Separation of the Condensing Enzyme of Aspergillus niger from Acetyl Coenzyme A Deacylase and Citridesmolase and the Effect of Magnesium Ion on the Purified Fraction

Nature ◽  
1958 ◽  
Vol 182 (4649) ◽  
pp. 1601-1602 ◽  
Author(s):  
C. V. RAMAKRISHNAN
Keyword(s):  
Aspergillus Niger ◽  
Coenzyme A ◽  
Magnesium Ion ◽  
Acetyl Coenzyme A ◽  
Acetyl Coenzyme ◽  
Condensing Enzyme

THE ENZYMATIC SYNTHESIS OF CITRIC ACID BY CELL-FREE EXTRACTS OF ASPERGILLUS NIGER

1954 ◽  
Vol 32 (4) ◽  
pp. 434-439 ◽  
Author(s):  
C. V. Ramakrishnan ◽  
S. M. Martin
Keyword(s):  
Citric Acid ◽  
Calcium Phosphate ◽  
Aspergillus Niger ◽  
Ammonium Sulphate ◽  
Enzymatic Synthesis ◽  
Coenzyme A ◽  
Acetyl Coenzyme A ◽  
Acetyl Coenzyme ◽  
Ammonium Sulphate Fractionation ◽  
Condensing Enzyme

Cell-free extracts of Aspergillus niger, N.R.C. 233, have been shown to contain the enzymes necessary to catalyze the synthesis of citrate from ATP, acetate, and oxalacetate. The "condensing enzyme", which catalyzes the condensation of acetyl-coenzyme A and oxalacetate to yield citrate, has been isolated and purified approximately 50-fold by a combination of steps involving ammonium sulphate fractionation and calcium phosphate gel adsorption.

THE ENZYMATIC SYNTHESIS OF CITRIC ACID BY CELL-FREE EXTRACTS OF ASPERGILLUS NIGER

1954 ◽  
Vol 32 (1) ◽  
pp. 434-439 ◽  
Author(s):  
C. V. Ramakrishnan ◽  
S. M. Martin
Keyword(s):  
Citric Acid ◽  
Calcium Phosphate ◽  
Aspergillus Niger ◽  
Ammonium Sulphate ◽  
Enzymatic Synthesis ◽  
Coenzyme A ◽  
Acetyl Coenzyme A ◽  
Acetyl Coenzyme ◽  
Ammonium Sulphate Fractionation ◽  
Condensing Enzyme

Cell-free extracts of Aspergillus niger, N.R.C. 233, have been shown to contain the enzymes necessary to catalyze the synthesis of citrate from ATP, acetate, and oxalacetate. The "condensing enzyme", which catalyzes the condensation of acetyl-coenzyme A and oxalacetate to yield citrate, has been isolated and purified approximately 50-fold by a combination of steps involving ammonium sulphate fractionation and calcium phosphate gel adsorption.

scholarly journals Studies with Acetyl Coenzyme A and Condensing Enzyme in D2O

1958 ◽  
Vol 233 (3) ◽  
pp. 727-730 ◽  
Author(s):  
Abraham Marcus ◽  
Birgit Vennesland
Keyword(s):  
Coenzyme A ◽  
Acetyl Coenzyme A ◽  
Acetyl Coenzyme ◽  
Condensing Enzyme

scholarly journals Acetyl Coenzyme A Carboxylase

1969 ◽  
Vol 244 (22) ◽  
pp. 6254-6262 ◽  
Author(s):  
Philip W. Majerus ◽  
Elisabeth Kilburn
Keyword(s):  
Coenzyme A ◽  
Acetyl Coenzyme A ◽  
Acetyl Coenzyme ◽  
Acetyl Coenzyme A Carboxylase

scholarly journals Anti-Warburg Effect of Melatonin: A Proposed Mechanism to Explain its Inhibition of Multiple Diseases

2021 ◽  
Vol 22 (2) ◽  
pp. 764
Author(s):  
Russel J. Reiter ◽  
Ramaswamy Sharma ◽  
Sergio Rosales-Corral
Keyword(s):  
Pyruvate Dehydrogenase ◽  
Warburg Effect ◽  
Coenzyme A ◽  
Aerobic Glycolysis ◽  
Pyruvate Dehydrogenase Complex ◽  
Pyruvate Dehydrogenase Kinase ◽  
Metabolic Phenotype ◽  
Common Denominator ◽  
Acetyl Coenzyme A ◽  
Acetyl Coenzyme

Glucose is an essential nutrient for every cell but its metabolic fate depends on cellular phenotype. Normally, the product of cytosolic glycolysis, pyruvate, is transported into mitochondria and irreversibly converted to acetyl coenzyme A by pyruvate dehydrogenase complex (PDC). In some pathological cells, however, pyruvate transport into the mitochondria is blocked due to the inhibition of PDC by pyruvate dehydrogenase kinase. This altered metabolism is referred to as aerobic glycolysis (Warburg effect) and is common in solid tumors and in other pathological cells. Switching from mitochondrial oxidative phosphorylation to aerobic glycolysis provides diseased cells with advantages because of the rapid production of ATP and the activation of pentose phosphate pathway (PPP) which provides nucleotides required for elevated cellular metabolism. Molecules, called glycolytics, inhibit aerobic glycolysis and convert cells to a healthier phenotype. Glycolytics often function by inhibiting hypoxia-inducible factor-1α leading to PDC disinhibition allowing for intramitochondrial conversion of pyruvate into acetyl coenzyme A. Melatonin is a glycolytic which converts diseased cells to the healthier phenotype. Herein we propose that melatonin’s function as a glycolytic explains its actions in inhibiting a variety of diseases. Thus, the common denominator is melatonin’s action in switching the metabolic phenotype of cells.

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