Activating Compound | Comment | Organism | Structure |
---|---|---|---|
EDTA | - |
Nilaparvata lugens |
Cloned (Comment) | Organism |
---|---|
gene NlnCDase, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of the enzyme in insect High Five cells in microsomes, quantitative enzyme expression analysis | Nilaparvata lugens |
Protein Variants | Comment | Organism |
---|---|---|
additional information | NlnCDase knockdown by specific RNA interference | Nilaparvata lugens |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
Cs+ | - |
Nilaparvata lugens | |
EGTA | - |
Nilaparvata lugens | |
Fe2+ | - |
Nilaparvata lugens |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
additional information | the enzyme has a putative signal peptide of 25 residues at the N-terminal | Nilaparvata lugens | - |
- |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | activates | Nilaparvata lugens | |
additional information | the enzyme activity is not affected by Mg2+, Mn2+, Ni+, and Zn2+ | Nilaparvata lugens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Nilaparvata lugens | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
adult | - |
Nilaparvata lugens | - |
egg | - |
Nilaparvata lugens | - |
head | - |
Nilaparvata lugens | - |
leg | - |
Nilaparvata lugens | - |
midgut | - |
Nilaparvata lugens | - |
additional information | the NlnCDase has higher transcript level and activity in adults than in eggs and nymphs, and in the reproductive organs (ovaries and spermaries) than in other tissues (i.e. heads, thorax, legs, midguts) | Nilaparvata lugens | - |
nymph | - |
Nilaparvata lugens | - |
ovary | - |
Nilaparvata lugens | - |
semen | - |
Nilaparvata lugens | - |
thorax | - |
Nilaparvata lugens | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
C12:0-ceramide + H2O | preferred substrate | Nilaparvata lugens | laurate + sphingosine | - |
? | |
C16:0-ceramide + H2O | low activity | Nilaparvata lugens | palmitate + sphingosine | - |
? | |
C20:0-ceramide + H2O | low activity | Nilaparvata lugens | arachidic acid + sphingosine | - |
? | |
C24:0-ceramide + H2O | low activity | Nilaparvata lugens | lignoceric acid + sphingosine | - |
? | |
C2:0-ceramide + H2O | low activity | Nilaparvata lugens | acetate + sphingosine | - |
? | |
C6:0-ceramide + H2O | - |
Nilaparvata lugens | hexanoate + sphingosine | - |
? | |
additional information | recombinant NlnCDase shows a broad capacity to hydrolyze different ceramide varieties and has a preference for the short and medium chain ceramide, the substrate preference in descending order is C12-ceramide, C6-ceramide, and C16-ceramide. The enzyme shows low activity for the very-short chain C2-ceramide and the long chain substrates C20-ceramide and C24-ceramide | Nilaparvata lugens | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 80213, sequence calculation | Nilaparvata lugens |
Synonyms | Comment | Organism |
---|---|---|
neutral ceramidase | - |
Nilaparvata lugens |
NlnCDase | - |
Nilaparvata lugens |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
36 | - |
recombinant enzyme | Nilaparvata lugens |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6 | - |
recombinant enzyme | Nilaparvata lugens |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
additional information | - |
NlnCDase enzyme has a broad pH range for its activity | Nilaparvata lugens |
Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|
Nilaparvata lugens | sequence calculation | - |
5.85 |
Organism | Comment | Expression |
---|---|---|
Nilaparvata lugens | transcripts and activity of the NlnCDase are upregulated under abiotic stresses including starvation, abnormal temperature, and insecticides, and biotic stress of resistant rice varieties | up |
General Information | Comment | Organism |
---|---|---|
malfunction | knocking down NlnCDase by RNA interference increases female survival under starvation and temperature stresses | Nilaparvata lugens |
physiological function | neutral ceramidase, NlnCDase, is involved in the stress responses of brown planthopper, Nilaparvata lugens. The NlnCDase level might be elevated in adult reproductive organs to mediate developmental process. NlnCDase might be involved in the stress response | Nilaparvata lugens |