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Literature summary for 2.7.11.19 extracted from

  • Herrera, J.E.; Thompson, J.A.; Rimmer, M.A.; Nadeau, O.W.; Carlson, G.M.
    Activation of phosphorylase kinase by physiological temperature (2015), Biochemistry, 54, 7524-7530.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.11.19

Activating Compound

Activating Compound Comment Organism Structure
additional information activation of phosphorylase kinase by physiological temperature Oryctolagus cuniculus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information the rate of product formation by the basal activity of PhK is not linear Oryctolagus cuniculus

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ required Oryctolagus cuniculus
Mg2+ required Oryctolagus cuniculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 ATP + phosphorylase b Oryctolagus cuniculus
-
 2 ADP + phosphorylase a
-
 ?
2 ATP + phosphorylase b Oryctolagus cuniculus New Zealand White
-
 2 ADP + phosphorylase a
-
 ?

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus P18688 AND P12798 subunits a and b
-
Oryctolagus cuniculus New Zealand White P18688 AND P12798 subunits a and b
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein the phoshorylase kinase i phosphorylated and activated Oryctolagus cuniculus

Source Tissue

Source Tissue Comment Organism Textmining
skeletal muscle
-
 Oryctolagus cuniculus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.05
-
 nonphosphorylated enzyme PhK, pH 6.8, 30°C Oryctolagus cuniculus
0.67
-
 nonphosphorylated enzyme PhK, pH 6.8, 40°C Oryctolagus cuniculus
1.3
-
 phosphorylated enzyme PhK, pH 6.8, 30°C Oryctolagus cuniculus
2.5
-
 nonphosphorylated enzyme PhK, pH 8.2, 30°C Oryctolagus cuniculus
3.09
-
 phosphorylated enzyme PhK, pH 6.8, 40°C Oryctolagus cuniculus
3.1
-
 phosphorylated enzyme PhK, pH 8.2, 30°C Oryctolagus cuniculus
6.7
-
 nonphosphorylated enzyme PhK, pH 8.2, 40°C Oryctolagus cuniculus
7.4
-
 phosphorylated enzyme PhK, pH 8.2, 40°C Oryctolagus cuniculus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 ATP + phosphorylase b
-
 Oryctolagus cuniculus 2 ADP + phosphorylase a
-
 ?
2 ATP + phosphorylase b
-
 Oryctolagus cuniculus New Zealand White 2 ADP + phosphorylase a
-
 ?

Synonyms

Synonyms Comment Organism
PhK
-
 Oryctolagus cuniculus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
40
-
 activation of phosphorylase kinase by physiological temperature Oryctolagus cuniculus

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
-
 40 the activity at pH 6.8 of nonphosphorylated PhK predictably increases, but between 30°C and 40°C, there is a dramatic jump in activity, resulting in the nonactivated enzyme having a far greater activity at body temperature than was previously realized. Both stimulation (by ADP and phosphorylation) and inhibition (by phosphate) were considerably less pronounced at 40°C than at 30°C. The probable underlying mechanism for the dramatic increase in PhK's activity between 30°C and 40°C is an abrupt change in the conformations of the regulatory beta and catalytic gamma subunits between these two temperatures. Activity profiles, overview Oryctolagus cuniculus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.8
-
 assay at Oryctolagus cuniculus

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Oryctolagus cuniculus