Literature summary for 2.4.1.212 extracted from

Agarwal, G.; K V, K.; Prasad, S.B.; Bhaduri, A.; Jayaraman, G.
Biosynthesis of Hyaluronic acid polymer Dissecting the role of sub structural elements of hyaluronan synthase (2019), Sci. Rep., 9, 12510 .

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Organism

Organism	UniProt	Comment	Textmining
Streptococcus equi subsp. zooepidemicus	Q84GC8	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	a three-dimensional atomic scale model of class I hyaluronan synthase enzymes is presented to gain insights on functional features. 9 hyaluronan synthase-specific sub-structural elements are identified. Docking studies with UDP-substrates in the enzyme show highly overlapping single binding sites for the two UDP-substrates. In-silico and mutation studies identify functional elements implicated in polymer binding and influencing hyaluronic acid production. The studies indicate a substrate binding role for Lys139, and a critical role for Gln248 and Thr283. Anisotropic Network Modeling (ANM)-based model is analysed to assess collective global dynamics in the enzyme. Based on ligand binding landscape and architecture of functional elements, a plausible three-step molecular mechanism to extend hyaluronic acid polymer from its reducing end is proposed. The release of UDP from polymeric end may be required for glycosyltransferase reaction	Streptococcus equi subsp. zooepidemicus	?	-	-

Synonyms

Synonyms	Comment	Organism
HAS	-	Streptococcus equi subsp. zooepidemicus

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Release 2023.1 (January 2023)