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PMID:24166757
| Citation |
Najmanová, L, Kutejová, E, Kadlec, J, Polan, M, Olšovská, J, Benada, O, Novotná, J, Kameník, Z, Halada, P, Bauer, J and Janata, J' (2013) Characterization of N-Demethyllincosamide Methyltransferases LmbJ and CcbJ. Chembiochem ' |
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| Abstract |
Chemical diversity: Two SAM-dependent N-methyltransferases-LmbJ from the biosynthesis of the antibiotic lincomycin and CcbJ from celesticetin biosynthesis-have been characterized and compared. Both tested enzymes form multimers and are able to utilize N-demethyllincomycin, the natural substrate of LmbJ, with comparable efficiency. |
| Links |
PubMed Online version:10.1002/cbic.201300389 |
| Keywords |
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| edit table |
Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0008170: N-methyltransferase activity |
ECO:0000314: |
F |
Figure 2:Plot shows rate of conversion of N-demethyllincomycin (NDL) into lincomycin showing methyltransferase activity. |
complete | ||||
|
enables |
GO:0008170: N-methyltransferase activity |
ECO:0000314: direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
| GO:0008170: N-methyltransferase activity |
ECO:0000314: |
F |
Figure 2:Plot shows rate of conversion of N-demethyllincomycin (NDL) into lincomycin showing methyltransferase activity. |
complete | ||||
|
enables |
GO:0008170: N-methyltransferase activity |
ECO:0000314: direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
See also
References
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