| EC |
3.5.1.112 |
| Accepted name: |
2′-N-acetylparomamine deacetylase |
| Reaction: |
2′-N-acetylparomamine + H2O = paromamine + acetate |
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For diagram of paromamine biosynthesis, click here |
| Glossary: |
paromamine = (1R)-O4-(2-amino-2-deoxy-α-D-glucopyranosyl)-2-deoxy-streptamine |
| Other name(s): |
btrD (gene name); neoL (gene name); kanN (gene name) |
| Systematic name: |
2′-N-acetylparomamine hydrolase (acetate-forming) |
| Comments: |
Involved in the biosynthetic pathways of several clinically important aminocyclitol antibiotics, including kanamycin, butirosin, neomycin and ribostamycin. The enzyme from the bacterium Streptomyces fradiae can also accept 2′′′-acetyl-6′′′-hydroxyneomycin C as substrate, cf. EC 3.5.1.113, 2′′′-acetyl-6′′′-hydroxyneomycin C deacetylase [2]. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
| References: |
| 1. |
Truman, A.W., Huang, F., Llewellyn, N.M. and Spencer, J.B. 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 (2007) 1462–1464. [DOI] [PMID: 17226887] |
| 2. |
Yokoyama, K., Yamamoto, Y., Kudo, F. and Eguchi, T. Involvement of two distinct N-acetylglucosaminyltransferases and a dual-function deacetylase in neomycin biosynthesis. ChemBioChem 9 (2008) 865–869. [DOI] [PMID: 18311744] |
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| [EC 3.5.1.112 created 2012] |
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