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Purification and properties of synephrinase from Arthrobacter synephrinum

Manne, Veeraswamy and Kutty, Krishnan R and Pillarisetti, Subba Rao V (1986) Purification and properties of synephrinase from Arthrobacter synephrinum. In: Archives of Biochemistry and Biophysics, 248 (1). 324 -334.

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Abstract

Synephrinase, an enzyme catalyzing the conversion of (−)-synephrine into p-hydroxyphenylacetaldehyde and methylamine, was purified to apparent homogeneity from the cell-free extracts of Arthrobacter synephrinum grown on (±)-synephrine as the sole source of carbon and nitrogen. A 40-fold purification was sufficient to produce synephrinase that is apparently homogeneous as judged by native polyacrylamide gel electrophoresis and has a specific activity of 1.8 μmol product formed /min/mg protein. Thus, the enzyme is a relatively abundant enzyme, perhaps comprising as much as 2.5% of the total protein. The enzyme essentially required a sulfhydryl compound for its activity. Metal ions like Mg2+, Ca2+, and Mn2+ stimulated the enzyme activity. Metal chelating agents, thiol reagents, denaturing agents, and metal ions like Zn2+, Hg2+, Ag1+, and Cu2+ inhibited synephrinase activity. Apart from (−)-synephrine, the enzyme acted upon (±)-octopamine and β-methoxysynephrine. Molecular oxygen was not utilized during the course of the reaction. The molecular mass of the enzyme as determined by Sephadex G-200 chromatography, was around 156,000. The enzyme was made up of four identical subunits with a molecular mass of 42,000.

Item Type: Journal Article
Additional Information: Copyright of this article belongs to Elsevier Science.
Department/Centre: Division of Biological Sciences > Biochemistry
Date Deposited: 03 Feb 2010 05:45
Last Modified: 19 Sep 2010 05:36
URI: http://eprints.iisc.ernet.in/id/eprint/21210

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