EC |
2.4.1.283 |
Accepted name: |
2-deoxystreptamine N-acetyl-D-glucosaminyltransferase |
Reaction: |
UDP-N-acetyl-α-D-glucosamine + 2-deoxystreptamine = UDP + 2′-N-acetylparomamine |
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For diagram of paromamine biosynthesis, click here |
Other name(s): |
btrM (gene name); neoD (gene name); kanF (gene name) |
Systematic name: |
UDP-N-acetyl-α-D-glucosamine:2-deoxystreptamine N-acetyl-D-glucosaminyltransferase |
Comments: |
Involved in the biosynthetic pathways of several clinically important aminocyclitol antibiotics, including kanamycin, butirosin, neomycin and ribostamycin. Unlike the enzyme from the bacterium Streptomyces kanamyceticus, which can also accept UDP-D-glucose [2] (cf. EC 2.4.1.284, 2-deoxystreptamine glucosyltransferase), the enzyme from Bacillus circulans can only accept UDP-N-acetyl-α-D-glucosamine [1]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
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] |
2. |
Park, J.W., Park, S.R., Nepal, K.K., Han, A.R., Ban, Y.H., Yoo, Y.J., Kim, E.J., Kim, E.M., Kim, D., Sohng, J.K. and Yoon, Y.J. Discovery of parallel pathways of kanamycin biosynthesis allows antibiotic manipulation. Nat. Chem. Biol. 7 (2011) 843–852. [DOI] [PMID: 21983602] |
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[EC 2.4.1.283 created 2012] |
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