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Bisfunction of propionic acid on purified rat liver β‐ureidopropionase
Author(s) -
Kikugawa Mariko,
Fujimoto Shigeko,
Mizota Chizuru,
Tamaki Nanaya
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)81153-0
Subject(s) - chemistry , biochemistry , chromatography
Propionic acid and isobutyric acid, which are structural analogues of N ‐carbamoyl‐β‐alanine and N ‐carbamoyl‐β‐aminoisobutyric acid, respectively, acted as an allosteric activator as well as a competitive inhibitor of purified rat liver β‐ureidopropionase. Propionic acid and isobutyric acid had a K i value of approx. 0.3 mM at pH 7.0. The Hill coefficient for N ‐carbamoyl‐β‐alanine was 2.0, but the cooperativity decreased to 1.0 in the presence of 1 mM propionic acid. The K value towards N ‐carbamoyl‐β‐alanine was calculated to be 0.17 mM from Hill plots and the K m value was determined to be 0.06 mM from replots of the apparent K m vs propionic acid.

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