Abstract
A newly isolated gram-negative bacterium, possibly Brevundimonas diminuta, utilised d,l-vanillylmandelate (d,l-VMA) as a sole carbon and energy source. The organism converted d,l-VMA to vanillylglyoxylate using a soluble NAD-dependent dehydrogenase specific for d-VMA and a dye-linked, membrane-associated l-VMA dehydrogenase. Vanillylglyoxylate was further metabolised by decarboxylation, dehydrogenation and demethylation to protocatechuate. A 4,5-dioxygenase cleaved protocatechuate to 2-hydroxy-4-carboxymuconic semialdehyde. Partially purified d-VMA dehydrogenase exhibited optimal activity at 30° C and pH 9.5 and had an apparent K m for d-VMA of 470 μM. Although induced by several substituted mandelates, the enzyme had a narrow substrate specificity range with virtually no activity towards d-mandelate. Such properties render the enzyme of potential use in both diagnostic and biosynthetic applications.
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Received: 23 January 1996 / Accepted: 9 April 1996
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Turner, J., Allison, N. & Fewson, C. Metabolic characterisation of a novel vanillylmandelate-degrading bacterium. Arch Microbiol 166, 252–259 (1996). https://doi.org/10.1007/s002030050381
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DOI: https://doi.org/10.1007/s002030050381