Alterations of glucose metabolism in Escherichia coli mutants defective in respiratory-chain enzymes. 2012

Chie Kihira, and Yukari Hayashi, and Naoki Azuma, and Sakiko Noda, and Soya Maeda, and Satoru Fukiya, and Masaru Wada, and Kazunobu Matsushita, and Atsushi Yokota
Laboratory of Microbial Physiology, Research Faculty of Agriculture, Hokkaido University, Kita-9 Nishi-9, Kita-ku, Sapporo, Hokkaido 060-8589, Japan.

The effects of reduced efficiency of proton-motive force (pmf) generation on glucose metabolism were investigated in Escherichia coli respiratory-chain mutants. The respiratory chain of E. coli consists of two NADH dehydrogenases and three terminal oxidases, all with different abilities to generate a pmf. The genes for isozymes with the highest pmf-generating capacity (NADH dehydrogenase-1 and cytochrome bo₃ oxidase) were knocked out singly or in combination, using a wild-type strain as the parent. Analyses of glucose metabolism by jar-fermentation revealed that the glucose consumption rate per cell increased with decreasing efficiency of pmf generation, as determined from the growth parameters of the mutants. The highest rate of glucose metabolism was observed in the double mutant, and the lowest was observed in the wild-type strain. The respiration rates of the single-knockout mutants were comparable to that of the wild-type strain, and that of the double mutant was higher, apparently as a result of the upregulation of the remaining respiratory chain enzymes. All of the strains excreted 2-oxoglutaric acid as a product of glucose metabolism. Additionally, all of the mutants excreted pyruvic acid and/or acetic acid. Interestingly, the double mutant excreted L-glutamic acid. Alterations of the fermentation profiles provide clues regarding the metabolic regulation in each mutant.

UI MeSH Term Description Entries
D007656 Ketoglutaric Acids A family of compounds containing an oxo group with the general structure of 1,5-pentanedioic acid. (From Lehninger, Principles of Biochemistry, 1982, p442) Oxoglutarates,2-Ketoglutarate,2-Ketoglutaric Acid,2-Oxoglutarate,2-Oxoglutaric Acid,Calcium Ketoglutarate,Calcium alpha-Ketoglutarate,Ketoglutaric Acid,Oxogluric Acid,alpha-Ketoglutarate,alpha-Ketoglutaric Acid,alpha-Ketoglutaric Acid, Calcium Salt (2:1),alpha-Ketoglutaric Acid, Diammonium Salt,alpha-Ketoglutaric Acid, Dipotassium Salt,alpha-Ketoglutaric Acid, Disodium Salt,alpha-Ketoglutaric Acid, Monopotassium Salt,alpha-Ketoglutaric Acid, Monosodium Salt,alpha-Ketoglutaric Acid, Potassium Salt,alpha-Ketoglutaric Acid, Sodium Salt,alpha-Oxoglutarate,2 Ketoglutarate,2 Ketoglutaric Acid,2 Oxoglutarate,2 Oxoglutaric Acid,Calcium alpha Ketoglutarate,alpha Ketoglutarate,alpha Ketoglutaric Acid,alpha Ketoglutaric Acid, Diammonium Salt,alpha Ketoglutaric Acid, Dipotassium Salt,alpha Ketoglutaric Acid, Disodium Salt,alpha Ketoglutaric Acid, Monopotassium Salt,alpha Ketoglutaric Acid, Monosodium Salt,alpha Ketoglutaric Acid, Potassium Salt,alpha Ketoglutaric Acid, Sodium Salt,alpha Oxoglutarate,alpha-Ketoglutarate, Calcium
D009154 Mutation Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations. Mutations
D009245 NADH Dehydrogenase A flavoprotein and iron sulfur-containing oxidoreductase that catalyzes the oxidation of NADH to NAD. In eukaryotes the enzyme can be found as a component of mitochondrial electron transport complex I. Under experimental conditions the enzyme can use CYTOCHROME C GROUP as the reducing cofactor. The enzyme was formerly listed as EC 1.6.2.1. NADH Cytochrome c Reductase,Diaphorase (NADH Dehydrogenase),NADH (Acceptor) Oxidoreductase,NADH Cytochrome c Oxidoreductase,Dehydrogenase, NADH
D010088 Oxidoreductases The class of all enzymes catalyzing oxidoreduction reactions. The substrate that is oxidized is regarded as a hydrogen donor. The systematic name is based on donor:acceptor oxidoreductase. The recommended name will be dehydrogenase, wherever this is possible; as an alternative, reductase can be used. Oxidase is only used in cases where O2 is the acceptor. (Enzyme Nomenclature, 1992, p9) Dehydrogenases,Oxidases,Oxidoreductase,Reductases,Dehydrogenase,Oxidase,Reductase
D010101 Oxygen Consumption The rate at which oxygen is used by a tissue; microliters of oxygen STPD used per milligram of tissue per hour; the rate at which oxygen enters the blood from alveolar gas, equal in the steady state to the consumption of oxygen by tissue metabolism throughout the body. (Stedman, 25th ed, p346) Consumption, Oxygen,Consumptions, Oxygen,Oxygen Consumptions
D004579 Electron Transport The process by which ELECTRONS are transported from a reduced substrate to molecular OXYGEN. (From Bennington, Saunders Dictionary and Encyclopedia of Laboratory Medicine and Technology, 1984, p270) Respiratory Chain,Chain, Respiratory,Chains, Respiratory,Respiratory Chains,Transport, Electron
D004926 Escherichia coli A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc. Alkalescens-Dispar Group,Bacillus coli,Bacterium coli,Bacterium coli commune,Diffusely Adherent Escherichia coli,E coli,EAggEC,Enteroaggregative Escherichia coli,Enterococcus coli,Diffusely Adherent E. coli,Enteroaggregative E. coli,Enteroinvasive E. coli,Enteroinvasive Escherichia coli
D005285 Fermentation Anaerobic degradation of GLUCOSE or other organic nutrients to gain energy in the form of ATP. End products vary depending on organisms, substrates, and enzymatic pathways. Common fermentation products include ETHANOL and LACTIC ACID. Fermentations
D005947 Glucose A primary source of energy for living organisms. It is naturally occurring and is found in fruits and other parts of plants in its free state. It is used therapeutically in fluid and nutrient replacement. Dextrose,Anhydrous Dextrose,D-Glucose,Glucose Monohydrate,Glucose, (DL)-Isomer,Glucose, (alpha-D)-Isomer,Glucose, (beta-D)-Isomer,D Glucose,Dextrose, Anhydrous,Monohydrate, Glucose
D018698 Glutamic Acid A non-essential amino acid naturally occurring in the L-form. Glutamic acid is the most common excitatory neurotransmitter in the CENTRAL NERVOUS SYSTEM. Aluminum L-Glutamate,Glutamate,Potassium Glutamate,D-Glutamate,Glutamic Acid, (D)-Isomer,L-Glutamate,L-Glutamic Acid,Aluminum L Glutamate,D Glutamate,Glutamate, Potassium,L Glutamate,L Glutamic Acid,L-Glutamate, Aluminum

Related Publications

Chie Kihira, and Yukari Hayashi, and Naoki Azuma, and Sakiko Noda, and Soya Maeda, and Satoru Fukiya, and Masaru Wada, and Kazunobu Matsushita, and Atsushi Yokota
January 1974, Biochemical and biophysical research communications,
Chie Kihira, and Yukari Hayashi, and Naoki Azuma, and Sakiko Noda, and Soya Maeda, and Satoru Fukiya, and Masaru Wada, and Kazunobu Matsushita, and Atsushi Yokota
June 1975, Proceedings of the National Academy of Sciences of the United States of America,
Chie Kihira, and Yukari Hayashi, and Naoki Azuma, and Sakiko Noda, and Soya Maeda, and Satoru Fukiya, and Masaru Wada, and Kazunobu Matsushita, and Atsushi Yokota
April 1972, The Biochemical journal,
Chie Kihira, and Yukari Hayashi, and Naoki Azuma, and Sakiko Noda, and Soya Maeda, and Satoru Fukiya, and Masaru Wada, and Kazunobu Matsushita, and Atsushi Yokota
September 1975, Molecular & general genetics : MGG,
Chie Kihira, and Yukari Hayashi, and Naoki Azuma, and Sakiko Noda, and Soya Maeda, and Satoru Fukiya, and Masaru Wada, and Kazunobu Matsushita, and Atsushi Yokota
March 1972, The Journal of biological chemistry,
Chie Kihira, and Yukari Hayashi, and Naoki Azuma, and Sakiko Noda, and Soya Maeda, and Satoru Fukiya, and Masaru Wada, and Kazunobu Matsushita, and Atsushi Yokota
June 1981, Journal of bacteriology,
Chie Kihira, and Yukari Hayashi, and Naoki Azuma, and Sakiko Noda, and Soya Maeda, and Satoru Fukiya, and Masaru Wada, and Kazunobu Matsushita, and Atsushi Yokota
January 2014, PloS one,
Chie Kihira, and Yukari Hayashi, and Naoki Azuma, and Sakiko Noda, and Soya Maeda, and Satoru Fukiya, and Masaru Wada, and Kazunobu Matsushita, and Atsushi Yokota
December 1978, Proceedings of the National Academy of Sciences of the United States of America,
Chie Kihira, and Yukari Hayashi, and Naoki Azuma, and Sakiko Noda, and Soya Maeda, and Satoru Fukiya, and Masaru Wada, and Kazunobu Matsushita, and Atsushi Yokota
January 1974, Nucleic acids research,
Chie Kihira, and Yukari Hayashi, and Naoki Azuma, and Sakiko Noda, and Soya Maeda, and Satoru Fukiya, and Masaru Wada, and Kazunobu Matsushita, and Atsushi Yokota
May 1986, Journal of bacteriology,
Copied contents to your clipboard!