Biology: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 / QuickGO | ||||||||
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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 [math]\displaystyle{ \rightleftharpoons }[/math] 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
- "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. 1997. doi:10.1128/jb.179.16.5118-5125.1997. PMID 9260954.
- "Two genes involved in the 1,3-diaminopropane production pathway in Haemophilus influenzae". Biol. Pharm. Bull. 21 (2): 170–3. 1998. doi:10.1248/bpb.21.170. PMID 9514614.
- "The biosynthesis of ectoine". FEMS Microbiol. Lett. 71 (1–2): 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.
- "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. 1997. doi:10.1099/00221287-143-4-1141. PMID 9141677.
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