Repozytorium

The unusual behavior of the inhibitor S(+)(1-amino-2-phenylethyl)phosphonic acid towards carboxypeptidase A.

Autorzy

Wojciech Bal

I. Bertini

Henryk Kozłowski

R. Monnanni

A. Scozzafava

Zdzisław Siatecki

Rok wydania

1990

Czasopismo

Journal of Inorganic Biochemistry

Numer woluminu

40

Strony

227-235

DOI

10.1016/0162-0134(90)80056-4

Kolekcja

Naukowa

Język

Angielski

Typ publikacji

Artykuł

Streszczenie

The molecule (1-Amino-2-phenylethyl)phosphonic acid is shown to inhibit the enzymatic activity of carboxypeptidase A. Through the spectroscopic investigation of the cobalt(II) substituted enzyme we propose that it binds the enzyme in the 1:1 ratio directly at the metal, probably through the phosphate group like phosphate itself. The aromatic group is proposed to sit in the so-called S1 hydrophobic pocket. This is a unique behavior among the inhibitors of the enzyme. The S′1 site is still available in the binary adduct so that a ternary complex can be obtained with molecules like L-Phenylalanine, which enter that site.

Adres publiczny

https://doi.org/10.1016/0162-0134(90)80056-4

Strona internetowa wydawcy

http://www.elsevier.com

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