[Thiol peptide hydrolases from animal tissues, their structure and function].
Data on properties, structure and biological functions of a variety of thiol (cysteine) peptide hydrolases from animal tissues have been summarized. This large group of diverse intracellular enzymes involves both endo- and exopeptidases. Best studied are lysosomal thiol peptide hydrolases: cathepsins B, H and L, the primary structure of which is deciphered. They present a family of homologous proteins, structurally similar to papain. Ca2+-dependent neutral proteinases is another family of related proteins. The biological functions of various thiol peptide hydrolases are considered: their participation in protein turnover, post-translational processing, regulation of unidirectional biological processes and metabolic refolding. Data on endogenous inhibitors of thiol peptide hydrolases and on regulation of enzymic activity are presented.
D000595:Amino Acid Sequence; D000818:Animals; D003546:Cysteine Endopeptidases; D015853:Cysteine Proteinase Inhibitors; D010450:Endopeptidases / Q000032:analysis* / Q000502:physiology; D011480:Protease Inhibitors / Q000032:analysis; D011487:Protein Conformation; D011506:Proteins / Q000032:analysis; D013045:Species Specificity; D013438:Sulfhydryl Compounds / Q000032:analysis; D014018:Tissue Distribution
D015853:Cysteine Proteinase Inhibitors; D011480:Protease Inhibitors; D011506:Proteins; D013438:Sulfhydryl Compounds; D010450:Endopeptidases; D003546:Cysteine Endopeptidases
Tiolovye peptidgidrolazy zhivotnykh tkaneĭ, ikh struktura i funktsii.