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Degradation of (+/-)-synephrine by Arthrobacter synephrinum. Oxidation of 3,4-dihydroxyphenylacetate to 2-hydroxy-5-carboxymethyl-muconate semialdehyde.

Kutty, R Krishnan and Devi, N Abitha and Veeraswamy, M and Ramesh, S and Rao, PV Subba (1977) Degradation of (+/-)-synephrine by Arthrobacter synephrinum. Oxidation of 3,4-dihydroxyphenylacetate to 2-hydroxy-5-carboxymethyl-muconate semialdehyde. In: Biochemical Journal, 167 (1). pp. 163-170.

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Official URL: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC118363...

Abstract

1. Cell-free extracts of Arthrobacter synephrinum catalyse the oxidation of 3,4-dihydroxy-phenylacetate. 2. The product of oxidation was characterized as 2-hydroxy-5-carboxymethylmuconate semialdehyde from its chemical behaviour as well as from nuclear-magnetic-resonance spectra. 3. A 3,4-dihydroxyphenylacetate 2,3-dioxygenase (EC 1.13.11.15) was partially purified from A. synephrinum. 4. The enzyme had a Km of 25 micrometer towards its substrate and exhibited typical Michaelis-Menten kinetics. 5. The enzyme also catalysed the oxidation of 3,4-dihydroxymandelate and 3,4-dihydroxyphenylpropionate, at reaction rates of 0.5 and 0.04 respectively of that for 3,4-dihydroxyphenylacetate. 6. The enzyme was sensitive to treatment with thiol-specific reagents. 7. The molecular weight of the enzyme as determined by Sephadex G-200 chromatography was approx. 282000.

Item Type: Journal Article
Publication: Biochemical Journal
Publisher: Portland Press
Additional Information: Copyright of this article belongs to Portland Press.
Department/Centre: Division of Biological Sciences > Biochemistry
Date Deposited: 21 Jan 2010 10:23
Last Modified: 19 Sep 2010 05:49
URI: http://eprints.iisc.ac.in/id/eprint/24326

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