Enzymes
| UniProtKB help_outline | 3 proteins |
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- Name help_outline ATP Identifier CHEBI:30616 (Beilstein: 3581767) help_outline Charge -4 Formula C10H12N5O13P3 InChIKeyhelp_outline ZKHQWZAMYRWXGA-KQYNXXCUSA-J SMILEShelp_outline Nc1ncnc2n(cnc12)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OP([O-])([O-])=O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 1,256 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline streptomycin Identifier CHEBI:58007 Charge 3 Formula C21H42N7O12 InChIKeyhelp_outline UCSJYZPVAKXKNQ-HZYVHMACSA-Q SMILEShelp_outline C[NH2+][C@H]1[C@H](O)[C@@H](O)[C@H](CO)O[C@H]1O[C@H]1[C@@H](O[C@@H](C)[C@]1(O)C=O)O[C@H]1[C@H](O)[C@@H](O)[C@H](NC(N)=[NH2+])[C@@H](O)[C@@H]1NC(N)=[NH2+] 2D coordinates Mol file for the small molecule Search links Involved in 6 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 6-O-adenylylstreptomycin Identifier CHEBI:146262 Charge 2 Formula C31H53N12O18P InChIKeyhelp_outline WTARMSKPYZJSQR-ZJVZNLSDSA-P SMILEShelp_outline C([C@H]1O[C@H]([C@@H]([C@@H]1O)O)N2C3=C(C(=NC=N3)N)N=C2)OP(O[C@H]4[C@@H]([C@H]([C@@H]([C@H]([C@@H]4O)O[C@@H]5O[C@H]([C@@]([C@H]5O[C@@H]6O[C@H]([C@@H]([C@H]([C@@H]6[NH2+]C)O)O)CO)(C=O)O)C)NC(=[NH2+])N)O)NC(N)=[NH2+])(=O)[O-] 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline diphosphate Identifier CHEBI:33019 (Beilstein: 185088) help_outline Charge -3 Formula HO7P2 InChIKeyhelp_outline XPPKVPWEQAFLFU-UHFFFAOYSA-K SMILEShelp_outline OP([O-])(=O)OP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 1,085 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:63236 | RHEA:63237 | RHEA:63238 | RHEA:63239 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Publications
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Enzymatic Adenylylation of Streptomycin and Spectinomycin by R-Factor-Resistant Escherichia coli.
Benveniste R., Yamada T., Davies J.
A resistance (R) factor-containing strain of Escherichia coli which is known to inactivate streptomycin by adenylylation has been shown to be spectinomycin resistant. An osmotic shockate of this strain catalyzes the formation of the biologically inactive spectinomycin adenylate, in which the adeny ... >> More
A resistance (R) factor-containing strain of Escherichia coli which is known to inactivate streptomycin by adenylylation has been shown to be spectinomycin resistant. An osmotic shockate of this strain catalyzes the formation of the biologically inactive spectinomycin adenylate, in which the adenylyl residue is probably attached to a d-threo methylamino alcohol moiety of spectinomycin. Both the streptomycin and spectinomycin adenylylating activities show the same temperature inactivation profile, and both are present in a protein fraction purified for the streptomycin inactivating enzyme. Mutants obtained from this strain which were sensitive to either spectinomycin or streptomycin were shown to lack both enzymatic activities when tested in vitro. Revertants of these mutants selected for recovery of either streptomycin resistance or spectinomycin resistance regain both activities. Therefore, we conclude that the inactivation of the two drugs is catalyzed by the same enzyme. Examination of a number of R factor-carrying strains has shown that those strains which are resistant to streptomycin and spectinomycin contain the adenylylating enzyme, whereas strains resistant to streptomycin but sensitive to spectinomycin inactivate streptomycin by phosphorylation. << Less
Infect Immun 1:109-119(1970) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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Structure of adenylylated streptomycin synthesized enzymatically by Bacillus subtilis.
O'Hara K., Ohmiya K., Kono M.
Antimicrob. Agents Chemother. 32:949-950(1988) [PubMed] [EuropePMC]
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Molecular recognition of aminoglycoside antibiotics by bacterial defence proteins: NMR study of the structural and conformational features of streptomycin inactivation by Bacillus subtilis aminoglycoside-6-adenyl transferase.
Corzana F., Cuesta I., Bastida A., Hidalgo A., Latorre M., Gonzalez C., Garcia-Junceda E., Jimenez-Barbero J., Asensio J.L.
The molecular recognition of streptomycin by Bacillus subtilis aminoglycoside-6-adenyl transferase has been analysed by a combination of NMR techniques and molecular dynamic simulations. This protein inactivates streptomycin by transferring an adenyl group to position six of the streptidine moiety ... >> More
The molecular recognition of streptomycin by Bacillus subtilis aminoglycoside-6-adenyl transferase has been analysed by a combination of NMR techniques and molecular dynamic simulations. This protein inactivates streptomycin by transferring an adenyl group to position six of the streptidine moiety. Our combined approach provides valuable information about the bioactive conformation for both the antibiotic and ATP and shows that the molecular recognition process for streptomycin involves a conformational selection phenomenon. The binding epitope for both ligands has also been analysed by 1D-STD experiments. Finally, the specificity of the recognition process with respect to the aminoglycoside and to the nucleotide has been studied. << Less
Chemistry 11:5102-5113(2005) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
Comments
Published in: Kano, M., K. Ohmiya, T. Kanda, N. Noguchi, and K. O'hara. 1987. Purification and characterization of chromosomal streptomycin adenylyltransferase from derivatives of