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Literature summary for 2.4.1.212 extracted from

  • Jing, W.; DeAngelis, P.L.
    Dissection of the two transferase activities of the Pasteurella multocida hyaluronan synthase: two active sites exist in one polypeptide (2000), Glycobiology, 10, 883-889.
    View publication on PubMed
Search for more literature for 2.4.1.212

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Pasteurella multocida

Protein Variants

Protein Variants Comment Organism
D196N mutants possess UDP-D-glucuronate-transferase activity Pasteurella multocida
D477K mutants possess UDP-N-acetyl-D-glucosamine-transferase activity Pasteurella multocida

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.14
-
 UDP-D-glucuronate
-
 Pasteurella multocida
0.16
-
 UDP-N-acetyl-D-glucosamine
-
 Pasteurella multocida

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
UDP-N-acetyl-D-glucosamine + UDP-D-glucuronate Pasteurella multocida
-
 [beta-N-acetyl-D-glucosaminyl(1-4)beta-D-glucuronosyl(1-3)]n + UDP
-
 ?

Organism

Organism UniProt Comment Textmining
Pasteurella multocida
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
UDP-N-acetyl-D-glucosamine + UDP-D-glucuronate
-
 Pasteurella multocida [beta-N-acetyl-D-glucosaminyl(1-4)beta-D-glucuronosyl(1-3)]n + UDP
-
 ?