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when functioning with hydrophobic electron acceptor essential in both leaflets of the membrane
-
stimulates in presence of Triton X-100
-
specific activation of enzyme in liposomes. Activation is due to promotion of iron-sulfur (M80) bond breaking and also due to facilitation of H2O2 penetration to the reaction center
-
strict concurrency between iron-sulfur of M80 bond breaking and enzyme activity enhancement at molar ratios of cardiolipin/cytochrome c of 0:1 to 50:1. Cardiolipin is 20times more effective than sodium dodecylsulfate, cardiolipin-activitated activity is reduced by high ionic strength solution, e.g. 1 M KCl
-
affinity of P-450scc for cholesterol is increased
-
most potent and effective activator lipid, binds to enzyme and enhances the binding of cholesterol
-
2.2fold activation at 0.5 mg/ml
-
stimulation in presence of detergent
stimulation in presence of detergent
10fold stimulation of partially purified enzyme with Escherichia coli cardiolipin
-
cardiolipin liposomes induce nitrite reductase activity of Fe(II)-cytc. The values observed can be compared with the kinetics of the NO2-mediated conversion of other ferrous heme-proteins. Cardiolipins facilitate the NO2-mediated nitrosylation of cytc-Fe(II) in a dose-dependent manner inducing the penta-coordination of the heme-Fe(II) atom
-
activation of reconstituted mitochondrial enzyme
-
inhibits conversion of palmitoylcarnitine to palmitoyl-CoA, stimulates palmitoylcarnitine formation
-
SIRT5 electrostatically binds to cardiolipin, an N-terminal amphipathic helix mediates SIRT5 binding to cardiolipin, cardiolipin activates desuccinylation of membrane proteins
-
activation, 35% as effective as phosphatidylethanolamine
-
no endogenous compound of strain A-EF22
-
very strong stimulation in the presence of 1,3-dioleoylglycerol
-
from bovine, 50% of activation with 1,2-dioleoylphosphatidylglycerol
-
required for full activity, activates up to 10fold, 14-18 molecules of cardiolipin are bound to one molecule of enzyme
-
the bacterial enzyme is strictly associated with cardiolipin and the catalytic activity is dependent on such lipid
-
the activity of MurG is increased in the presence of cardiolipin
-
presence of 1 mM in assay, enhances activity
-
from bovine, enhancement factor: 0.8 in absence of Triton X-100, 0.1 in presence of 0.1% Triton X-100
-
Lactobacillus plantarum, Escherichia coli, and bovine cardiolipin. Good activator in absence of detergent
-
marked effect in activating lipid-depleted enzyme
-
half-maximal activation by 1 mol%
-
mitochondrial, half-maximal activation at 2.3 mol%
-
other phospholipids including phosphatidylethanolamine, phosphatidylserine, phosphatidylcholine and phosphatidylglycerol are not as effective as cardiolipin
-
activates isozyme PKNalpha
-
activates, phosphorylation of beta2-AR
-
stimulates 6fold at 0.36 mM
-
stimulates activity of enzyme in endoplasmic membrane vesicles, due to better solubilization of the dolichol phosphate
-
activates. The enzyme is completely desensitized by treatment for 5 min at 40°C against the effect of cadiolipin without loss of activity
-
membrane association and activity of PtdSer synthase is increased, studied with mixed micelles containing phosphatidylglycerol (one charge) or diphosphatidylglycerol (two charges), the two main anionic membrane lipids in Escherichia coli
-
cytosolic isoform PLA2beta action on phosphatidylcholine vesicles is activated by anionic phosphoinositides and cardiolipin
-
activation, antagonized by sphinganine
-
PAH1-encoded PAP activity is enhanced by the phospholipids CDP-diacylglycerol, phosphatidylinositol, and cardiolipin
-
0.1 mM, approx. 40fold activation
-
anionic phospholipids required for activity, maximal activation at 1 mM, 21% of activation with phosphatidylserine
-
enzymatic activity is induced 23fold at 0.1 mM
-
from bovine liver, activates by 68% at 1 mM
-
enhances DegP proteolytic activity at high temperatures
-
activates the ceramidase activity by 2.5fold at 8-10 mol%, inhibits the ceramide synthesis activity, mechanism
-
phosphatidylglycerol and cardiolipin, which are major lipid components of Staphylococcus aureus, are effective in stimulating the hydrolysis of human skin-type ceramides in the absence of detergents
-
Drp1 binding to anionic lipids such as cardiolipin increases its GTPase activity
-
stimulates Drp1, synergistically with mitochondrial fission factor
-
activates the enzyme with the optimum concentration at 0.04 mg/ml
-
activation if horse heart or Candida krusei cytchrome c are used as electron donors
activation if horse heart or Candida krusei cytchrome c are used as electron donors
activation if horse heart or Candida krusei cytchrome c are used as electron donors
activation if horse heart or Candida krusei cytchrome c are used as electron donors
activation if horse heart or Candida krusei cytchrome c are used as electron donors
activation if horse heart or Candida krusei cytchrome c are used as electron donors
activation if horse heart or Candida krusei cytchrome c are used as electron donors
activation if horse heart or Candida krusei cytchrome c are used as electron donors
activation if horse heart or Candida krusei cytchrome c are used as electron donors
activation if horse heart or Candida krusei cytchrome c are used as electron donors
activation if horse heart or Candida krusei cytchrome c are used as electron donors
activation if horse heart or Candida krusei cytchrome c are used as electron donors
activation if horse heart or Candida krusei cytchrome c are used as electron donors
activation if horse heart or Candida krusei cytchrome c are used as electron donors
activation if horse heart or Candida krusei cytchrome c are used as electron donors
activation if horse heart or Candida krusei cytchrome c are used as electron donors
activation if horse heart or Candida krusei cytchrome c are used as electron donors
activation if horse heart or Candida krusei cytchrome c are used as electron donors
activation if horse heart or Candida krusei cytchrome c are used as electron donors
activation if horse heart or Candida krusei cytchrome c are used as electron donors
activation if horse heart or Candida krusei cytchrome c are used as electron donors
activation if horse heart or Candida krusei cytchrome c are used as electron donors
activation if horse heart or Candida krusei cytchrome c are used as electron donors
activation if horse heart or Candida krusei cytchrome c are used as electron donors
activation if horse heart or Candida krusei cytchrome c are used as electron donors
activation if horse heart or Candida krusei cytchrome c are used as electron donors
activation if horse heart or Candida krusei cytchrome c are used as electron donors
approx. 10fold stimulation
approx. 10fold stimulation
approx. 10fold stimulation
approx. 10fold stimulation
approx. 10fold stimulation
approx. 10fold stimulation
approx. 10fold stimulation
approx. 10fold stimulation
approx. 10fold stimulation
approx. 10fold stimulation
approx. 10fold stimulation
approx. 10fold stimulation
approx. 10fold stimulation
approx. 10fold stimulation
approx. 10fold stimulation
approx. 10fold stimulation
approx. 10fold stimulation
approx. 10fold stimulation
approx. 10fold stimulation
approx. 10fold stimulation
approx. 10fold stimulation
approx. 10fold stimulation
approx. 10fold stimulation
approx. 10fold stimulation
approx. 10fold stimulation
approx. 10fold stimulation
approx. 10fold stimulation
stimulation of reaction with horse ferrocytochrome c, reactivity with cytochrome c550 is not affected
stimulation of reaction with horse ferrocytochrome c, reactivity with cytochrome c550 is not affected
stimulation of reaction with horse ferrocytochrome c, reactivity with cytochrome c550 is not affected
stimulation of reaction with horse ferrocytochrome c, reactivity with cytochrome c550 is not affected
stimulation of reaction with horse ferrocytochrome c, reactivity with cytochrome c550 is not affected
stimulation of reaction with horse ferrocytochrome c, reactivity with cytochrome c550 is not affected
stimulation of reaction with horse ferrocytochrome c, reactivity with cytochrome c550 is not affected
stimulation of reaction with horse ferrocytochrome c, reactivity with cytochrome c550 is not affected
stimulation of reaction with horse ferrocytochrome c, reactivity with cytochrome c550 is not affected
stimulation of reaction with horse ferrocytochrome c, reactivity with cytochrome c550 is not affected
stimulation of reaction with horse ferrocytochrome c, reactivity with cytochrome c550 is not affected
stimulation of reaction with horse ferrocytochrome c, reactivity with cytochrome c550 is not affected
stimulation of reaction with horse ferrocytochrome c, reactivity with cytochrome c550 is not affected
stimulation of reaction with horse ferrocytochrome c, reactivity with cytochrome c550 is not affected
stimulation of reaction with horse ferrocytochrome c, reactivity with cytochrome c550 is not affected
stimulation of reaction with horse ferrocytochrome c, reactivity with cytochrome c550 is not affected
stimulation of reaction with horse ferrocytochrome c, reactivity with cytochrome c550 is not affected
stimulation of reaction with horse ferrocytochrome c, reactivity with cytochrome c550 is not affected
stimulation of reaction with horse ferrocytochrome c, reactivity with cytochrome c550 is not affected
stimulation of reaction with horse ferrocytochrome c, reactivity with cytochrome c550 is not affected
stimulation of reaction with horse ferrocytochrome c, reactivity with cytochrome c550 is not affected
stimulation of reaction with horse ferrocytochrome c, reactivity with cytochrome c550 is not affected
stimulation of reaction with horse ferrocytochrome c, reactivity with cytochrome c550 is not affected
stimulation of reaction with horse ferrocytochrome c, reactivity with cytochrome c550 is not affected
stimulation of reaction with horse ferrocytochrome c, reactivity with cytochrome c550 is not affected
stimulation of reaction with horse ferrocytochrome c, reactivity with cytochrome c550 is not affected
stimulation of reaction with horse ferrocytochrome c, reactivity with cytochrome c550 is not affected
stimulation with non-physiological electron donors
stimulation with non-physiological electron donors
stimulation with non-physiological electron donors
stimulation with non-physiological electron donors
stimulation with non-physiological electron donors
stimulation with non-physiological electron donors
stimulation with non-physiological electron donors
stimulation with non-physiological electron donors
stimulation with non-physiological electron donors
stimulation with non-physiological electron donors
stimulation with non-physiological electron donors
stimulation with non-physiological electron donors
stimulation with non-physiological electron donors
stimulation with non-physiological electron donors
stimulation with non-physiological electron donors
stimulation with non-physiological electron donors
stimulation with non-physiological electron donors
stimulation with non-physiological electron donors
stimulation with non-physiological electron donors
stimulation with non-physiological electron donors
stimulation with non-physiological electron donors
stimulation with non-physiological electron donors
stimulation with non-physiological electron donors
stimulation with non-physiological electron donors
stimulation with non-physiological electron donors
stimulation with non-physiological electron donors
stimulation with non-physiological electron donors
the hydrolytic activity of CopA is stimulated by phosphoholipid cardiolipin and to some extent by phosphatidylglycerol. The amphipathic platform helix MBC of CopA shows a significant preference for interaction with cardiolipin
-
stimulates activity of full-length GspEEpsE when in complex with the cytoplasmic domain of GspLEpsL
-
stimulates, K417 and K419 contribute to EpsE's ability to be stimulated by cardiolipin
-
via the EpsE/cyto-EpsL complex
-
binds the co-purified EpsE/cyto-EpsL complex and stimulates its ATPase activity 30-130fold, whereas the activity of EpsE alone is unaffected. Removal of the last 11 residues, residues 243-253, from cyto-EpsL prevents cardiolipin binding as well as stimulation of the ATPase activity of EpsE
-
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