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At least 289 records · Page 16Linked to original sources
PubMed1990

Mandelate pathway of Pseudomonas putida: sequence relationships involving mandelate racemase, (S)-mandelate dehydrogenase, and benzoylformate decarboxylase and expression of benzoylformate decarboxylase in Escherichia coli.

The genes that encode the five known enzymes of the mandelate pathway of Pseudomonas putida (ATCC 12633), mandelate racemase (mdlA), (S)-mandelate dehydrogenase (mdlB), benzoylformate decarboxylase (mdlC), NAD(+)-dependent benzaldehyde dehydrogenase (mdlD), and NADP(+)-dependent benzaldehyde dehydrogenase (mdlE), have been cloned. The genes for (S)-mandelate dehydrogenase and benzoylformate decarboxylase have been sequenced; these genes and that for mandelate racemase [Ransom, S. C., Gerlt, J. A., Powers, V. M., & Kenyon, G. L. (1988) Biochemistry 27, 540] are organized in an operon (mdlCBA). Mandelate racemase has regions of sequence similarity to muconate lactonizing enzymes I and II from P. putida. (S)-Mandelate dehydrogenase is predicted to be 393 amino acids in length and to have a molecular weight of 43,352; it has regions of sequence similarity to glycolate oxidase from spinach and ferricytochrome b2 lactate dehydrogenase from yeast. Benzoylformate decarboxylase is predicted to be 499 amino acids in length and to have a molecular weight of 53,621; it has regions of sequence similarity to enzymes that decarboxylate pyruvate with thiamin pyrophosphate as cofactor. These observations support the hypothesis that the mandelate pathway evolved by recruitment of enzymes from preexisting metabolic pathways. The gene for benzoylformate decarboxylase has been expressed in Escherichia coli with the trc promoter, and homogeneous enzyme has been isolated from induced cells.

Acetolactate Synthase↗
PubMed1995

[Adult Leigh syndrome. A rare differential diagnosis of central respiratory insufficiency].

Subacute necrotizing encephalomyelopathy (Leigh's syndrome) is a rare neurodegenerative disease in the adult. The precise metabolic defect is unknown, but abnormalities of a mitochondrial enzyme system related to cytochrome-c oxidase or pyruvate dehydrogenase are described. The clinical picture usually consists of an altered breathing pattern, oculomotor paralysis, other signs of cranial nerve dysfunction, ataxia, myoclonic jerks, nystagmus, generalized seizures, optic atrophy and demyelinating peripheral neuropathy. Hypopnea leads to CO2-retention with consecutive loss of consciousness demanding mechanical ventilation. Respiratory failure is the most frequent cause of death. Here we describe two patients with adult onset Leigh's syndrome and we discuss the longterm treatment strategies including vitamin B1 and CPAP mask.

Adult↗
PubMed1950

Regulatory mechanisms of cellular respiration. III. Enzyme distribution in the cell. Its influence on the metabolism of pyruvic acid by bakers' yeast.

The rate of the aerobic metabolism of pyruvic acid by bakers' yeast cells is determined mainly by the amount of undissociated acid present. As a consequence, the greatest rate of oxidation was observed at pH 2.8. Oxidation, at a slow rate, started at pH 1.08; at pH 9.4 there was no oxidation at all. The anaerobic metabolism, only a fraction of the aerobic, was observed only in acid solutions. There was none at pH values higher than 3. Pyruvic acid in the presence of oxygen was oxidized directly to acetic acid; in the absence of oxygen it was metabolized mainly by dismutation to lactic and acetic acids, and CO(2). Acetic acid formation was demonstrated on oxidation of pyruvic acid at pH 1.91, and on addition of fluoroacetic acid. Succinic acid formation was shown by addition of malonic acid. These metabolic pathways in a cell so rich in carboxylase may be explained by the arrangement of enzymes within the cell, so that carboxylase is at the center, while pyruvic acid oxidase is located at the periphery. Succinic and citric acids were oxidized only in acid solutions up to pH 4. Malic and alpha-ketoglutaric acids were not oxidized, undoubtedly because of lack of penetration.

Cell Respiration↗
PubMed1974

Subcellular distribution and properties of kynurenine transaminase in rat liver.

Kynurenine transaminase activity in rat liver was found in both the mitochondrial and supernatant fractions. The mitochondrial and supernatant fractions contained (a) kynurenine-pyruvate transaminase, which showed a preference for pyruvate as amino acceptor and a pH optimum between 8.0 and 8.5, and (b) kynurenine-alpha-oxoglutarate transaminase, with a preference for alpha-oxoglutarate and a pH optimum between 6.0 and 6.5. Possible roles of these enzymes in tryptophan metabolism in the liver are discussed.

Alcohol Oxidoreductases↗
PubMed1991

Sudden infant death syndrome (SIDS) and disordered blood flow.

Naeye (1) has long linked SIDS with low utero-placental blood flow and foetal hypoxia. Gestational hypotension, maternal smoking and disorders of the foetal membranes are considered by Naeye to promote brainstem and neurological abnormalities. Naeye also found that SIDS' victims often showed a growth lag after birth and suggested a reduced oxygen environment after birth which pointed to chronic under-ventilation of the lungs. Another abnormality observed by Naeye was that brown fat was retained for an abnormally long time. Now Mitchell (New Zealand Herald, 27.11.90) has concluded a 3-year study of SIDS' victims in New Zealand and found a combination of stomach sleeping position, mothers' smoking and bottle feeding was implicated in 79% of SIDS' victims. (The sleeping position and maternal smoking may be additive in disordered blood flow). The effect of circulatory shock (cardiogenic) on skeletal muscle mitochondrial activity shows there is a large decrease in the activity of the mitochondrial enzyme cytochrome oxidase during circulatory shock. There is also a reduced capacity to oxidase succinate, pyruvate and palmitoyl carnitine (2). These authors discuss cellular oxidative damage due to severe hypoxia during circulatory shock and the effect on the skeletal muscle mitochondrial electron transport chain (ETC). The reasons for carnitine supplement to these patients are explained. It was concluded that during the course of circulatory shock in humans inactivation or damage to the mitochondrial ETC plays a crucial role in cellular oxidative damage. The activation of brown fat mitochondria via the ETC revolves around elevated blood flow, and the high content of cytochromes which give this tissue its characteristic brownish colour (3]. Other forms of interrupted blood flow, similar to cardiogenic shock disorders in skeletal muscle, will be discussed.

Adipose Tissue, Brown↗
PubMed1999

Interplay of organic and biological chemistry in understanding coenzyme mechanisms: example of thiamin diphosphate-dependent decarboxylations of 2-oxo acids.

With the publication of the three-dimensional structures of several thiamin diphosphate-dependent enzymes, the chemical mechanism of their non-oxidative and oxidative decarboxylation reactions is better understood. Chemical models for these reactions serve a useful purpose to help evaluate the additional catalytic rate acceleration provided by the protein component. The ability to generate, and spectroscopically observe, the two key zwitterionic intermediates invoked in such reactions allowed progress to be made in elucidating the rates and mechanisms of the elementary steps leading to and from these intermediates. The need remains to develop chemical models, which accurately reflect the enzyme-bound conformation of this coenzyme.

Acetoin Dehydrogenase↗
PubMed2003

Development of an electrochemical immunosensor for alanine aminotransferase.

Alanine aminotransferase (ALT) has been regarded as one of the most sensitive indicators of hepatocellular damage. While ALT is widely used in the practice of medicine, few attempts have been made to develop biosensors applicable to the on-site diagnosis of liver diseases. In the hope of developing an immunosensor for measurement of ALT activity, we have generated monoclonal antibodies to human recombinant ALT and fabricated them for use in a sensor. The ALT immunosensor was composed of the followings: (1) anti-ALT antibody-immobilized outer membrane; (2) pyruvate oxidase-absorbed inner membrane; (3) a self assembled monolayer mediator-coated gold working electrode and an Ag/AgCl reference electrode. The chronoamperometric measurement of the immunosensor was performed with 40 microl of PBS containing substrates and ALT without a washing step in less than 5 min. The dynamic range of ALT immunosensor was presented as five orders of magnitude, ranging between 10 pg/ml and 1 microg/ml. The detection limit and the sensitivity were 10 pg/ml and 26.3 nA/(ng/ml), respectively. In the meantime, the enzyme sensor fabricated without anti-ALT antibody showed much poorer analytical values. The dynamic range, the detection limit, and the sensitivity were 10 ng/ml-100 microg/ml, 10 ng/ml and 11.4 nA/(ng/ml), respectively. The presented results indicated that the immunosensor system provided much better technical performance in all of the aspects evaluated than did the enzyme sensor without the immobilized-antibody.

Adsorption↗
PubMed1998

The phosphate sensor.

The field of phosphate sensors is reviewed. Sensors in the form of potentiometric ion-selective electrodes, amperometric and potentiometric enzyme electrodes, amperometric plant-tissue electrodes and other devices in the form of integrated probes used for determining orthophosphate concentrations in aqueous solutions, are described. Information provided includes conditions like pH and temperature at which the device is operated, as well as experimental results in the form of linear ranges, detection limits and interfering substances. The time period covered ranges from 1986 up to mid-1997. Earlier work is included in some cases.

Alkaline Phosphatase↗
PubMedDate not supplied

Characterization of the acetate-producing pathways in Escherichia coli.

Although the bacterium E. coli is chosen as the host in many bioprocesses, the accumulation of a common byproduct, acetate, is often problematic. Acetate, when present at high levels, will inhibit both cell growth and recombinant protein productivity. In addition, products derived from the central aerobic metabolic pathway often compete with the acetate-producing pathways poxB and ackA-pta for glucose as the substrate. As such, a significant portion of the glucose may be excreted as acetate, wasting substrate that otherwise could have been used for the desired product. We have created mutant E. coli strains with a deletion of either the poxB or the ackA-pta pathway. These two strains, along with the wild-type strain, have been studied in batch reactors over a 12 h time period, at pH 7.0 and 6.0. The wild-type strain has also been studied using glucose as the carbon source. Data were collected to correlate cellular growth, extracellular metabolite production, enzyme activity, and gene expression. Results show that the ackA-pta pathway dominates in exponential phase, and the poxB pathway dominates in stationary phase. The ackA-pta pathway is repressed in acidic environments, whereas the poxB pathway is activated.

Acetate Kinase↗