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. 1970 Feb;116(4):689–692. doi: 10.1042/bj1160689

A reinvestigation of residues 64–68 and 175 in papain. Evidence that residues 64 and 175 are asparagine

S S Husain 1, G Lowe 1
PMCID: PMC1185414  PMID: 5435495

Abstract

The tryptophan-containing peptides were isolated from the chymotryptic digest of S-carboxymethylated papain. Residue 175, which is strongly hydrogen-bonded to the active-site histidine residue in the tertiary structure of papain, is asparagine, confirming the work of Kimmel, Rogers & Smith (1965). Its function is probably to maintain the orientation and tautomeric state of the imidazole ring of histidine-159. The amino acid sequence predicted from the electron-density map of papain for residues 64–68 was confirmed, but residue 64 is asparagine, not aspartic acid. This residue, which is about 10 Å from the thiol group of the active-site cysteine-25, cannot therefore be a site of electrostatic attraction for substrates of basic amino acids.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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