Premium
Isolement d'une alcool déshydrogénase chez Rhizobium et rôle dans le métabolisme indolique
Author(s) -
RIGAUD JEAN,
TRINCHANT JEANCHARLES
Publication year - 1973
Publication title -
physiologia plantarum
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.351
H-Index - 146
eISSN - 1399-3054
pISSN - 0031-9317
DOI - 10.1111/j.1399-3054.1973.tb01169.x
Subject(s) - acetaldehyde , chemistry , sephadex , alcohol dehydrogenase , enzyme , ethanol , nad+ kinase , acetic acid , ammonium sulfate , rhizobium , biochemistry , alcohol , chromatography , gene
Rhizabium meliloti contains an alcohol dehydrogenase (E.C.1.1.1.1.) which can be isolated by breaking the cells. This soluble enzyme was purified 16.1‐fold by fractional precipitations with ammonium sulfate followed by gel filtration on Sephadex. The activity of the enzyme was tested with various aldehydes as substrates in the presence of NADH. Indole‐3‐acetaldehyde (IAAld) can be reduced to tryptophol (Tr‐ol), and the optimal pH for this reaction is ca. 6.5. The reaction can be reversed, and Tr‐ol is oxidised in the presence of NAD, but is was found that the yield was very poor; the optimal pH was ca. 8.6. This alcohol dehydrogenase is responsible for Tr‐ol formation in Rhizobium , but under our experimental conditions tryptophol cannot really be considered as a precursor of IAAld and indole‐3‐acetic acid.