Literature summary for 2.4.1.316 extracted from

Melancon, C.E. 3rd; Takahashi, H.; Liu, H.W.
Characterization of tylM3/tylM2 and mydC/mycB pairs required for efficient glycosyltransfer in macrolide antibiotic biosynthesis (2004), J. Am. Chem. Soc., 126, 16726-16727.

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Activating Compound

Activating Compound	Comment	Organism	Structure
tylM3 protein	activity is significantly enhanced by the presence of an accessory protein encoded by the tylM3 gene	Streptomyces fradiae

Cloned(Commentary)

Cloned (Comment)	Organism
expression in double mutant (KdesI/KdesVII) of Streptomyces venezuelae	Streptomyces fradiae

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
tylactone + dTDP-alpha-D-mycaminose	Streptomyces fradiae	the enzyme participates in the biosynthetic pathway of the macrolide antibiotic tylosin	dTDP + 5-O-beta-D-mycaminosyltylactone	-	?

Organism

Organism	UniProt	Comment	Textmining
Streptomyces fradiae	P95747	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
tylactone + dTDP-alpha-D-mycaminose	the enzyme participates in the biosynthetic pathway of the macrolide antibiotic tylosin	Streptomyces fradiae	dTDP + 5-O-beta-D-mycaminosyltylactone	-	?
tylactone + dTDP-alpha-D-mycaminose	the enzyme is flexible toward the acceptor substrate, glycosylating 16-membered tylactone and 12-membered ring macrolide	Streptomyces fradiae	dTDP + 5-O-beta-D-mycaminosyltylactone	-	?

Synonyms

Synonyms	Comment	Organism
TylM2	-	Streptomyces fradiae

General Information

General Information	Comment	Organism
physiological function	the enzyme participates in the biosynthetic pathway of the macrolide antibiotic tylosin	Streptomyces fradiae

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Release 2023.1 (January 2023)