2'-N-acetylparomamine deacetylase

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
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins
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

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  1. ^ 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.
  2. ^ 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.
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