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 transaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 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 | ||||||||
| |||||||||
- neamine + 2-oxoglutarate 6'-dehydroparomamine + L-glutamate
The reaction occurs in vivo in the opposite direction.
References
edit- ^ 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)
