Über die Spaltung von Threonin durchEscherichia coli
- 1 January 1953
- journal article
- research article
- Published by Walter de Gruyter GmbH in Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie
- Vol. 293 (Jahresband) , 234-238
- https://doi.org/10.1515/bchm2.1953.293.1.234
Abstract
Resting suspensions of E. coli deaminate threonine aerobically to ammonia and acetaldehyde. Pyridoxal phosphate, glutathione and adenosine-5-phosphate activate the reaction. The relative proportions of NH3 and acetaldehyde are affected by both activators and inhibitors (toluol, arsenite, azide), so that the processes leading to their formation probably are independent of each other.This publication has 4 references indexed in Scilit:
- d-SERINE DEHYDRASE OF NEUROSPORAJournal of Biological Chemistry, 1952
- Pyridoxal phosphate as a cofactor for serine and threonine deaminase of neurosporaArchives of Biochemistry and Biophysics, 1952
- SERINE AND THREONINE DEAMINASES OF ESCHERICHIA COLI: ACTIVATORS FOR A CELL-FREE ENZYMEJournal of Biological Chemistry, 1949
- THE RÔLE OF BIOTIN AND ADENYLIC ACID IN AMINO ACID DEAMINASESJournal of Biological Chemistry, 1948