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Literature summary for 2.4.1.16 extracted from

  • Gay, L.; Hebraud, M.; Girard, V.; Fevre, M.
    Chitin synthase activity from Neocallimastix frontalis, an anaerobic rumen fungus (1989), J. Gen. Microbiol., 135, 279-283.
No PubMed abstract available

Activating Compound

Activating Compound Comment Organism Structure
GlcNAc 20 mM stimulates, allosteric activator Neocallimastix frontalis

Inhibitors

Inhibitors Comment Organism Structure
Polyoxin D
-
Neocallimastix frontalis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2
-
UDP-GlcNAc
-
Neocallimastix frontalis

Localization

Localization Comment Organism GeneOntology No. Textmining
plasma membrane
-
Neocallimastix frontalis 5886
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ divalent cation required for maximal activity, Mg2+ is most efficient Neocallimastix frontalis

Organism

Organism UniProt Comment Textmining
Neocallimastix frontalis
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification following treatment with trypsin, the chitin synthase activity is increased by 6fold, indicating that most of the chitin synthase activity is zymogenic Neocallimastix frontalis

Source Tissue

Source Tissue Comment Organism Textmining
mycelium
-
Neocallimastix frontalis
-

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
-
Neocallimastix frontalis UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1 chitin ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
32
-
-
Neocallimastix frontalis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
10 mM Tris/HCl buffer Neocallimastix frontalis

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.004
-
Polyoxin D
-
Neocallimastix frontalis