FACTORS INVOLVED IN THE BACTERIAL DECARBOXYLATION OF SUCCINIC ACID

1961 ◽  
Vol 7 (6) ◽  
pp. 889-893
Author(s):  
A. A. Yousten ◽  
E. A. Delwiche
Keyword(s):  
Succinic Acid ◽  
Adenosine Triphosphate ◽  
Coenzyme A ◽  
Magnesium Ions

The succinic decarboxylase system of Veillonella alcalescens loses activity when aged at 2 °C for a few days. Evolution of CO2 by aged extracts of this organism was greatly stimulated by boiled cell-free extracts of Propionibacterium pentosaceum. These boiled extracts could not be replaced by coenzyme A (CoA), adenosine triphosphate (ATP), magnesium ions, biotin, or dimethylbenzimidazolylcobamide coenzyme (DBC).

The role of adenosine triphosphate citrate lyase in the metabolism of acetyl coenzyme a and function of blood platelets in diabetes mellitus

Metabolism ◽  
2004 ◽  
Vol 53 (1) ◽  
pp. 66-72 ◽  
Author(s):  
Anna Michno ◽  
Anna Skibowska ◽  
Anna Raszeja-Specht ◽  
Justyna Ćwikowska ◽  
Andrzej Szutowicz
Keyword(s):  
Diabetes Mellitus ◽  
Adenosine Triphosphate ◽  
Coenzyme A ◽  
Blood Platelets ◽  
Acetyl Coenzyme A ◽  
Acetyl Coenzyme ◽  
Citrate Lyase ◽  
And Function

Solubility of palmitoyl-coenzyme A in acyltransferase assay buffers containing magnesium ions

1986 ◽  
Vol 250 (1) ◽  
pp. 267-270 ◽  
Author(s):  
Panayiotis P. Constantinides ◽  
Joseph M. Steim
Keyword(s):  
Coenzyme A ◽  
Magnesium Ions

BIOSYNTHESIS OF LIPIDS IN PLANTS: II. INCORPORATION OF GLYCEROPHOSPHATE-32P INTO PHOSPHATIDES BY CELL-FREE PREPARATIONS FROM SPINACH LEAVES

1966 ◽  
Vol 44 (4) ◽  
pp. 459-467 ◽  
Author(s):  
P. S. Sastry ◽  
M. Kates
Keyword(s):  
Adenosine Triphosphate ◽  
Lysophosphatidic Acid ◽  
Coenzyme A ◽  
Phosphatidyl Inositol ◽  
Phosphatidyl Glycerol ◽  
Enzyme Systems ◽  
Microsome Fraction ◽  
Chloroplast Fraction ◽  
Phosphatide Acid ◽  
Spinach Leaves

Cell-free homogenates of spinach leaves incorporated glycerophosphate-32P into phosphatides when supplied with adenosine triphosphate, Mg++and coenzyme A (CoA). Most of the activity of the homogenate was associated with the microsome fraction sedimented at 104,000 × g, but some activity was also present in the chloroplast fraction. In all systems, most of the32P incorporated appeared in phosphatide acid (+ lysophosphatidic acid), with small to trace amounts in phosphatidyl glycerol and phosphatidyl inositol. Coenzyme A and adenosine triphosphate + Mg++were obligatory cofactors for the incorporation of α-glycerophosphate-32P but acetate + bicarbonate, cytidine triphosphate, or light were not essential. The results demonstrate the presence of acyl-CoA:L-glycerol-3-phosphate O-acyltransferase in the microsome fraction of spinach leaves and also indicate the existence of enzyme systems catalyzing the conversion of phosphatidic acid to phosphatidyl inositol and phosphatidyl glycerol.

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