2.7.11.19 (NH4)2SO4 activation, 0.05-0.1 M, inhibits above 0.2 M 492104 2.7.11.19 Ba2+ - 492109 2.7.11.19 Ba2+ activation, can replace Ca2+ with 26% efficiency 492109 2.7.11.19 Ba2+ activation, can replace Ca2+ with 60% efficiency 492095 2.7.11.19 Ca2+ - 492100, 492104, 492106, 492109, 492120, 492122, 492123, 492124, 492125, 492129, 492154, 662844, 675419 2.7.11.19 Ca2+ 12 mol Ca2+ per mol (alphabetagammadelta)4 492102 2.7.11.19 Ca2+ activated by Ca2+ 706785 2.7.11.19 Ca2+ activates 762340, 762341 2.7.11.19 Ca2+ activates, binding structure modeling, Ca2+-binding induces structural perturbation of the subunits and promotes redistribution of density throughout the lobes and bridges of the enzyme structure 663335 2.7.11.19 Ca2+ activates, dependent on, required for binding of calmodulin 661075 2.7.11.19 Ca2+ activates, the four integral delta subunits of the phosphorylase kinase complex are identical to calmodulin and confer Ca2+ sensitivity to the enzyme, but bind independently of Ca2+, Ca2+ influences the conformational substrates of the subunits, overview 677024 2.7.11.19 Ca2+ activation, 0.0001-0.001 mM, inhibits above 0.001 mM 492115 2.7.11.19 Ca2+ allosteric mechanism 492101 2.7.11.19 Ca2+ binding studies 492102 2.7.11.19 Ca2+ Ca2+ stimulates enzyme activity 761263 2.7.11.19 Ca2+ Ca2+-dependent reaction 685264 2.7.11.19 Ca2+ Ca2+-independent activity: A0 492116, 492117 2.7.11.19 Ca2+ Ca2+-sensitivity of the enzyme is mediated by the delta-subunit which is identical with calmodulin 650575 2.7.11.19 Ca2+ delta-subunit confers Ca2+-sensitivity to the phosphorylase kinase reaction 492110 2.7.11.19 Ca2+ dependent on 663347, 740074, 740540 2.7.11.19 Ca2+ dependent on, induces enzyme self-association and increases interaction with glycogen 662670 2.7.11.19 Ca2+ induces association, obligatory allosteric activator, binds to an integral, nondissociable molecule of calmodulin (delta-subunit), and thus reveals the protein kinase activity of the catalytic gamma-subunit, which in the absence of Ca2+ ions is constrained by the regulatory alpha- and beta-subunits 691329 2.7.11.19 Ca2+ irreversible activation of nonactivated kinase by preincubation together with a separate kinase-activating factor independent of cAMP, kinetics 492095 2.7.11.19 Ca2+ is an obligatory allosteric activator absolutely required by the enzyme, Ca2+ activates PhK by binding to its nondissociable calmodulin subunits, it couples the cascade activation of glycogenolysis with muscle contraction, enzyme surface electrostatic properties of solvent accessible charged and polar groups are altered upon the binding of Ca2+ ions 677034 2.7.11.19 Ca2+ isolated delta-subunit from rabbit has 4 Ca2+-binding sites of which 2 are lost at high ionic strength and 2 Mg2+/Ca2+-binding sites that can bind either ion, treatment of gammadelta-subunit complex with EGTA with following centrifugation leads to Ca2+-independent catalytic activity 492101 2.7.11.19 Ca2+ not 492092 2.7.11.19 Ca2+ phosphorylase kinase is a Ca2+-regulated, multisubunit enzyme that contains calmodulin as an integral subunit, the gamma-subunit of skeletal muscle phosphorylase kinase contains two noncontiguous domains that act in concert to bind calmodulin 491215 2.7.11.19 Ca2+ required 695055, 740075, 740638, 740880, 741081 2.7.11.19 Ca2+ required for activity 702389, 760477 2.7.11.19 Ca2+ required for activity and activation 492101, 492117 2.7.11.19 Ca2+ required for complex formation 672305 2.7.11.19 Ca2+ required for efficient substrate binding of active and nonactivated enzyme and for maximal catalysis of active enzyme 492105 2.7.11.19 Ca2+ required, binds to the delta subunit 695012 2.7.11.19 Ca2+ required, interacts with the delta subunit 690324 2.7.11.19 Ca2+ requirement 492101, 492106, 492107, 492109, 492123, 492126, 492132 2.7.11.19 Ca2+ requirement (trypsin activation leads to loss of absolute requirement) 492110 2.7.11.19 Ca2+ stabilization, no absolute requirement for catalytic subunit gamma2 492108 2.7.11.19 Ca2+ stimulates autophosphorylation in micromolar range at pH 6.8, inhibits at millimolar range 492117 2.7.11.19 Ca2+ stimulates phosphorylase b binding to enzyme, but to a considerable lesser extent than Mg2+ 492155 2.7.11.19 Ca2+ synergism with Mg2+ 492101, 492111, 492112 2.7.11.19 Calcium dependent on 491218 2.7.11.19 Cd2+ can partially substitue Mg2+ 490935 2.7.11.19 Co2+ activation, can replace Ca2+ with 10% efficiency 492109 2.7.11.19 Co2+ can partially substitue Mg2+ 490935 2.7.11.19 Co2+ not 492095 2.7.11.19 Fe3+ activation, can replace Ca2+ with 10% efficiency 492109 2.7.11.19 Fe3+ not 492095 2.7.11.19 Li+ activation 492106, 492109 2.7.11.19 Li+ can replace Ca2+ with 10% efficiency 492109 2.7.11.19 Li+ LiBr 492106 2.7.11.19 Mg2+ - 490796, 490797, 490800, 490801, 662844, 663347, 675419, 675990, 677024, 677034 2.7.11.19 Mg2+ 10 mM 492113, 492129 2.7.11.19 Mg2+ activator, changes in the physicochemical properties of the enzyme induced by Mg2+ under nonactivating (pH 6.8) and activating (pH 8.2) conditions are investigated by circular dichroism spectroscopy, zeta potential analyses, dynamic light scattering, second derivative UV absorption, negative stain electron microscopy, and differential chemical crosslinking. The effects of the activator Mg2+ on some of the properties of the enzyme measured by these techniques are quite different at the two pH values. 728763 2.7.11.19 Mg2+ allosteric effector, rabbit delta-subunit has two Mg2+/Ca2+-binding sites that can bind either ion 492101 2.7.11.19 Mg2+ can replace Mn2+ 492092 2.7.11.19 Mg2+ dependent on, induces enzyme self-association and increases interaction with glycogen 662670 2.7.11.19 Mg2+ dependent on, Mg2+ is the physiologic metal ion, other divalent cations are able to support nucleotide binding, but only Mn2+, Co2+, and Cd2+ can substitute Mg2+ in supporting the catalytic activity 490935 2.7.11.19 Mg2+ effect of Mg2+ on Ca2+-binding properties of nonactivated enzyme at pH 6.8 492102 2.7.11.19 Mg2+ enzyme catalyzes its own phosphorylation (i.e. alpha and beta subunits, not gammadelta subunit complex) in the presence of MgATP2- and Ca2+ 492101 2.7.11.19 Mg2+ free Mg2+ inhibits activated enzyme 492129 2.7.11.19 Mg2+ free Mg2+ stimulates (nonactivated enzyme) 492129 2.7.11.19 Mg2+ greatly enhances affinity for phosphorylase b 492155 2.7.11.19 Mg2+ induces association 691329 2.7.11.19 Mg2+ major role of Mg2+: cosubstrate in Mg2+-ATP complex 491214, 491218, 492092, 492093, 492094, 492095, 492096, 492097, 492098, 492099, 492100, 492101, 492102, 492103, 492104, 492105, 492106, 492107, 492108, 492109, 492110, 492111, 492112, 492113, 492114, 492115, 492116, 492117, 492118, 492119, 492120, 492121, 492122, 492123, 492124, 492125, 492126, 492128, 492129, 492130, 492131, 492132, 492133, 492134, 492135, 492136, 492137, 492138, 492139, 492140, 492141, 492142, 492143, 492144, 492145, 492146, 492147, 492148, 492149, 492150, 492151, 492152, 492154, 492155 2.7.11.19 Mg2+ Mg2+ added in excess of ATP concentration stimulates 492101 2.7.11.19 Mg2+ Mg2+ stimulates enzyme activity 761263 2.7.11.19 Mg2+ not 492095 2.7.11.19 Mg2+ required 740074, 740075, 740540, 740638, 740880, 741081 2.7.11.19 Mg2+ required for activity and activation (by autophosphorylation) 492115 2.7.11.19 Mg2+ required for activity phosphorylation by (cAMP-dependent protein kinase) 492101, 492112, 492115, 492125, 492129 2.7.11.19 Mg2+ required for complex formation and activity 672305 2.7.11.19 Mg2+ required in form of Mg2+ 760477 2.7.11.19 Mg2+ requirement 491214, 491218, 492092, 492093, 492094, 492095, 492096, 492097, 492098, 492099, 492100, 492101, 492102, 492103, 492104, 492105, 492106, 492107, 492108, 492109, 492110, 492111, 492112, 492113, 492114, 492115, 492116, 492117, 492118, 492119, 492120, 492121, 492122, 492123, 492124, 492125, 492126, 492128, 492129, 492130, 492131, 492132, 492133, 492134, 492135, 492136, 492137, 492138, 492139, 492140, 492141, 492142, 492143, 492144, 492145, 492146, 492147, 492148, 492149, 492150, 492151, 492152, 492154, 492155 2.7.11.19 Mg2+ synergism with Ca2+ 492101, 492111, 492112 2.7.11.19 Mn2+ activation 492125 2.7.11.19 Mn2+ at equimolar concentration of metal ion and ATP Mn2+ more effective than Mg2+ 492113 2.7.11.19 Mn2+ can partially substitue Mg2+ 490935 2.7.11.19 Mn2+ can replace Ca2+ with 15% efficiency 492109 2.7.11.19 Mn2+ can substitute for Ca2+ 492095 2.7.11.19 Mn2+ can substitute for Mg2+ 492094, 492113 2.7.11.19 Mn2+ can substitute for Mg2+ (less effective) 492107 2.7.11.19 Mn2+ enhances enzyme/phosphorylase b interaction more effectively 492155 2.7.11.19 Mn2+ free Mn2+ inhibits 492113 2.7.11.19 Mn2+ optimal at ATP:Mg ratio of 1:1 492092, 492113 2.7.11.19 Mn2+ requirement 492092, 492093, 492094, 492095, 492107, 492109, 492113, 492155 2.7.11.19 Mn2+ stimulates activation by catalytic subunit of cAMP-dependent protein kinase 492125 2.7.11.19 additional information Ca2+ and Mg2+ induce self-aggregation of PhK at 37°C 740540 2.7.11.19 additional information Fe2+, Zn2+ or Ni2+ 492095, 492109 2.7.11.19 additional information no activation by Cu2+, Cd2+, Sn2+, Al3+ 492109 2.7.11.19 additional information synopsis of activity by Ca2+/Mg2+ and phosphorylation 492146 2.7.11.19 additional information three separate activities can be characterized by their response to Ca2+, Mg2+, NH4Cl and pH: A0, A1 and A2 492116, 492117 2.7.11.19 phosphate 20 mol/mol holoenzyme, phosphate content of subunits 492130 2.7.11.19 phosphate alpha and beta subunits are phosphorylated by protein kinases or autophosphorylation 492122, 492123 2.7.11.19 phosphate alphagammadelta complex undergoes autophosphorylation: up to 4.2 mol phosphate/mol complex incorporated into alpha subunit 492113 2.7.11.19 phosphate contains 7.18-19 mol per mol (alphabetagammadelta)4 depending on phosphorylation status 492101 2.7.11.19 phosphate gammadelta subunit complex cannot phosphorylate itself but phosphorylates and activates native enzyme, even in the presence of EGTA or protein kinase inhibitor 492113 2.7.11.19 phosphate nonactivated enzyme is activated by phosphorylation 492101 2.7.11.19 phosphate requirement, phosphate containing enzyme 491214, 491218, 492092, 492093, 492094, 492095, 492096, 492097, 492098, 492099, 492100, 492101, 492102, 492103, 492104, 492105, 492106, 492107, 492108, 492109, 492110, 492111, 492112, 492113, 492114, 492115, 492116, 492117, 492118, 492119, 492120, 492121, 492122, 492123, 492124, 492125, 492126, 492128, 492129, 492130, 492131, 492132, 492133, 492134, 492135, 492136, 492137, 492138, 492139, 492140, 492141, 492142, 492143, 492144, 492145, 492146, 492147, 492148, 492149, 492150, 492151, 492152, 492154, 492155 2.7.11.19 Sr2+ activation, can replace Ca2+ with 45% efficiency 492109 2.7.11.19 Sr2+ activation, can replace Ca2+ with 60% efficiency 492095