FEBS Letters · 1989 · 142 citations · 23 references
Life SciencesBiochemistryMolecular BiologyEnzymologyPlant BiochemistryProtein BiochemistryEnzyme InhibitionPlant EnzymesStructural EnzymologyAmino Acid N-substitutionsAmino Acid Sequence EffectsAmino Acid Sequence-structure RelationshipsCysteine Protease MechanismCysteine Proteases
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].
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A gas-liquid solid phase peptide and protein sequenator.
Rodney M. Hewick, Michael W. Hunkapiller, Leroy Hood et al. · Journal of Biological Chemistry · 1981 · 2.2K citations · Full text
A. John Barrett, A A Kembhavi, M A Brown et al. · Biochemical Journal · 1982 · 1K citations · Full text
Joost P.H. Drenth, J.N. Jansonius, Roelof Koekoek et al. · Nature · 1968 · 480 citations