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The importance of the Arg-Tyr peptide bond in the structure and activity of the immunosuppressive peptide tyrostat-3 (Tyr-Phe-Tyr) was demonstrated in the present study. The Arg-Tyr bond was cleaved more effectively by carboxypeptidase G2 than by other proteases tested, suggesting that BACE1, the only mammalian carboxypeptidase with a preference for the Arg-Tyr bond, is responsible for the cleavage. Although purified human BACE1 cleaves the Arg-Tyr bond effectively, cell surface BACE1 was expressed in 293 cells and was activated by the addition of a phosphorylation mimic, suggesting the existence of a regulatory mechanism. A peptide analog with an N-terminal phosphorylated Tyr inhibited efficiently the enzymatic activity of human BACE1. Given this and the observation that BACE1 is more active in brain than in blood, a strong possibility exists that BACE1 plays a pivotal role in the brain. Inhibition of BACE1 thus may offer a new therapeutic target for Alzheimer’s disease.Pediatrics Problem Solving

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