Neamine transaminase
| Neamine transaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.6.1.93 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
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] It catalyses a chemical reaction that is part of the biosynthesis of a number of aminoglycoside antibiotics including lividomycin, neomycin and kanamycin. In these pathways in bacteria such as Streptomyces kanamyceticus the reaction converts 6'-oxoparomamine to neamine.[2][3][4]
References
[edit]- ↑ Enzyme 2.6.1.93 at KEGG Pathway Database.
- ↑ Huang F, Spiteller D, Koorbanally NA, Li Y, Llewellyn NM, Spencer JB (February 2007). "Elaboration of neosamine rings in the biosynthesis of neomycin and butirosin". ChemBioChem. 8 (3): 283–8. doi:10.1002/cbic.200600371. PMID 17206729.
- ↑ Clausnitzer D, Piepersberg W, Wehmeier UF (September 2011). "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. doi:10.1111/j.1365-2672.2011.05082.x. PMID 21689223.
- ↑ Park JW, Park SR, Nepal KK, Han AR, Ban YH, Yoo YJ, Kim EJ, Kim EM, Kim D, Sohng JK, Yoon YJ (October 2011). "Discovery of parallel pathways of kanamycin biosynthesis allows antibiotic manipulation". Nature Chemical Biology. 7 (11): 843–52. doi:10.1038/nchembio.671. PMID 21983602.
External links
[edit]- Neamine+transaminase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
