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Results 1 - 9 of 9
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EC Number Substrates Commentary Substrates Organism Products Commentary (Products) Reversibility
Display the reaction diagram Show all sequences 2.1.1.2352 S-adenosyl-L-methionine + dTDP-3-amino-3,4,6-trideoxy-alpha-xylo-hexopyranose kcat/KM is about 3fold lower than kcat/Km for the natural substrated TDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose Streptomyces fradiae 2 S-adenosyl-L-homocysteine + dTDP-3-dimethylamino-3,4,6-trideoxy-alpha-xylo-hexopyranose i.e. TDP-alpha-D-desosamine ?
Display the reaction diagram Show all sequences 2.1.1.2352 S-adenosyl-L-methionine + dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose - Streptomyces fradiae 2 S-adenosyl-L-homocysteine + dTDP-3-dimethylamino-3,6-dideoxy-alpha-D-glucopyranose - ?
Display the reaction diagram Show all sequences 2.1.1.2352 S-adenosyl-L-methionine + dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose the enzyme is involved in biosynthesis of D-mycaminose. It is synthesized by the Gram-positive bacterium Streptomyces fradiae as a dTDP-linked sugar Streptomyces fradiae 2 S-adenosyl-L-homocysteine + dTDP-3-dimethylamino-3,6-dideoxy-alpha-D-glucopyranose - ?
Display the reaction diagram Show all sequences 2.1.1.2352 S-adenosyl-L-methionine + dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose the enzyme is involved in the biosynthesis of mycaminose, an essential structural component of the macrolide antibiotic tylosin poduced by Streptomyces fradiae Streptomyces fradiae 2 S-adenosyl-L-homocysteine + dTDP-3-dimethylamino-3,6-dideoxy-alpha-D-glucopyranose - ?
Display the reaction diagram Show all sequences 2.1.1.2352 S-adenosyl-L-methionine + dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose TylM1 has relaxed specificity toward its sugar substrate. The kcat/KM for dTDP-3-amino-4,6-dideoxy-alpha-D-glucopyranose is about 3fold lower than kcat/Km for the natural substrated TDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose Streptomyces fradiae 2 S-adenosyl-L-homocysteine + dTDP-3-dimethylamino-3,6-dideoxy-alpha-D-glucopyranose - ?
Display the reaction diagram Show all sequences 2.1.1.2352 S-adenosyl-L-methionine + dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose i.e dTDP-mycaminose, binding pocket structure and binding mechanism, overview Streptomyces fradiae 2 S-adenosyl-L-homocysteine + dTDP-3-dimethylamino-3,6-dideoxy-alpha-D-glucopyranose analysis of the binding structure of the dTDP-sugar in enzyme TylM1 active site, overview. Only a water molecule is expelled from the active site to accommodate one of the methyl substituents on the C-3' amino group ?
Display the reaction diagram Show all sequences 2.1.1.235more the enzyme also catalyzes the methylation of dTDP-3-amino-3,6-dideoxy-alpha-D-galactopyranose, EC 2.1.1.236 Streptomyces fradiae ? - ?
Display the reaction diagram Show all sequences 2.1.1.235more modeling of substrate binding Streptomyces fradiae ? - ?
Display the reaction diagram Show all sequences 2.1.1.235S-adenosyl-L-methionine + dTDP-3-methylamino-3,6-dideoxy-alpha-D-glucopyranose chemically prepared monomethylated compound is a substrate for TylM1 and could be swiftly converted by TylM1 to the dimethylated product. TylM1 catalyzes an N,N-dimethylation reaction by way of a monomethylated intermediate. Since the monomethylated amino group is intrinsically a better nucleophile than the unsubstituted amino group, the reaction rate of this SN2-type methyl transfer reaction is expected to be higher for the second half reaction than for the first methylation reaction Streptomyces fradiae S-adenosyl-L-homocysteine + dTDP-3-dimethylamino-3,6-dideoxy-alpha-D-glucopyranose - ?
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