Regulation of synthesis of benzyl alcohol dehydrogenase in Acinetobacter calcoaceticus NCIB8250.
Specific activity of benzyl alcohol dehydrogenase in carbon-limited continuous cultures was at a maximum at a specific growth rate of 0.2 h-1, but fell off at lower and higher growth rates. The specific activity in nitrogen-limited cultures was always lower and was inversely proportional to growth rate. There was severe repression of benzyl alcohol dehydrogenase during metabolism of L(+)-mandelate or phenylglyoxylate in batch cultures. Synthesis of benzyl alcohol dehydrogenase was followed in experiments where various compounds, including a gratuitous inducer and an anti-inducer of the mandelate enzymes, were added to uninduced or pre-induced cultures and to constitutive and blocked mutants. The results led to the conclusion that there were at least two types of repression. One was caused by phenylglyoxylate carbon-lyase (or a compound synthesized co-ordinately with it), but not by the other mandelate enzymes or by L(+)-mandelate, phenylglyoxylate, benzaldehyde or benzoate. A second type of repression was observed during rapid growth or after the addition of compound such as succinate which are rapidly and completely metabolized.
D000150:Acinetobacter / Q000201:enzymology*; D000429:Alcohol Oxidoreductases / Q000037:antagonists & inhibitors / Q000096:biosynthesis*; D001547:Benzaldehydes / Q000494:pharmacology; D001592:Benzyl Alcohols / Q000378:metabolism; D002701:Chloramphenicol / Q000494:pharmacology; D000242:Cyclic AMP / Q000494:pharmacology; D004790:Enzyme Induction; D004794:Enzyme Repression; D005971:Glutamates / Q000378:metabolism; D006038:Glyoxylates / Q000494:pharmacology; D008333:Mandelic Acids / Q000494:pharmacology; D012293:Rifampin / Q000494:pharmacology
D001547:Benzaldehydes; D001592:Benzyl Alcohols; D005971:Glutamates; D006038:Glyoxylates; D008333:Mandelic Acids; D002701:Chloramphenicol; D000242:Cyclic AMP; D000429:Alcohol Oxidoreductases; D012293:Rifampin