dormouse (Member)
04-24-00 12:47
No 108788
      Methylamine from yer friendly Arthrobacter synephrinum -dwarfer  Bookmark   


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Author  Topic:   Methylamine from yer friendly Arthrobacter synephrinum 
dwarfer
Member   posted 08-31-99 08:36 PM          
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Worlock, whose foeted, fervid steps have already been referenced (and whose trail I am destined to follow, as in an ever repeating cyclic dream, never catching up with the Wraith from the West) , posited the dubious conjecture that indigenous microbes or molds may actually produce methamphetamine when ephedra cuttings are allowed to mold and semi-decompose in anaerobic (maybe?) conditions inside closed plastic bags with a little water.
Interesting, but unlikely: said I: the euphoria he and some friends realized when processing the bags of material probably arose from another source. (What, I can only conjecture!)

Then, while sniffing along the synephrine trail (trying to get my sinus opened!) along comes this little mard: kinda makes me wonder.

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Conversion of (+/-)-synephrine into p-hydroxyphenylacetaldehyde by Arthrobacter synephrinum. A novel enzymic reaction.

Veeraswamy M, Devi NA, Kutty RK, Rao PV

A partically purified enzyme from Arthrobacter synephrinum was found to catalyse the conversion of (+/-)-synphrine into p-hydroxyphrenylacetaldehyde and methylamine. The enzyme is highly specific for synephrine and is distinctly different from monoamine oxidase.


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The Biochemical Society, London 1976

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Anybody have access to this document for further information??

Thanks!

dwarfer


 
plazmid
Junior Member   posted 09-09-99 07:26 PM          
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Here's another ref:
TI: Purification and properties of synephrinase from Arthrobacter synephrinum.
AU: MANNE-V; KUTTY-K-R; PILLARISETTI-S-R-V
SO: ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS 248(1):324-334.
PY: 1986
LA: English
AB: 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 aspecific activity of 1.8 mu-mol 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 Mg-2+, Ca-2+, and Mn-2+ stimulated the enzyme activity.
Metal chelating agents, thiol reagents, denaturing agents, and metal ions like Zn-2+, Hg-2+, Ag-1+, and Cu-2+ inhibited synephrinase activity. Apart from (-)-synephrine, the enzyme acted upon (+-)-octopamine and beta-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.

.... in short, there's a boat-load of the enzyme in the bacteria for a secondary metabolism pathway. However, the bacteria itself may be a bitch to grow, and the methylamine would be a drag to separate from a reaction mixture. Still, kinda neat.
Just wait till I find the bloody enzymes that make safrole. THEN, we'll talk.


rev drone
Member   posted 09-13-99 12:41 PM          
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Out of curiosity, why is it relevant? Seems like a rather expensive and elaborate way of making tiny amounts of methylamine...
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-the good reverend drone


 
dwarfer
Member   posted 09-13-99 08:12 PM          
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Two reasons I thought it was relevant.
1. It's novel, at least to me; and should it be possible for culturing methylamine in a home-base brewerey, it may be productive of more than tiny amounts.

2. It was a "follow on" reference to my reaction to Worlock's ideation about meth (or some similar euphoriant) having been produced by fungus, or enzymes, on ephedra.

What seemed somewhat nonesensical at first blush appeared less so after reading this material.


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