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.
PDF
http___www.sciencedirect.com_science__ob=MImg&_imagekey=B6WB5-4DPBX9M-BS-1&_cdi=6701&_user=512776&_orig=search&_coverDate=07_31_1986&_sk=997519998&view=c&wchp=dGLbVlb-zSkWb&md5=5ef06fd2e946b0.pdf - Published Version Restricted to Registered users only Download (1MB) | Request a copy |
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 |
---|---|
Publication: | Archives of Biochemistry and Biophysics |
Publisher: | Elsevier Science |
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.ac.in/id/eprint/21210 |
Actions (login required)
View Item |