Ectoine synthase
In enzymology, an ectoine synthase (EC 4.2.1.108) is an enzyme that catalyzes the chemical reaction
- N4-acetyl-L-2,4-diaminobutanoate L-ectoine + H2O
Ectoine synthase | |||||||||
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Identifiers | |||||||||
EC number | 4.2.1.108 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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Hence, this enzyme has one substrate, N4-acetyl-L-2,4-diaminobutanoate, and two products, L-ectoine and H2O.
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is N4-acetyl-L-2,4-diaminobutanoate hydro-lyase (L-ectoine-forming). Other names in common use include N-acetyldiaminobutyrate dehydratase, N-acetyldiaminobutanoate dehydratase, L-ectoine synthase, EctC, and 4-N-acetyl-L-2,4-diaminobutanoate hydro-lyase (L-ectoine-forming). This enzyme participates in glycine, serine and threonine metabolism.
References
- Peters P, Galinski EA, Truper HG (1990). "The biosynthesis of ectoine". FEMS Microbiol. Lett. 71 (1–2): 157–162. doi:10.1111/j.1574-6968.1990.tb03815.x.
- Ono H, Sawada K, Khunajakr N, et al. (1999). "Characterization of biosynthetic enzymes for ectoine as a compatible solute in a moderately halophilic eubacterium, Halomonas elongata". J. Bacteriol. 181 (1): 91–9. PMC 103536. PMID 9864317.
- Kuhlmann AU, Bremer E (2002). "Osmotically regulated synthesis of the compatible solute ectoine in Bacillus pasteurii and related Bacillus spp". Appl. Environ. Microbiol. 68 (2): 772–83. doi:10.1128/AEM.68.2.772-783.2002. PMC 126723. PMID 11823218.
- Louis P, Galinski EA (1997). "Characterization of genes for the biosynthesis of the compatible solute ectoine from Marinococcus halophilus and osmoregulated expression in Escherichia coli". Microbiology. 143 (4): 1141–9. doi:10.1099/00221287-143-4-1141. PMID 9141677.
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