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