Über den enzymatischen Abbau und Aufbau der Glutaminsäure III. In Bacterium Coli
- 1 January 1938
- journal article
- research article
- Published by Walter de Gruyter GmbH in Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie
- Vol. 255 (1-3) , 14-26
- https://doi.org/10.1515/bchm2.1938.255.1-3.14
Abstract
Animal tissues contained an apodehydrase which catalysed the reversible reaction: glutamic acid, + codehydrase iminoglutaric acid + dihydro-code-hydrase. In aq. soln. iminoglutaric acid and [image] keto-glutario acid were in equilibrium: iminoglutaric acid + water ketoglutaric acid + ammonia. That these reactions were reversible was detd. spectro-photometrically. This synthesis in B. coli of an amino acid by the addition of ammonia to a keto acid was similar to that in animals. The glutamic acid apodehydrase was prepared by extracting Bacterium coli that had been dehydrated in acetone and solid CO2. The glutamic acid dehydrase of B. coli, similar to that of yeast, consisted of an apodehydrase which combined specifically with codehydrase II (but not with codehydrase I) to form an active holohydrase. The specific substrate was 1( +) glutamic acid. Synonyms for codehydrase II were, Warburg''s co-ferment or triphospho-pyridine-nucleotide. For codehydrase I: cozymase or diphospho-pyridin-nucleatid.This publication has 2 references indexed in Scilit:
- Coenzyme factor—a new oxidation catalystBiochemical Journal, 1938
- On lactic dehydrogenaseBiochemical Journal, 1928