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Aspartic proteinases of the A1 family are widely distributedamong plant species and have been purified from a varietyof tissues. They are most active at acidic pH, are specificallyinhibited by pepstatin A and contain two aspartic residuesindispensible for catalytic activity. The three-dimensionalstructure of two plant aspartic proteinases has been deter-mined, sharing significant structural similarity with otherknown structures of mammalian aspartic proteinases. Witha few exceptions, the majority of plant aspartic proteinasesidentified so far are synthesized with a prepro-domain andsubsequently converted to mature two-chain enzymes....
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Báo cáo khoa học: Structure and function of plant aspartic proteinases
