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Journal ArticleDOI

Purification and properties of Escherichia coli coenzyme A-transferase.

TLDR
The E. coli CoA-transferase is partially inactivated by acyl-CoA substrates in the absence of carboxylic acid substrates, presumably as the result of a metal-catalyzed acylation of the ϵ-amino group of a lysine residue near the active site.
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This article is published in Archives of Biochemistry and Biophysics.The article was published on 1975-11-01. It has received 95 citations till now. The article focuses on the topics: Active site & Enzyme assay.

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Citations
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Journal ArticleDOI

Thiolase from Clostridium acetobutylicum ATCC 824 and Its Role in the Synthesis of Acids and Solvents.

TL;DR: Studies of thiolase specific activity under various types of continuous fermentations show that regulation of this enzyme at both the genetic and enzyme levels is important.
Journal ArticleDOI

Genetic and molecular characterization of the genes involved in short-chain fatty acid degradation in Escherichia coli: the ato system.

L S Jenkins, +1 more
TL;DR: The structural organization and regulation of the genes involved in short-chain fatty acid degradation in Escherichia coli, referred to as the ato system, have been studied by a combination of classic genetic and recombinant DNA techniques and suggest that two loci, atoD and atoA, are required for the expression of functional AA-CoA transferase.
Journal ArticleDOI

Coenzyme A transferase from Clostridium acetobutylicum ATCC 824 and its role in the uptake of acids.

TL;DR: The acetate and butyrate conversion reactions in vitro were inhibited by physiological levels of acetone and butanol, and this may be another factor in the in vivo regulation of enzyme activity.
Journal ArticleDOI

Glutaconate CoA‐Transferase from Acidaminococcus fermentans

TL;DR: Experiments with an antiserum against the enzyme indicate that the transferase is necessary for the decarboxylation of glutaconate but not for the dehydration of (R)-2-hydroxyglutarate.
Patent

Production of isoprenoids

TL;DR: In this article, a method for robust production of isoprenoids via one or more biosynthetic pathways is presented, which also provides nucleic acids, enzymes, expression vectors, and genetically modified host cells for carrying out the subject methods.
References
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Journal Article

Protein Measurement with the Folin Phenol Reagent

TL;DR: Procedures are described for measuring protein in solution or after precipitation with acids or other agents, and for the determination of as little as 0.2 gamma of protein.
Journal ArticleDOI

The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis

TL;DR: The results show that the polyacrylamide gel electrophoresis method can be used with great confidence to determine the molecular weights of polypeptide chains for a wide variety of proteins.
Journal ArticleDOI

A Method for Determining the Sedimentation Behavior of Enzymes: Application to Protein Mixtures

TL;DR: Sucrose gradient centrifugation is found to be a suitable method for determining sedimentation coefficients of enzymes in protein mixtures and the sedimentation behavior of several of the enzymes in the pathway of histidine biosynthesis in S. typhimurium has been determined.
Journal ArticleDOI

Estimation of the molecular weights of proteins by Sephadex gel-filtration.

P Andrews
- 01 May 1964 - 
TL;DR: The results are similar to those of previous studies, where the objective was to establish a cause-and-effect relationship, rather than a straightforward relationship between the number of cells and the content of the molecule.
Journal ArticleDOI

Determination of molecular weights and frictional ratios of proteins in impure systems by use of gel filtration and density gradient centrifugation. Application to crude preparations of sulfite and hydroxylamine reductases

TL;DR: With a Stokes radius measured by the chromatographic method and a sedimentation coefficient determined by density gradient centrifugation, reasonable estimates for both the molecular weight and the frictional ratio (f/f0) of a macromolecule are available.
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