Diaminobutyrate acetyltransferase
| Diaminobutyrate acetyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.3.1.178 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Diaminobutyrate acetyltransferase (EC 2.3.1.178) is an enzyme that catalyzes the chemical reaction
-2%252C4-Diaminobutyric_acid.svg.png)
-acetyl-L-2%252C4-diaminobutyric_acid.svg.png)
The two substrates of this enzyme are (S)-2,4-diaminobutyric acid and acetyl-CoA. Its products are N(4)-acetyl-L-2,4-diaminobutyric acid and coenzyme A.[1][2] The enzyme has been characterised in a number of organisms including Halomonas elongata, Methylomicrobium alcaliphilum and Bacillus pasteurii. The product of the reaction is converted to ectoine by the enzyme ectoine synthase in these species.[3][4][5]
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acetyl-CoA:L-2,4-diaminobutanoate N4-acetyltransferase. Other names in common use include L-2,4-diaminobutyrate acetyltransferase, L-2,4-diaminobutanoate acetyltransferase, EctA, diaminobutyric acid acetyltransferase, DABA acetyltransferase, 2,4-diaminobutanoate acetyltransferase, DAB acetyltransferase, DABAcT, and acetyl-CoA:L-2,4-diaminobutanoate 4-N-acetyltransferase.[6]
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.
- ↑ Louis P, Galinski EA (April 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.
- ↑ 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. doi:10.1128/JB.181.1.91-99.1999. PMC 103536. PMID 9864317.
- ↑ Reshetnikov AS, Mustakhimov II, Khmelenina VN, Trotsenko YA (August 2005). "Cloning, purification, and characterization of diaminobutyrate acetyltransferase from the halotolerant methanotroph Methylomicrobium alcaliphilum 20Z". Biochemistry. 70 (8). Mosc: 878–83. doi:10.1007/s10541-005-0197-x. PMID 16212543.
- ↑ 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. Bibcode:2002ApEnM..68..772K. doi:10.1128/AEM.68.2.772-783.2002. PMC 126723. PMID 11823218.
- ↑ Enzyme 2.3.1.178 at KEGG Pathway Database.