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SECONDARY STRUCTURE OF SOME ASPARTYL PROTEINASES
Author(s) -
YADA R. Y.,
NAKAI S.
Publication year - 1986
Publication title -
journal of food biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.507
H-Index - 47
eISSN - 1745-4514
pISSN - 0145-8884
DOI - 10.1111/j.1745-4514.1986.tb00098.x
Subject(s) - chymosin , pepsin , chemistry , protein secondary structure , enzyme , aspartic acid , protein tertiary structure , proteinase k , amino acid residue , biochemistry , chromatography , amino acid , peptide sequence , gene
ABSTRACT A structural study of some aspartyl proteinases was undertaken. Secondary structure prediction methods indicate that chymosin, pepsin, penicillopepsin and Mucor miehei proteinase have relatively high proportions of β‐sheet with active site aspartic acid residues located in β‐turn regions. Secondary structure determination from far‐UV CD spectral data support the above finding that the aspartyl proteinases have a high proportion of β‐sheet. The proportion of β‐sheet generally decreased at pH values greater than 6.3. More extensive unfolding occurred with pepsin and penicillopepsin than chymosin , Mucor miehei proteinase , Mucor pusillus proteinase and Endothia parasitica proteinase in the neutral to alkaline pH range. Results obtained from the near‐UV CD spectra of the aspartyl proteinases indicate a change in spectra in the neutral to alkaline pH range which suggests the importance of aromatic groups to tertiary structure stability.