title: Primary structure of streptococcal proteinase. III. Isolation of cyanogen bromide peptides: complete covalent structure of the polypeptide chain.
abstract: The following sequence has been derived for streptococcal proteinase. (See article). The sequence permits the assignment of the single cysteine residue essential for catalytic action at position 47 from the NH2 terminus of the protein. The tryptophan residue at the binding site of the enzyme is at position 214. A histidine residue at position 195 has been assigned as the catalytically important entity in the molecule. Streptococcal proteinase and papain, an enzyme with similar properties, are compared with respect to structure and function.
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D001665:Binding Sites; D003488:Cyanogen Bromide; D003545:Cysteine / Q000032:analysis; D006639:Histidine / Q000032:analysis; D010206:Papain; D010446:Peptide Fragments / Q000032:analysis; D010447:Peptide Hydrolases; D011487:Protein Conformation; D013291:Streptococcus / Q000201:enzymology*; D014357:Trypsin
chemical_list: D000596:Amino Acids; D010446:Peptide Fragments; D006639:Histidine; D010447:Peptide Hydrolases; D014357:Trypsin; D010206:Papain; D003545:Cysteine; D003488:Cyanogen Bromide