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J. Biol. Chem., Vol. 275, Issue 29, 22196-22201, July 21, 2000
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From the § Danisco Cultor Innovation, Kantvik,
Sokeritehtaantie 20, FIN-02460 Kantvik, Finland
Glycine betaine is a compatible solute, which is
able to restore and maintain osmotic balance of living cells. It is
synthesized and accumulated in response to abiotic stress. Betaine acts
also as a methyl group donor and has a number of important applications including its use as a feed additive. The known biosynthetic pathways of betaine are universal and very well characterized. A number of
enzymes catalyzing the two-step oxidation of choline to betaine have
been isolated. In this work we have studied a novel betaine biosynthetic pathway in two phylogenically distant extreme halophiles, Actinopolyspora halophila and Ectothiorhodospira
halochloris. We have identified a three-step series of
methylation reactions from glycine to betaine, which is catalyzed by
two methyltransferases, glycine sarcosine methyltransferase and
sarcosine dimethylglycine methyltransferase, with partially overlapping
substrate specificity. The methyltransferases from the two organisms
show high sequence homology. E. halochloris
methyltransferase genes were successfully expressed in
Escherichia coli, and betaine accumulation and improved salt tolerance were demonstrated.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF216281, AF216282, and AF216283.
Extreme Halophiles Synthesize Betaine from Glycine by
Methylation*
,, and
*
This work was supported in part by the Finnish National
Technology Agency (TEKES).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Currrent address: Helsinki University of Technology, Laboratory of
Bioprocess Engineering, P. O. Box 6100, FIN-02015 HUT, Finland.
¶
Current address: Haartman Institute, Dept. of Virology, P. O.
Box 21, FIN-00014 University of Helsinki, Finland.
To whom correspondence should be addressed. Tel.:
358-9-2974619; Fax: 358-9-2982203; E-mail:
Tapani.Reinikainen@danisco.com.
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