Diaminobutyrate—2-oxoglutarate transaminase
| diaminobutyrate-2-oxoglutarate transaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.6.1.76 | ||||||||
| CAS number | 196622-96-5 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / EGO | ||||||||
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In enzymology, a diaminobutyrate-2-oxoglutarate transaminase (EC 2.6.1.76) is an enzyme that catalyzes the chemical reaction
- L-2,4-diaminobutanoate + 2-oxoglutarate L-aspartate 4-semialdehyde + L-glutamate
Thus, the two substrates of this enzyme are L-2,4-diaminobutanoate and 2-oxoglutarate, whereas its two products are L-aspartate 4-semialdehyde and L-glutamate.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-2,4-diaminobutanoate:2-oxoglutarate 4-aminotransferase. Other names in common use include L-2,4-diaminobutyrate:2-ketoglutarate 4-aminotransferase, 2,4-diaminobutyrate 4-aminotransferase, diaminobutyrate aminotransferase, DABA aminotransferase, DAB aminotransferase, EctB, diaminibutyric acid aminotransferase, and L-2,4-diaminobutyrate:2-oxoglutarate 4-aminotransferase. This enzyme participates in glycine, serine and threonine metabolism.
References
- Ikai H, Yamamoto S (1997). "Identification and analysis of a gene encoding L-2,4-diaminobutyrate:2-ketoglutarate 4-aminotransferase involved in the 1,3-diaminopropane production pathway in Acinetobacter baumannii". J. Bacteriol. 179 (16): 5118–25. PMC 179370
. PMID 9260954. - Ikai H, Yamamoto S (1998). "Two genes involved in the 1,3-diaminopropane production pathway in Haemophilus influenzae". Biol. Pharm. Bull. 21 (2): 170–3. doi:10.1248/bpb.21.170. PMID 9514614.
- Peters P, Galinski EA, Truper HG (1990). "The biosynthesis of ectoine". FEMS Microbiol. Lett. 71: 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. "Characterization of genes for the biosynthesis of the compatible solute ectoine from Marinococcus halophilus and osmoregulated expression in Escherichia coli". Microbiology. 143: 1141–9. doi:10.1099/00221287-143-4-1141. PMID 9141677.