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Science 13 July 1990:
Vol. 249. no. 4965, pp. 160 - 162
DOI: 10.1126/science.2371563
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Articles

Science, Vol 249, Issue 4965, 160-162
Copyright © 1990 by American Association for the Advancement of Science

articles

Methyl chloride transferase: a carbocation route for biosynthesis of halometabolites

AM Wuosmaa and LP Hager

Roger Adams Laboratory, Department of Biochemistry, University of Illinois, Urbana 61801.

Enzymatic synthesis of methyl halides through an S-adenosyl methionine transfer mechanism has been detected in cell extracts of Phellinus promaceus (a white rot fungus), Endocladia muricata (a marine red algae), and Mesembryanthemum crystallium (ice plant). This mechanism represents a novel pathway for the formation of halometabolites. The Michaelis constants for chloride and bromide ion and for S-adenosyl methionine in the reaction have been determined for the enzyme from E. muricata. A recent survey of marine algae indicates that there may be a broad distribution of this enzyme among marine algae.


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