Metabolic characterisation of a novel vanillylmandelate-degrading bacterium |
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Authors: | Janet E Turner N Allison Charles A Fewson |
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Institution: | (1) Microbial Antigens Department, Centre for Applied Microbiology & Research, Porton Down, Salisbury, Wiltshire SP4 OJG, UK Tel. +44-1980-612267; Fax +44-1980-611096, GB;(2) West Medical Building, University of Glasgow, Glasgow G12 8QQ, UK, GB |
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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.
Received: 23 January 1996 / Accepted: 9 April 1996 |
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Keywords: | Brevundimonas sp Demethylation Dioxygenase Mandelic acid NAD-dependent dehydrogenase Vanillylmandelic acid |
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