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Literature summary for 2.4.1.16 extracted from

  • Uchida, Y.; Shimmi, O.; Sudoh, M.; Arisawa, M.; Yamada-Okabe, H.
    Characterization of chitin synthase 2 of Saccharomyces cerevisiae II: Both full size and processed enzymes are active for chitin synthesis (1996), J. Biochem., 119, 659-666.
    View publication on PubMed
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Cloned(Commentary)

Cloned (Comment) Organism
since chitin synthase 2 can not expressed in bacterial cells or insect cells in an active form, Saccharomyces cerevisiae is used as the host for overexpression Saccharomyces cerevisiae

Inhibitors

Inhibitors Comment Organism Structure
Nikkomycin nikkomycin Z Saccharomyces cerevisiae
nikkomycin Z
-
 Saccharomyces cerevisiae

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ significant chitin synthase activity in the presence of Mg2+ or Mn2+, even without trypsin treatment Saccharomyces cerevisiae
Mn2+ significant chitin synthase activity in the presence of Mg2+ or Mn2+, even without trypsin treatment Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
 chitin synthetase 2
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification chitin synthase 2 activity is independent of the N-terminal 193 amino acid truncation, because partially purified full length enzyme also exhibits the activity without trypsin treatment in the presence of appropriate cations Saccharomyces cerevisiae

Purification (Commentary)

Purification (Comment) Organism
-
 Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
-
 Saccharomyces cerevisiae UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
 ?

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.0068
-
 nikkomycin Z
-
 Saccharomyces cerevisiae