Nuclear‐Magnetic‐Resonance Studies of Carboxypeptidase B: Binding of Inhibitors to the Manganese Enzyme

Nava ZISAPEL*, Mordechai SOKOLOVSKY, Gil NAVON

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

Longitudinal and transverse proton relaxation rates of water in solutions of porcine manganese carboxypeptidase B have been measured in the presence of various competitive inhibitors by pulse nuclear magnetic reasonance (NMR) spectrometry. The inhibition constant of Mn‐carboxypeptidase activity by l‐argininic acid and acetyl‐l‐arginine was in agreement with the equilibrium constant obtained by the NMR method, indicating similar and specific binding of the inhibitors to the active site of the manganese enzyme. Titration of the water bound to the metal ion revealed the presence of one water molecule which could be displaced from the sphere of the manganese ion by various inhibitors. The structural features of the inhibitors required for this displacement as well as the mode of interaction is described.

Original languageEnglish
Pages (from-to)487-492
Number of pages6
JournalEuropean Journal of Biochemistry
Volume52
Issue number3
DOIs
StatePublished - Apr 1975

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