Biology:Neamine transaminase
From HandWiki
| Neamine transaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.6.1.93 | ||||||||
| 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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Neamine transaminase (EC 2.6.1.93, glutamate---6'-dehydroparomamine aminotransferase, btrB (gene), neoN (gene), kacL (gene)) is an enzyme with systematic name neamine:2-oxoglutarate aminotransferase.[1][2][3] This enzyme catalyses the following chemical reaction
- neamine + 2-oxoglutarate 6'-dehydroparomamine + L-glutamate
The reaction occurs in vivo in the opposite direction.
References
- ↑ "Elaboration of neosamine rings in the biosynthesis of neomycin and butirosin". ChemBioChem 8 (3): 283–8. February 2007. doi:10.1002/cbic.200600371. PMID 17206729.
- ↑ "The oxidoreductases LivQ and NeoQ are responsible for the different 6'-modifications in the aminoglycosides lividomycin and neomycin". Journal of Applied Microbiology 111 (3): 642–51. September 2011. doi:10.1111/j.1365-2672.2011.05082.x. PMID 21689223.
- ↑ "Discovery of parallel pathways of kanamycin biosynthesis allows antibiotic manipulation". Nature Chemical Biology 7 (11): 843–52. October 2011. doi:10.1038/nchembio.671. PMID 21983602.
External links
- Neamine+transaminase at the US National Library of Medicine Medical Subject Headings (MeSH)
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