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Literature summary for 2.4.1.16 extracted from
- Biochemical characterization of chitin synthase activity and inhibition in the African malaria mosquito, Anopheles gambiae (2013), Insect Sci., 20, 158-166.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| N-acetyl-alpha-D-glucosamine | stimulates CHS activity at 2.5 mM but inhibits enzyme activity at higher concentrations | Anopheles gambiae |  |
| UDP-N-acetyl-alpha-D-glucosamine | - |
Anopheles gambiae | |
General Stability
| General Stability | Organism |
|---|---|
| dithithreitol is required to prevent melanization of the enzyme extract | Anopheles gambiae |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Diflubenzuron | slight in vitro inhibition | Anopheles gambiae | |
| Mg2+ | low concentration of Mg2+ at 1.0-4.0 mmol/l significantly increase CHS activity, whereas 10.0 mmol/l or higher significantly inhibit CHS enzyme activity | Anopheles gambiae | |
| additional information | no in vitro inhibition by polyoxin D. Inhibition of chitin synthesis by the chemicals is not due to direct inhibition of chitin synthase in Anopheles gambiae | Anopheles gambiae | |
| nikkomycin Z | slight in vitro inhibition | Anopheles gambiae | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| intracellular | - |
Anopheles gambiae | 5622 | - |
| membrane | transmembrane protein, the insect chitin synthase contains multiple transmembrane helices reflecting their association with either the plasma membrane or intracellular vesicles such as chitosomes | Anopheles gambiae | 16020 | - |
| plasma membrane | - |
Anopheles gambiae | 5886 | - |
| vesicle | - |
Anopheles gambiae | 31982 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | low concentration of Mg2+ at 1.0-4.0 mmol/l significantly increase CHS activity, whereas 10.0 mmol/l or higher significantly inhibit CHS enzyme activity | Anopheles gambiae | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| UDP-N-acetyl-alpha-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n | Anopheles gambiae | - |
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1 | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Anopheles gambiae | - |
two CHS genes, AgCHS1 and AgCHS2 | - |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| proteolytic modification | proteolytic activation of CHS activity | Anopheles gambiae |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| pupa | both two CHS genes, AgCHS1 and AgCHS2, are highly expressed in the pupal stage | Anopheles gambiae | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | method optimzation to assay chitin synthase activity, overview | Anopheles gambiae | ? | - |
? | |
| UDP-N-acetyl-alpha-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n | - |
Anopheles gambiae | UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1 | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| CHS | - |
Anopheles gambiae |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | 44 | - |
Anopheles gambiae |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
cell-free enzyme extract, pH 7.5, stable for over 60 min | Anopheles gambiae |
| 95 | - |
cell-free enzyme extract, pH 7.5, 10 min, inactivation | Anopheles gambiae |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6.5 | 7 | - |
Anopheles gambiae |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | the enzyme belongs to the family of beta-glycosyltransferases | Anopheles gambiae |
| metabolism | chitin production in arthropods is a complicated process and a series of biochemical pathways are involved in individual chitin polymer biosynthesis in which the terminal step is catalyzed by chitin synthase | Anopheles gambiae |
| physiological function | CHS catalyzes the transfer of sugar moieties from activated sugar donors to specific acceptors in all chitin-containing organisms | Anopheles gambiae |
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