2-Deoxystreptamine N-acetyl-D-glucosaminyltransferase
| 2-deoxystreptamine N-acetyl-D-glucosaminyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.4.1.283 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
2-deoxystreptamine N-acetyl-D-glucosaminyltransferase (EC 2.4.1.283, btrM (gene), neoD (gene), kanF (gene)) is an enzyme with systematic name UDP-N-acetyl-alpha-D-glucosamine:2-deoxystreptamine N-acetyl-D-glucosaminyltransferase.[1][2] This enzyme catalyses the following chemical reaction
- UDP-N-acetyl-alpha-D-glucosamine + 2-deoxystreptamine UDP + 2'-N-acetylparomamine
Involved in the biosynthetic pathways of several clinically important aminocyclitol antibiotics.
References
- ↑ Yokoyama, K.; Yamamoto, Y.; Kudo, F.; Eguchi, T. (2008). "Involvement of two distinct N-acetylglucosaminyltransferases and a dual-function deacetylase in neomycin biosynthesis". ChemBioChem. 9 (6): 865–869. doi:10.1002/cbic.200700717. PMID 18311744.
- ↑ Park, J.W.; Park, S.R.; Nepal, K.K.; Han, A.R.; Ban, Y.H.; Yoo, Y.J.; Kim, E.J.; Kim, E.M.; Kim, D.; Sohng, J.K.; Yoon, Y.J. (2011). "Discovery of parallel pathways of kanamycin biosynthesis allows antibiotic manipulation". Nat. Chem. Biol. 7 (11): 843–852. doi:10.1038/nchembio.671. PMID 21983602.
External links
- 2-deoxystreptamine N-acetyl-D-glucosaminyltransferase at the US National Library of Medicine Medical Subject Headings (MeSH)
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