2'-N-acetylparomamine deacetylase (EC 3.5.1.112, btrD (gene), neoL (gene), kanN (gene)) is an enzyme with systematic name 2'-N-acetylparomamine hydrolase (acetate-forming).[1][2] This enzyme catalyses the following chemical reaction
| 2'-N-acetylparomamine deacetylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.5.1.112 | ||||||||
| 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'-N-acetylparomamine + H2O paromamine + acetate
This enzyme takes part in the biosynthetic pathways of several clinically important aminocyclitol antibiotics, including kanamycin, butirosin, neomycin and ribostamycin.
References
edit- ^ Truman AW, Huang F, Llewellyn NM, Spencer JB (2007). "Characterization of the enzyme BtrD from Bacillus circulans and revision of its functional assignment in the biosynthesis of butirosin". Angewandte Chemie. 46 (9): 1462–4. doi:10.1002/anie.200604194. PMID 17226887.
- ^ 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.
External links
edit- 2'-N-acetylparomamine+deacetylase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
