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Ligand demethyllactenocin Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Basic Ligand Information Molecular Structure
C3 7 H6 1 NO1 4
demethyllactenocin
QZCOVMJUGCBXHV-ZSLVOGAPSA-N
Roles as Enzyme Ligand
In Vivo Substrate in Enzyme-catalyzed Reactions (1 result)
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dTDP-beta-L-mycarose + demethyllactenocin = dTDP + demethylmacrocin
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In Vivo Product in Enzyme-catalyzed Reactions (1 result)
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5-O-beta-D-mycaminosyltylonolide + dTDP-6-deoxy-alpha-D-allose = dTDP + demethyllactenocin
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Substrate in Enzyme-catalyzed Reactions (3 results)
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S-adenosyl-L-methionine + demethyllactenocin = S-adenosyl-L-homocysteine + 2'''-O-demethyldesmycosin
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S-adenosyl-L-methionine + demethyllactenocin = S-adenosyl-L-homocysteine + lactenocin
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dTDP-beta-L-mycarose + demethyllactenocin = dTDP + demethylmacrocin
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Product in Enzyme-catalyzed Reactions (1 result)
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5-O-beta-D-mycaminosyltylonolide + dTDP-6-deoxy-alpha-D-allose = dTDP + demethyllactenocin
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Inhibitor in Enzyme-catalyzed Reactions (1 result)
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Enzyme Kinetic Parameters
KM Value (1 result)
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References & Links Literature References (4)
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Purification, characterization, and kinetic mechanism of S-adenosyl-L-methionine:macrocin O-methyltransferase from Streptomyces fradiae
1988
Bauer, N.J.; Kreuzman, A.J.; Dotzlaf, J.E.; Yeh, W.K.
J. Biol. Chem.
263
15619-15625
Two distinctive O-methyltransferases catalyzing penultimate and terminal reactions of macrolide antibiotic (tylosin) biosynthesis. Substrate specificity, enzyme inhibition, and kinetic mechanism
1988
Kreuzman, A.J.; Turner, J.R.; Yeh, W.K.
J. Biol. Chem.
263
15626-15633
The mycarose-biosynthetic genes of Streptomyces fradiae, producer of tylosin
2000
Bate, N.; Butler, A.R.; Smith, I.P.; Cundliffe, E.
Microbiology
146
139-146
Characterization of the two methylation steps involved in the biosynthesis of mycinose in tylosin
2016
Kim, E.; Song, M.; Kim, M.; Beom, J.; Lee, E.; Kim, D.; Nam, S.; Yoon, Y.
J. Nat. Prod.
79
2014-2021
Links to other databases for demethyllactenocin