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- W1998086075 abstract "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 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 second type of repression was observed during rapid growth or after the addition of compounds such as succinate which are rapidly and completely metabolized." @default.
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- W1998086075 date "1977-11-01" @default.
- W1998086075 modified "2023-09-25" @default.
- W1998086075 title "Regulation of Synthesis of Benzyl Alcohol Dehydrogenase in Acinetobacter calcoaceticus NCIB8250" @default.
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- W1998086075 doi "https://doi.org/10.1099/00221287-103-1-127" @default.
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