Open AccessThe biosynthesis of ectoine
Author(s) -
Peters Petra,
Galinski E.A.,
Trüper H.G.
Publication year - 1990
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1990.tb03815.x
Subject(s) - ectoine , biosynthesis , chemistry , biology , biochemistry , gene , osmoprotectant , amino acid , proline
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.