Biology:2'-N-acetylparomamine deacetylase
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Short description: Class of enzymes
| 2'-N-acetylparomamine deacetylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 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 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 + H2O [math]\displaystyle{ \rightleftharpoons }[/math] paromamine + acetate
This enzyme takes part in the biosynthetic pathways of several clinically important aminocyclitol antibiotics, including kanamycin, butirosin, neomycin and ribostamycin.
References
- ↑ "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. 2007. doi:10.1002/anie.200604194. PMID 17226887.
- ↑ "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.
External links
- 2'-N-acetylparomamine+deacetylase at the US National Library of Medicine Medical Subject Headings (MeSH)
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