Coenzyme for Acetylation, a Pantothenic Acid Derivative

Lipmann, Fritz; No, Kaplan

doi:10.1016/s0021-9258(17)30973-0

Cited by 190 publications

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“…7) agreed well with values of 0-65-0-71 jug. pantothenate/Lipmann unit reported for the pantothenate content of CoA (Lipmann et al 1947;Beinert et at. 1953).…”

Section: Coenzyme a Synthesismentioning

confidence: 99%

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The synthesis of coenzyme A by Lactobacillus arabinosus 17–5

Pierpoint

Hughes

1954

Biochemical Journal

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I954 cation of the enzyme with an over-all yield of 20 % was effected.3. A purified preparation of the enzyme attacked all three phosphoproteins studied, but had no appreciable action on glycerophosphate or casein phosphopeptone. The enzyme is hence a true phosphoprotein phosphatase, distinct from the acid phosphomonoesterase.4. Optimum enzyme activity was found at pH 6-0 and at a substrate concentration corresponding to about 10,umoles/ml. of casein phosphorus with 0 001 M thioglycollic acid as activator.5. From the activation and inhibition studies it is deduced that sulphydryl and amino groups are essential for the activity of the enzyme. However the enzyme requires no dialysable coenzyme for its activity.The authors wish to thank the University of Madras for the award of a research studentship to one of us (T. A.S.) and for kind permission to publish the results which form part of a thesis approved for the degree of Master of Science.

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“…7) agreed well with values of 0-65-0-71 jug. pantothenate/Lipmann unit reported for the pantothenate content of CoA (Lipmann et al 1947;Beinert et at. 1953).…”

Section: Coenzyme a Synthesismentioning

confidence: 99%

“…EXPERIMENTAL Material. The acetylating enzymes required for the estimation of coenzyme A according to Handschumacher, Mueller & Strong (1950) and Lipmann, Kaplan, Novelli, Tuttle & Guirard (1947) were obtained from the livers of decapitated pigeons. The 4-aminoazobenzene was a chromatographically pure specimen prepared and given by Dr J.…”

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confidence: 99%

The synthesis of coenzyme A by Lactobacillus arabinosus 17–5

Pierpoint

Hughes

1954

Biochemical Journal

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“…Since coenzyme A (Lipmann et al, 1947(Lipmann et al, , 1950 has been shown to contain LBF-active material after digestion with intestinal phosphatase (Brown et al, 1950), we have applied the bioautograph technique to such digests. A highly purified coenzyme A preparation' containing 400 coenzyme A units per mg was digested (Novelli et al, 1949) with a very concentrated preparation of alkaline intestinal phosphatase.4 Both these preparations were initially free of LBF.…”

Section: Resultsmentioning

confidence: 99%

Bioautographic Studies on the Lactobacillus Bulgaricus Factors

Long

Williams

1951

J Bacteriol

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A strain of Lactobacillus bulgaricus has been shown to require an unidentified growth factor present in a variety of natural materials (Williams et al., 1949).This has been called the L. bulgaricus factor and is conveniently referred to as LBF. LBF has been shown to exist in natural materials in three to five forms all interchangeable for growth of the organism (Rasmussen et al., 1950). Two reports Brown et al., 1950) have indicated that high amounts of calcium pantothenate will replace the unidentified LBF and that at least two forms of LBF contain bound pantothenate. This paper reports experiments extending the paper chromatography studies and presents evidence for the existence of at least seven separate entities in crude materials. The location of pantothenate on paper strips, the activity of certain of the forms of LBF for other organisms, and the chromatographic behavior of concentrates from different sources are also reported. A concentrate of coenzyme A was found to yield three forms of LBF after enzymatic digestion. EXPERIMENTAL METHODSThe general chromatographic procedures are similar to the bioautographic techniques described and used by Eigen (1949, 1950). These techniques are well suited for demonstrating the existence of interchangeable or alternative growth factors. Bacillus megatherium, B-938, culture filtrate was obtained through the kindness of Dr. J. C. Lewis, Western Regional Laboratories, Albany, California. This material contained 380 LBF units per ml by the tube assay method (Williams et al., 1949), and had a potency of 20 units per mg. The purified concentrate from this source had a potency of 4,000 units per mg and was prepared by charcoal adsorption and elution with n-butanol, followed by chromatography on a charcoal column using n-butanol as a developing solvent. LBF produced by Ashbya gossypii, NRRL 1056, was obtained by water extraction of the dried whole culture grown aerobically and contained 525 units per ml. The concentrate prepared from this organism had a potency of 1,500 units per mg and was prepared by a method similar to that used for the concentrate from B. megatherium culture filtrate.From 1.75 to 21 LBF units contained in 0.01 to 0.1 ml were spotted or spread 1 Published with the approval of the directors of the Experiment Station as paper no. 369 of the Journal Series.

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“…The knowledge about CoA has grown significantly since its first description by Fritz Lipmann [137]. It is involved in a large number of biochemical transformations, acting as an acyl-group carrier and a carbonyl-activating factor.…”

Section: Discussionmentioning

confidence: 99%

Coenzyme a Biochemistry: From Neurodevelopment to Neurodegeneration

et al. 2021

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Coenzyme A (CoA) is an essential cofactor in all living organisms. It is involved in a large number of biochemical processes functioning either as an activator of molecules with carbonyl groups or as a carrier of acyl moieties. Together with its thioester derivatives, it plays a central role in cell metabolism, post-translational modification, and gene expression. Furthermore, recent studies revealed a role for CoA in the redox regulation by the S-thiolation of cysteine residues in cellular proteins. The intracellular concentration and distribution in different cellular compartments of CoA and its derivatives are controlled by several extracellular stimuli such as nutrients, hormones, metabolites, and cellular stresses. Perturbations of the biosynthesis and homeostasis of CoA and/or acyl-CoA are connected with several pathological conditions, including cancer, myopathies, and cardiomyopathies. In the most recent years, defects in genes involved in CoA production and distribution have been found in patients affected by rare forms of neurodegenerative and neurodevelopmental disorders. In this review, we will summarize the most relevant aspects of CoA cellular metabolism, their role in the pathogenesis of selected neurodevelopmental and neurodegenerative disorders, and recent advancements in the search for therapeutic approaches for such diseases.

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Coenzyme for Acetylation, a Pantothenic Acid Derivative

Cited by 190 publications

References 0 publications

The synthesis of coenzyme A by Lactobacillus arabinosus 17–5

The synthesis of coenzyme A by Lactobacillus arabinosus 17–5

Bioautographic Studies on the Lactobacillus Bulgaricus Factors

Coenzyme a Biochemistry: From Neurodevelopment to Neurodegeneration

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