Biology:Diaminobutyrate acetyltransferase
| Diaminobutyrate acetyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.3.1.178 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
In enzymology, a diaminobutyrate acetyltransferase (EC 2.3.1.178) is an enzyme that catalyzes the chemical reaction
- acetyl-CoA + L-2,4-diaminobutanoate [math]\displaystyle{ \rightleftharpoons }[/math] CoA + N4-acetyl-L-2,4-diaminobutanoate
Thus, the two substrates of this enzyme are acetyl-CoA and L-2,4-diaminobutanoate, whereas its two products are CoA and N4-acetyl-L-2,4-diaminobutanoate.
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. This enzyme participates in glycine, serine and threonine metabolism.
References
- "The biosynthesis of ectoine". FEMS Microbiol. Lett. 71: 157–162. 1990. doi:10.1111/j.1574-6968.1990.tb03815.x.
- "Characterization of Biosynthetic Enzymes for Ectoine as a Compatible Solute in a Moderately Halophilic Eubacterium, Halomonas elongata". J. Bacteriol. 181 (1): 91–9. 1999. PMID 9864317.
- "Cloning, purification, and characterization of diaminobutyrate acetyltransferase from the halotolerant methanotroph Methylomicrobium alcaliphilum 20Z". Biochemistry (Mosc) 70 (8): 878–83. August 2005. doi:10.1007/s10541-005-0197-x. PMID 16212543.
- "Osmotically Regulated Synthesis of the Compatible Solute Ectoine in Bacillus pasteurii and Related Bacillus spp". Appl. Environ. Microbiol. 68 (2): 772–83. 2002. doi:10.1128/AEM.68.2.772-783.2002. PMID 11823218.
- "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. April 1997. doi:10.1099/00221287-143-4-1141. PMID 9141677.
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