EC 2.4.1.283 - 2-deoxystreptamine N-acetyl-D-glucosaminyltransferase

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IntEnz Enzyme Nomenclature
EC 2.4.1.283

Names

Accepted name:
2-deoxystreptamine N-acetyl-D-glucosaminyltransferase
Other names:
btrM (gene name)
neoD (gene name)
kanF (gene name)
Systematic name:
UDP-N-acetyl-α-D-glucosamine:2-deoxystreptamine N-acetyl-D-glucosaminyltransferase

Reaction

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

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0102319
UniProtKB/Swiss-Prot:

References

  1. Yokoyama, K., Yamamoto, Y., Kudo, F., Eguchi, T.
    Involvement of two distinct N-acetylglucosaminyltransferases and a dual-function deacetylase in neomycin biosynthesis.
    Chembiochem 9 : 865-869 (2008). [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., Yoon, Y. J.
    Discovery of parallel pathways of kanamycin biosynthesis allows antibiotic manipulation.
    Nat. Chem. Biol. 7 : 843-852 (2011). [PMID: 21983602]

[EC 2.4.1.283 created 2012]