The enzyme is involved in the synthesis of dTDP-D-ravidosamine, the amino sugar moiety of the antibiotic ravidomycin V, which is produced by the bacterium Streptomyces ravidus.
The expected taxonomic range for this enzyme is: Streptomyces
The enzyme is involved in the synthesis of dTDP-D-ravidosamine, the amino sugar moiety of the antibiotic ravidomycin V, which is produced by the bacterium Streptomyces ravidus.
Substrates: RavNMT catalyzes the transfer of methyl groups from S-adenosyl-L-methionine to the amino nitrogen of in a sequential manner Products: TDP-3-dimethylamino-3,6-dideoxy-alpha-D-galactopyranose i.e. TDP-D-ravidosamine
Substrates: - Products: 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
structure model of TylM1 with bound S-adenosyl-L-methionine and dTDP-phenol: Model of the Michaelis complex in stereo. The C-3' amino group is positioned to attack the methyl group of S-adenoyl-L-methionine. dTDP-mycaminose binding pocket structure, overview
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme in complex with S-adenosyl-L-homocysteine and dTDP-3-N-methylamino-3,6-dideoxygalactose., X-ray diffraction structure determination and analysis at 2.2 A resolution
synthesis of TDP-D-ravidosamine, necessary for future in vitro glycosylation assays. TDP-D-ravidosamine is the anticipated sugar donor substrate of RavGT (the glycosyltransferase that links D-ravidosamine to the polyketide derived backbone defuco-gilvocarcin V). Defuco-gilvocarcin V exhibits superior anticancer/antibacterial activities
Characterization of the TDP-D-ravidosamine biosynthetic pathway: one-pot enzymatic synthesis of TDP-D-ravidosamine from thymidine-5-phosphate and glucose-1-phosphate
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