Selective cleavage of glycyl bonds by papaya proteinase IV
1990; Wiley; Volume: 260; Issue: 2 Linguagem: Inglês
10.1016/0014-5793(90)80101-n
ISSN1873-3468
AutoresDavid J. Buttle, Anka Ritonja, Laurence H. Pearl, Vito Türk, A. John Barrett,
Tópico(s)Pineapple and bromelain studies
ResumoThe specificity of papaya proteinase IV (PPIV) has been examined with small substrates and a protein. With both classes of substrate, the enzyme shows a marked selectivity for cleaving glycyl bonds. Boc‐Ala‐Ala‐Gly‐NHPhNO 2 is a convenient substrate for routine assays that discriminate well against chymopapain, the most common contaminant of PPIV. Sixteen cleavage points in β‐trypsin were identified, of which 13 are glycyl bonds. Tentative suggestions are made as to the reasons for lack of cleavage of some other glycyl bonds. The structure of PPIV has been modelled on that of papain, and we suggest that the replacement of the highly conserved residues Gly‐65 and Gly‐23 by arginine and glutamic acid, respectively, can account for the specificity of PPIV.
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