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  • Stem bromelain: amino acid sequence and implications for weak binding of cystatin.

Stem bromelain: amino acid sequence and implications for weak binding of cystatin.

FEBS letters (1989-04-24)
A Ritonja, A D Rowan, D J Buttle, N D Rawlings, V Turk, A J Barrett
ABSTRACT

The amino acid sequence of stem bromelain, the major cysteine proteinase from pineapple stem is described. It shows that the enzyme is a member of the papain superfamily of cysteine proteinases, but is not very closely related to any other known member of this group. The sequence shows mutation or deletion of several residues that have been conserved in cysteine proteinases examined previously, including Asn-175 (papain). We suggest that some of these changes have the effect of altering the active-site geometry of stem bromelain, and that this accounts for the resistance of the enzyme to inhibition by cystatins and E-64[L-3-carboxy-2,3-trans-epoxypropionylleucylamido(4-guanidino)b utane].

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Bromelain from pineapple stem, ≥3 units/mg protein
Sigma-Aldrich
Bromelain from pineapple stem, ≥4 units/mg protein, (chromatography purified)