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Literature summary for 2.7.11.11 extracted from
- cAMP-dependent protein kinase of Manduca sexta phosphorylates but does not activate the fat body triglyceride lipase (2004), Insect Biochem. Mol. Biol., 34, 1269-1279.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| adipokinetic hormone | rapid enzyme activation | Manduca sexta |  |
| cAMP | dependent on, 450% activation | Manduca sexta | |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | strong inhibition | Manduca sexta | |
| ethylmaleimide | complete inhibition at 2 mM | Manduca sexta | |
| genistein | partial inhibition | Manduca sexta | |
| H-89 | potent inhibitor of PKA | Manduca sexta | |
| HA1077 | partial inhibition | Manduca sexta | |
| Mn2+ | strong inhibition | Manduca sexta | |
| PKI | specific PKA inhibitor protein | Manduca sexta | |
| staurosporine | partial inhibition | Manduca sexta | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.031 | - |
Kemptide | pH 7.0, 22°C, catalytic subunit | Manduca sexta | |
| 0.039 | - |
ATP | pH 7.0, 22°C, catalytic subunit | Manduca sexta | |
| 0.039 | - |
ATP | ATP in form of MgATP2- | Manduca sexta | |
| 0.73 | - |
histone | pH 7.0, 22°C, catalytic subunit | Manduca sexta | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| cytosol | - |
Manduca sexta | 5829 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | absolutely required, as MgATP2-, best at 0.5 mM Mg2+, inhibitory at higher Mg2+ concentrations, cannot be substituted by Mn2+ | Manduca sexta | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 45100 | - |
1 * 45100, isolated catalytic subunit, SDS-PAGE | Manduca sexta |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Manduca sexta | the enzyme plays a central role in the adipokinetic signaling controling the mobilization of stored lipids in the fat body | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Manduca sexta | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| enzyme catalytic subunit from fat body 1773fold to homogeneity by ultracentrifugation and 3 steps of ion exchange chromatography | Manduca sexta |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| fat body | - |
Manduca sexta | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 0.266 | - |
purified catalytic subunit | Manduca sexta |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + fat body triglyceride lipase | protein substrate is phosphorylated at Ser563, but not activated by the enzyme, Ser563 is the regulatory site of the enzyme substrate | Manduca sexta | ADP + phosphorylated fat body triglyceride lipase | - |
? | |
| ATP + histone | - |
Manduca sexta | ADP + phosphorylated histone | - |
? | |
| ATP + Kemptide | - |
Manduca sexta | ADP + phosphorylated Kemptide | - |
? | |
| ATP + LRRASLG | i.e. Kemptide | Manduca sexta | ADP + LRRA-phosphoserine-LG | - |
? | |
| ATP + PLARTLSVAGLPGKK | syntide 2-derived peptide substrate | Manduca sexta | ADP + PLARTL-phosphoserine-VAGLPGKK | - |
? | |
| ATP + RFARKGSLRQKNV | PKC-derived peptide substrate | Manduca sexta | ADP + RFARKG-phosphoserine-LRQKNV | - |
? | |
| additional information | the enzyme plays a central role in the adipokinetic signaling controling the mobilization of stored lipids in the fat body | Manduca sexta | ? | - |
? | |
| additional information | substrate specificity, no activity with peptides derived from Thr-kinase or Tyr-kinase, overview | Manduca sexta | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| monomer | 1 * 45100, isolated catalytic subunit, SDS-PAGE | Manduca sexta |
| More | 2 catalytic subunits and 2 regulatory subunits form a tetramer, the inactive holoenzyme, upon cAMP binding the catalytic subunits are released as monomers and become catalytically active | Manduca sexta |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| PKA | - |
Manduca sexta |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 22 | - |
assay at room temperature | Manduca sexta |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
- |
Manduca sexta |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | as MgATP2- | Manduca sexta | |
Ki Value [mM]
| Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.000048 | - |
H-89 | pH 7.0, 22°C, catalytic subunit | Manduca sexta | |
pI Value
| Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|
| Manduca sexta | large differences between catalytic and regulatory subunits | - |
additional information |
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