Biology:2-Deoxystreptamine N-acetyl-D-glucosaminyltransferase
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Short description: Class of enzymes
| 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 [math]\displaystyle{ \rightleftharpoons }[/math] UDP + 2'-N-acetylparomamine
Involved in the biosynthetic pathways of several clinically important aminocyclitol antibiotics.
References
- ↑ "Involvement of two distinct N-acetylglucosaminyltransferases and a dual-function deacetylase in neomycin biosynthesis". ChemBioChem 9 (6): 865–9. April 2008. doi:10.1002/cbic.200700717. PMID 18311744.
- ↑ "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
- 2-deoxystreptamine+N-acetyl-D-glucosaminyltransferase at the US National Library of Medicine Medical Subject Headings (MeSH)
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