2'-N-acetylparomamine deacetylase
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 paromamine + acetate
This enzyme takes part in the biosynthetic pathways of several clinically important aminocyclitol antibiotics, including kanamycin, butirosin, neomycin and ribostamycin.
References
- ↑ Truman, A.W.; Huang, F.; Llewellyn, N.M.; Spencer, J.B. (2007). "Characterization of the enzyme BtrD from Bacillus circulans and revision of its functional assignment in the biosynthesis of butirosin". Angew. Chem. Int. Ed. Engl. 46 (9): 1462–1464. doi:10.1002/anie.200604194. PMID 17226887.
- ↑ 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: 865–869. doi:10.1002/cbic.200700717. PMID 18311744.
External links
- 2'-N-acetylparomamine deacetylase at the US National Library of Medicine Medical Subject Headings (MeSH)
This article is issued from Wikipedia - version of the 5/16/2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.