The biosynthesis of ectoine

The biosynthetic pathway of the novel compatible solute ectoine (1,4,5,6‐tetrahydro‐2‐methyl‐4‐pyrimidine carboxylic acid) was studied in the two extremely halophilic eubacteria Ectothiorhodospira halochloris and Halomonas elongata. The pathway starts with the phosphorylation of l‐aspartate and shar...

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Bibliographic Details
Published in:FEMS microbiology letters 1990-09, Vol.71 (1‐2), p.157-162
Main Authors: Peters, Petra, Galinski, E.A., Trüper, H.G.
Format: Article
Language:English
Subjects:
Compatible solute
Ectoine biosynthesis
Ectothiorhodospira halochloris
Halomonas elongata
Tetrahydropyrimidine
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Summary:The biosynthetic pathway of the novel compatible solute ectoine (1,4,5,6‐tetrahydro‐2‐methyl‐4‐pyrimidine carboxylic acid) was studied in the two extremely halophilic eubacteria Ectothiorhodospira halochloris and Halomonas elongata. The pathway starts with the phosphorylation of l‐aspartate and shares its first two enzymatic steps with the biosynthesis of amino acids of the aspartate family: aspartokinase and l‐aspartate‐β‐semialdehyde dehydrogenase. Evidence is presented for the presence of the enzymes l‐diaminobutyric acid transaminase and l‐diaminobutyric acid acetyl transferase and for the new enzyme the ring‐forming ectoine synthase.
ISSN:0378-1097
1574-6968
DOI:10.1111/j.1574-6968.1990.tb03815.x