EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
2.4.1.16 | N-acetyl-alpha-D-glucosamine | stimulates CHS activity at 2.5 mM but inhibits enzyme activity at higher concentrations | Anopheles gambiae | |
2.4.1.16 | UDP-N-acetyl-alpha-D-glucosamine | - |
Anopheles gambiae |
EC Number | General Stability | Organism |
---|---|---|
2.4.1.16 | dithithreitol is required to prevent melanization of the enzyme extract | Anopheles gambiae |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
2.4.1.16 | Diflubenzuron | slight in vitro inhibition | Anopheles gambiae | |
2.4.1.16 | 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 | |
2.4.1.16 | 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 | |
2.4.1.16 | nikkomycin Z | slight in vitro inhibition | Anopheles gambiae |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
2.4.1.16 | intracellular | - |
Anopheles gambiae | 5622 | - |
2.4.1.16 | 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 | - |
2.4.1.16 | plasma membrane | - |
Anopheles gambiae | 5886 | - |
2.4.1.16 | vesicle | - |
Anopheles gambiae | 31982 | - |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
2.4.1.16 | 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 |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.4.1.16 | 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 | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.4.1.16 | Anopheles gambiae | - |
two CHS genes, AgCHS1 and AgCHS2 | - |
EC Number | Posttranslational Modification | Comment | Organism |
---|---|---|---|
2.4.1.16 | proteolytic modification | proteolytic activation of CHS activity | Anopheles gambiae |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
2.4.1.16 | pupa | both two CHS genes, AgCHS1 and AgCHS2, are highly expressed in the pupal stage | Anopheles gambiae | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.4.1.16 | additional information | method optimzation to assay chitin synthase activity, overview | Anopheles gambiae | ? | - |
? | |
2.4.1.16 | 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 | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.4.1.16 | CHS | - |
Anopheles gambiae |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.4.1.16 | 37 | 44 | - |
Anopheles gambiae |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.4.1.16 | 37 | - |
cell-free enzyme extract, pH 7.5, stable for over 60 min | Anopheles gambiae |
2.4.1.16 | 95 | - |
cell-free enzyme extract, pH 7.5, 10 min, inactivation | Anopheles gambiae |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
2.4.1.16 | 6.5 | 7 | - |
Anopheles gambiae |
EC Number | General Information | Comment | Organism |
---|---|---|---|
2.4.1.16 | evolution | the enzyme belongs to the family of beta-glycosyltransferases | Anopheles gambiae |
2.4.1.16 | 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 |
2.4.1.16 | physiological function | CHS catalyzes the transfer of sugar moieties from activated sugar donors to specific acceptors in all chitin-containing organisms | Anopheles gambiae |