Kinetic fractionation of stable nitrogen isotopes during amino acid transamination
Abstract
This study evaluates a kinetic isotope effect involving 15N, during the transamination reactions catalyzed by glutamic oxalacetic transaminase. During the transfer of amino nitrogen from glutamic acid to oxaloacetate to form aspartic acid, 14NH 2 reacted 1.0083 times faster than 14NH 2. In the reverse reaction transferring NH 2 from aspartic acid to α-ketoglutarate, 14NH 2 was incorporated 1.0017 times faster than 15NH 2. Knowledge of the magnitude and sign of these isotope effects will be useful in the interpretation of the distribution of 15N in biological and geochemical systems.
- Publication:
-
Geochimica et Cosmochimica Acta
- Pub Date:
- October 1986
- DOI:
- 10.1016/0016-7037(86)90068-2
- Bibcode:
- 1986GeCoA..50.2143M