Regulation of Synthesis of Benzyl Alcohol Dehydrogenase in Acinetobacter calcoaceticus NCIB8250

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Abstract
Specific activity of benzyl alcohol dehydrogenase in C-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 N-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. Apparently, there were at least 2 types of repression. One was caused by phenylglyoxylate carboxy-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 2nd type of repression was observed during rapid growth or after the addition of compounds, such as succinate, which are rapidly and completely metabolized.

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