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Literature summary for 2.4.1.212 extracted from

  • Yang, J.; Cheng, F.; Yu, H.; Wang, J.; Guo, Z.; Stephanopoulos, G.
    Key role of the carboxyl terminus of hyaluronan synthase in processive synthesis and size control of hyaluronic acid polymers (2017), Biomacromolecules, 18, 1064-1073 .
    View publication on PubMed
Search for more literature for 2.4.1.212

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Streptococcus dysgalactiae subsp. equisimilis

Protein Variants

Protein Variants Comment Organism
delD409-L417 deletion of 409-DWGTRKKLL-417 causes significant decreases in hyaluronic acid titer and in vitro hyaluronan synthase activity and undetectable hyaluronic acid weight-average molecular weight. Stepping truncations from L417 to K415 have little impact on hyaluronic acid and molecular weight. The removal of L417-K414, the hyaluronic acid titer of the resulting WGTR413 variant dramatically decreased to 16.8% of the wild type, while the same hyaluronic acid molecular weight is still detectable. With the further removal of R413, the hyaluronic acid titer of the resulting WGT412 variant dropps to less than 10% of the wild-type, and no hyaluronic acid products are detectable Streptococcus dysgalactiae subsp. equisimilis
K414A mutation does not notably affect hyaluronic acid titer Streptococcus dysgalactiae subsp. equisimilis
K414R mutation does not notably affect hyaluronic acid titer. The molecular weight of the hyaluronic acid produced by the K414R variant is significantly increased Streptococcus dysgalactiae subsp. equisimilis
K415A mutation does not notably affect hyaluronic acid titer Streptococcus dysgalactiae subsp. equisimilis
K415R mutation does not notably affect hyaluronic acid titer Streptococcus dysgalactiae subsp. equisimilis
R406A hyaluronic acid titer is greatly decreased Streptococcus dysgalactiae subsp. equisimilis
R413A hyaluronic acid titer is greatly decreased Streptococcus dysgalactiae subsp. equisimilis
R413K the variant barely produces hyaluronic acid Streptococcus dysgalactiae subsp. equisimilis
T412A mutations completely deactivates the enzyme Streptococcus dysgalactiae subsp. equisimilis
W410A mutations completely deactivates the enzyme Streptococcus dysgalactiae subsp. equisimilis

Organism

Organism UniProt Comment Textmining
Streptococcus dysgalactiae subsp. equisimilis A0A514TRT9
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information a catalysis-transformation-translocation model is proposed for the hyaluronic acid synthesis and translocation processes. The residue R406 and R413 are primarily involved in catalysis, while the residues between 414 and 417 are involved in hyaluronic acid translocation Streptococcus dysgalactiae subsp. equisimilis ?
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