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Seno, E.T.; Baltz, R.H.: Properties of S-adenosyl-L-methionine:macrocin O-methyltransferase in extracts of Streptomyces fradiae strains which produce normal or elevated levels of tylosin and in mutants blocked in specific O-methylations. Antimicrob. Agents Chemother., 20, 370–377 (1981)
Bauer, N.J.; Kreuzman, A.J.; Dotzlaf, J.E.; Yeh, W.K.: Purification, characterization, and kinetic mechanism of S-adenosyl-L-methionine:macrocin O-methyltransferase from Streptomyces fradiae. J. Biol. Chem., 263, 15619–15625 (1988)
Yeh, W.K.; Bauer, N.J.; Dotzlaf, J.E.: High-performance liquid chromato-graphic assay for S-adenosyl-L-methionine: macrocin O-methyltransferase. J. Chromatogr., 288, 157–165 (1984)
Kreuzman, A.J.; Turner, J.R.; Yeh, W.K.: Two distinctive O-methyltransferases catalyzing penultimate and terminal reactions of macrolide antibiotic (tylosin) biosynthesis. Substrate specificity, enzyme inhibition, and kinetic mechanism. J. Biol. Chem., 263, 15626–15633 (1988)
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(2006). Macrocin O-methyltransferase. In: Schomburg, D., Schomburg, I., Chang, A. (eds) Class 2 · Transferases I. Springer Handbook of Enzymes, vol 28. Springer, Berlin, Heidelberg. https://doi.org/10.1007/3-540-37715-8_101
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DOI: https://doi.org/10.1007/3-540-37715-8_101
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