Enzymes
| UniProtKB help_outline | 1 proteins |
| Enzyme class help_outline |
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Reaction participants Show >> << Hide
- Name help_outline neamine Identifier CHEBI:65076 Charge 4 Formula C12H30N4O6 InChIKeyhelp_outline SYJXFKPQNSDJLI-HKEUSBCWSA-R SMILEShelp_outline [NH3+]C[C@H]1O[C@H](O[C@@H]2[C@@H]([NH3+])C[C@@H]([NH3+])[C@H](O)[C@H]2O)[C@H]([NH3+])[C@@H](O)[C@@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 4 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline UDP-α-D-kanosamine Identifier CHEBI:71964 Charge -1 Formula C15H24N3O16P2 InChIKeyhelp_outline KGGAKOCPPBMRSA-SAINOKEESA-M SMILEShelp_outline [NH3+][C@H]1[C@H](O)[C@@H](CO)O[C@H](OP([O-])(=O)OP([O-])(=O)OC[C@H]2O[C@H]([C@H](O)[C@@H]2O)n2ccc(=O)[nH]c2=O)[C@@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 5 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline kanamycin B Identifier CHEBI:58549 Charge 5 Formula C18H42N5O10 InChIKeyhelp_outline SKKLOUVUUNMCJE-FQSMHNGLSA-S SMILEShelp_outline [NH3+]C[C@H]1O[C@H](O[C@@H]2[C@@H]([NH3+])C[C@@H]([NH3+])[C@H](O[C@H]3O[C@H](CO)[C@@H](O)[C@H]([NH3+])[C@H]3O)[C@H]2O)[C@H]([NH3+])[C@@H](O)[C@@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 3 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline UDP Identifier CHEBI:58223 Charge -3 Formula C9H11N2O12P2 InChIKeyhelp_outline XCCTYIAWTASOJW-XVFCMESISA-K SMILEShelp_outline O[C@@H]1[C@@H](COP([O-])(=O)OP([O-])([O-])=O)O[C@H]([C@@H]1O)n1ccc(=O)[nH]c1=O 2D coordinates Mol file for the small molecule Search links Involved in 577 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,521 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:35783 | RHEA:35784 | RHEA:35785 | RHEA:35786 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Enzymatic activity of a glycosyltransferase KanM2 encoded in the kanamycin biosynthetic gene cluster.
Kudo F., Sucipto H., Eguchi T.
J Antibiot (Tokyo) 62:707-710(2009) [PubMed] [EuropePMC]
This publication is cited by 3 other entries.
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The last step of kanamycin biosynthesis: unique deamination reaction catalyzed by the alpha-ketoglutarate-dependent nonheme iron dioxygenase KanJ and the NADPH-dependent reductase KanK.
Sucipto H., Kudo F., Eguchi T.
Mystery solved: using heterologous expression, the activities of two enzymes exclusively belonging to the kanamycin biosynthetic pathway have been identified in vitro. A distinctive reaction mechanism to produce kanamycin is proposed and the previously unknown catalytic deamination activity of Kan ... >> More
Mystery solved: using heterologous expression, the activities of two enzymes exclusively belonging to the kanamycin biosynthetic pathway have been identified in vitro. A distinctive reaction mechanism to produce kanamycin is proposed and the previously unknown catalytic deamination activity of KanJ dioxygenase is uncovered. << Less
Angew. Chem. Int. Ed. 51:3428-3431(2012) [PubMed] [EuropePMC]
This publication is cited by 5 other entries.
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Discovery of parallel pathways of kanamycin biosynthesis allows antibiotic manipulation.
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.
Kanamycin is one of the most widely used antibiotics, yet its biosynthetic pathway remains unclear. Current proposals suggest that the kanamycin biosynthetic products are linearly related via single enzymatic transformations. To explore this system, we have reconstructed the entire biosynthetic pa ... >> More
Kanamycin is one of the most widely used antibiotics, yet its biosynthetic pathway remains unclear. Current proposals suggest that the kanamycin biosynthetic products are linearly related via single enzymatic transformations. To explore this system, we have reconstructed the entire biosynthetic pathway through the heterologous expression of combinations of putative biosynthetic genes from Streptomyces kanamyceticus in the non-aminoglycoside-producing Streptomyces venezuelae. Unexpectedly, we discovered that the biosynthetic pathway contains an early branch point, governed by the substrate promiscuity of a glycosyltransferase, that leads to the formation of two parallel pathways in which early intermediates are further modified. Glycosyltransferase exchange can alter flux through these two parallel pathways, and the addition of other biosynthetic enzymes can be used to synthesize known and new highly active antibiotics. These results complete our understanding of kanamycin biosynthesis and demonstrate the potential of pathway engineering for direct in vivo production of clinically useful antibiotics and more robust aminoglycosides. << Less
Nat. Chem. Biol. 7:843-852(2011) [PubMed] [EuropePMC]
This publication is cited by 13 other entries.