A new bacterial alcohol dehydrogenase active on degraded lignin and several low molecular weight aromatic compounds.
A new intracellular bacterial dehydrogenase has been purified. It was active in the reversible reduction by NADH of conjugated carbonyl groups in partially degraded lignin. It was also active on various aromatic aldehydes such as vanillin, syringaldehyde and cinnamaldehyde, but had no effect on acetovanillone and lignin models carrying a conjugated ketone. It is proposed that this enzyme functions as a broadly specific lignin dehydrogenase at the level of aldehydic groups that are present in the lignin preparations.
Pelmont
J
J
Laboratoire de Biochimie des Micro-organismes, Université Joseph Fourier, Grenoble, France.
Tournesac
C
C
Mliki
A
A
Barrelle
M
M
Beguin
C
C
D000171:Acrolein / Q000031:analogs & derivatives; D000426:Alcohol Dehydrogenase / Q000302:isolation & purification / Q000378:metabolism*; D000447:Aldehydes; D001547:Benzaldehydes; D008031:Lignin; D009243:NAD; D010084:Oxidation-Reduction; D011549:Pseudomonas / Q000201:enzymology*; D013056:Spectrophotometry, Ultraviolet; D013379:Substrate Specificity
D000447:Aldehydes; D001547:Benzaldehydes; D009243:NAD; D000171:Acrolein; D008031:Lignin; C100058:vanillin; D000426:Alcohol Dehydrogenase; C012843:cinnamaldehyde