Phosphonate Analogues of Carboxypeptidase A Substrates Are Potent Transition-State Analogue Inhibitors ?

@inproceedings{Basu2001PhosphonateAO,
  title={Phosphonate Analogues of Carboxypeptidase A Substrates Are Potent Transition-State Analogue Inhibitors ?},
  author={Amaresh Basu and Padmini Kedar and L Samuel and Wilson and Mukund J. Modak},
  year={2001}
}
Analogues of triand tetrapeptide substrates of carboxypeptidase A in which the scissile peptide linkage is replaced with a phosphonate moiety (-PO2--O-) were synthesized and evaluated as inhibitors of the enzyme. The inhibitors terminated with either L-lactate or L-phenyllactate [designated ( 0 ) A l a and (O)Phe, respectively] in the P,’ position. Transition-state analogy was shown for a series of 14 triand tetrapeptide derivatives containing the structure RCO-AlaP-(0)Ala [RCO-AP(0)A, AP… CONTINUE READING

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