Characterization of biosynthetic enzymes for ectoine as a compatible solute in a moderately halophilic eubacterium, Halomonas elongata.

@article{Ono1999CharacterizationOB,
  title={Characterization of biosynthetic enzymes for ectoine as a compatible solute in a moderately halophilic eubacterium, Halomonas elongata.},
  author={Hiroshi Ono and Kazuhisa Sawada and N Khunajakr and Tao Tao and Mami Yamamoto and M Hiramoto and Atsuhiko Shinmyō and Mitsuo Takano and Yoshikatu Murooka},
  journal={Journal of bacteriology},
  year={1999},
  volume={181 1},
  pages={91-9}
}
1,4,5,6-Tetrahydro-2-methyl-4-pyrimidinecarboxylic acid (ectoine) is an excellent osmoprotectant. The biosynthetic pathway of ectoine from aspartic beta-semialdehyde (ASA), in Halomonas elongata, was elucidated by purification and characterization of each enzyme involved. 2,4-Diaminobutyrate (DABA) aminotransferase catalyzed reversively the first step of the pathway, conversion of ASA to DABA by transamination with L-glutamate. This enzyme required pyridoxal 5'-phosphate and potassium ions for… CONTINUE READING
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