Book ChapterDOI
Catabolite Repression and other Control Mechanisms in Carbohydrate Utilization
Kenneth Paigen,Beverly Williams +1 more
TLDR
This chapter focuses on three devices: catabolite repression, transient repression, and catabolites inhibition, which regulate the utilization of many carbohydrates, which influences many aspects of microbial growth and metabolism.Abstract:
Publisher Summary This chapter focuses on three devices: catabolite repression, transient repression, and catabolite inhibition, which regulate the utilization of many carbohydrates. Catabolite repression is a reduction in the rate of synthesis of certain enzymes, particularly those of degradative metabolism, in the presence of glucose or other readily metabolized carbon sources. Catabolite inhibition is a control exerted by glucose on enzyme activity rather than on enzyme formation, analogous to feedback inhibition in biosynthetic pathways. Catabolite repression influences many aspects of microbial growth and metabolism. In addition to the well known repressions of carbohydrate utilization and amino-acid degradation in bacteria and yeast, catabolite repression affects the formation of enzymes that function in the tricarboxylic acid cycle, glyoxylate cycle, fatty acid degradation, carbon dioxide fixation, and the respiratory chain. In higher organisms, catabolite repression has been observed in sugar cane, rats, and man. The question of whether catabolite repression acts to inhibit the transcription of DNA into m-RNA or to inhibit translation of messenger into protein has received conflicting answers. Catabolite repression is a control system that usually affects catabolic enzymes. If catabolite repression and transient repression are not mediated by the specific apo-repressor of each operon, there must be another protein that recognizes the low molecular-weight effector. The significance of a control mechanism, which influences the activity as opposed to the concentration of a carbohydrate-metabolizing enzyme is readily appreciated because bacteria have a limited ability to change enzyme concentrations.read more
Citations
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Journal ArticleDOI
Phosphoenolpyruvate:carbohydrate phosphotransferase systems of bacteria.
TL;DR: The IIAGlc protein, part of the glucose-specific PTS, is a central regulatory protein which in its nonphosphorylated form can bind to and inhibit several non-PTS uptake systems and thus prevent entry of inducers.
Book ChapterDOI
Regulation of glucose metabolism in growing yeast cells
TL;DR: This chapter discusses two distinct groups of yeasts—namely, glucose insensitive and glucose-sensitive yeasts, and indicates that there are possibly differences in internal metabolite concentrations, which may be expressed in the different regulatory responses.
Book ChapterDOI
The utilization of sugars by yeasts.
TL;DR: This chapter outlines the breakdown of sugars by yeasts and is based chiefly on studies yeast such as Saccharomyces cerevisiae, Candida utilis, and Kluyveromyces fragilis.
Journal ArticleDOI
Transcriptional regulation in constraints-based metabolic models of Escherichia coli
TL;DR: The combined metabolic/regulatory model can predict the ability of mutant E. coli strains to grow on defined media as well as time courses of cell growth, substrate uptake, metabolic by-product secretion, and qualitative gene expression under various conditions, as indicated by comparison with experimental data under a variety of environmental conditions.
Journal ArticleDOI
The bacterial phosphoenolpyruvate: Sugar phosphotransferase system
Pieter W. Postma,Saul Roseman +1 more
TL;DR: Isolation of different proteins of the phosphotransferase system and reconstitution of the complex shows that in the net transfer of the phosphate group from phosphoenolpyruvate to a given sugar the phosphoryl group is sequentially transferred from one protein to another.
References
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Journal ArticleDOI
Genetic regulatory mechanisms in the synthesis of proteins.
François Jacob,Jacques Monod +1 more
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Journal ArticleDOI
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Journal ArticleDOI
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Journal ArticleDOI
Influence of inorganic phosphate in the formation of phosphatases by Escherichia coli.
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