Literature summary for 2.4.1.288 extracted from

Szczepina, M.G.; Zheng, R.B.; Completo, G.C.; Lowary, T.L.; Pinto, B.M.
STD-NMR studies suggest that two acceptor substrates for GlfT2, a bifunctional galactofuranosyltransferase required for the biosynthesis of Mycobacterium tuberculosis arabinogalactan, compete for the same binding site (2009), ChemBioChem, 10, 2052-2059.

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Organism

Organism	UniProt	Comment	Textmining
Mycobacterium tuberculosis	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	GlfT2 has one active site pocket capable of catalyzing both beta-(1->5) and beta-(1->6) galactofuranosyl transfer reactions	Mycobacterium tuberculosis	?	-	?
UDP-alpha-D-galactofuranose + beta-D-Galf-(1->5)-beta-D-Galf-(1->6)-beta-D-Galf-O(CH2)7CH3	-	Mycobacterium tuberculosis	beta-D-Galf-(1->6)-beta-D-Galf-(1->5)-beta-D-Galf-(1->6)-beta-D-Galf-O(CH2)7CH3	-	?
UDP-alpha-D-galactofuranose + beta-D-Galf-(1->6)-beta-D-Galf-(1->5)-beta-D-Galf-O(CH2)7CH3	-	Mycobacterium tuberculosis	UDP + beta-D-Galf-(1->5)-beta-D-Galf-(1->6)-beta-D-Galf-(1->5)-beta-D-Galf-O(CH2)7CH3	-	?

Synonyms

Synonyms	Comment	Organism
GlfT2	-	Mycobacterium tuberculosis

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Release 2023.1 (January 2023)