J. Biol. Chem., Vol. 262, Issue 4, 1461-1467, 02, 1987
Amino acid sequence of rhizopuspepsin isozyme pI 5
R Delaney, RN Wong, GZ Meng, NH Wu and J Tang
The complete amino acid sequence of an aspartic protease from Rhizopus
chinensis, rhizopuspepsin isozyme pI 5, has been determined. Partial
sequences were first obtained from the isolated isozyme by a combination of
chemical and proteolytic enzyme cleavages, peptide purifications, and Edman
degradations. About one-half of the sequence was revealed by this approach.
To complete the amino acid sequence, a cDNA library of R. chinensis in
pBR322 was constructed. An oligonucleotide probe was synthesized based on
the sequence Trp-Trp-Gly- Ile-Thr, and about 40 positive clones were
identified by colony hybridization. A clone, 33E2, which had an insert size
of about 1.1 kilobase pairs, was found to contain the entire coding region
of rhizopuspepsin isozyme pI 5. The sequence of rhizopuspepsin contains 325
amino acid residues. The alignment of the rhizopuspepsin sequence against
other aspartic proteases revealed expected homology, with the closest
similarity to penicillopepsin which shares 39% identical residues. Porcine
pepsin shares about 36% identical residues with rhizopuspepsin.
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