humans; D008247:Lysosomes / Q000201:enzymology; D008954:Models, Biological; D008969:Molecular Sequence Data; D009369:Neoplasms / Q000201:enzymology / Q000378:metabolism / Q000473:pathology; D010802:Phylogeny; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity
D016326:Extracellular Matrix Proteins; D002403:Cathepsins; D003546:Cysteine Endopeptidases