2-Deoxystreptamine N-acetyl-D-glucosaminyltransferase
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| 2-deoxystreptamine N-acetyl-D-glucosaminyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 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[edit]
- ^ Yokoyama K, Yamamoto Y, Kudo F, Eguchi T (April 2008). "Involvement of two distinct N-acetylglucosaminyltransferases and a dual-function deacetylase in neomycin biosynthesis". ChemBioChem. 9 (6): 865–9. doi:10.1002/cbic.200700717. PMID 18311744.
- ^ 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]
- 2-deoxystreptamine+N-acetyl-D-glucosaminyltransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
