Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: KEGG:D02011 (FAD)
5,530 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We have cloned a 1620-nucleotide gene encoding the catalytic subunit (alpha subunit) of a thermostable glucose dehydrogenase (GDH) from Burkholderia cepacia. The FAD binding motif was found in the N-terminal region of the alpha subunit. The deduced primary structure of the alpha subunit showed about 48% identity to the catalytic subunits of sorbitol dehydrogenase (SDH) from Gluconobacter oxydans and 2-keto-D-gluconate dehydrogenases (2KGDH) from Erwinia herbicola and Pantoea citrea. The alpha subunit of B. cepacia was expressed in Escherichia coli in its active water-soluble form, showing maximum dye-mediated GDH activity at 70 degrees C, retaining high thermal stability. A putative open reading frame (ORF) of 507 nucleotides was also found upstream of the alpha subunit encoding an 18-kDa peptide, designated as gamma subunit. The deduced primary structure of gamma subunit showed about 30% identity to the small subunits of the SDH from G. oxydans and 2KGDHs from E. herbicola and P. citrea.
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PMID:Cloning and expression of the gene encoding catalytic subunit of thermostable glucose dehydrogenase from Burkholderia cepacia in Escherichia coli. 1257 42

The comparative kinetic study of two glucose oxidizing enzymes, FAD-dependent glucose oxidase and PQQ-dependent glucose dehydrogenase, is presented in the artificial electron transfer mediator system based on ruthenium(III) compounds. It is demonstrated that FAD-dependent glucose oxidase and PQQ-dependent glucose dehydrogenase follow Michaelis kinetics in the D-glucose/ruthenium(III) system. PQQ-dependent glucose dehydrogenase is more active than FAD-dependent glucose oxidase in the process of D-glucose oxidation by ruthenium(III) compounds, this being due to the different catalytic mechanisms of these enzymes.
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PMID:Comparative kinetic study of D-glucose oxidation by ruthenium(III) compounds catalyzed by FAD-dependent glucose oxidase and PQQ-dependent glucose dehydrogenase. 1276 23

Cotesia congregata and Manduca sexta were used as a model system to study the mechanism and effect of a polydnavirus (PDV). We hypothesized that (1) FAD-glucose dehydrogenase (GLD) (EC 1.1.99.10) hemolymph titer would increase in response to parasitism, (2) hemocyte targeting behavior would be altered by parasitism, and (3) changes observed in GLD activity and hemocyte behavior immediately post-parasitization would be due to the presence of PDV. GLD specific activity was measured at four time points early during parasitism using a spectrophotometric enzyme assay. Hemocyte behavior was measured using direct observations of hemocyte response to a foreign target in vitro. Results demonstrate that GLD increases immediately post-oviposition and post-injection of purified PDV, indicating that virions elicit nonself recognition. This increase relative to unparasitized controls also occurs in response to trioxsalen-UV inactivated virus, indicating that the initial disruption of the host immune response is not dependent upon viral transcription. Further, we demonstrate that plasmatocytes are actively spreading and aggregating but are not targeting nonself material in both parasitized and polydnavirus treatments. These results indicate that purified PDV is recognized as nonself and is triggering an immediate cellular immune response prior to viral transcription.
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PMID:Alteration in FAD-glucose dehydrogenase activity and hemocyte behavior contribute to initial disruption of Manduca sexta immune response to Cotesia congregata parasitoids. 1277 Feb 64

In this article we show the recent progress in the field of glucose sensing based on the utilization of enzymes and proteins as probes for stable and non-consuming fluorescence biosensors. We developed a new methodology for glucose sensing using inactive forms of enzymes such as the glucose oxidase from Aspergillus niger, the glucose dehydrogenase from the thermophilic microorganism Thermoplasma acidophilum, and the glucokinase from the thermophilic eubacterium Bacillus stearothermophilus. Glucose oxidase was rendered inactive by removal of the FAD cofactor. The resulting apo-glucose oxidase still binds glucose as observed from a decrease in its intrinsic tryptophan fluorescence. 8-Anilino-1-naphthalene sulfonic acid was found to bind spontaneously to apo-glucose oxidase as seen from an enhancement of the ANS fluorescence. The steady state intensity of the bound ANS decreased 25% upon binding of glucose, and the mean lifetime of the bound ANS decreased about 40%. These spectral changes occurred with a midpoint from 10 to 20 mM glucose, which is comparable to the KD of holo-glucose oxidase. The ANS-labeled apo-glucose dehydrogenase from Thermoplasma acidophilum also displayed an approximate 25% decrease in emission intensity upon binding glucose. This decrease can be also used to measure the glucose concentration. The thermophilic apo-glucose dehydrogenase was also stable in the presence of organic solvents, allowing determination of glucose in the presence of acetone. The third enzyme used for glucose sensing was the glucokinase from Bacillus stearothermophilus. A fluorescence competitive assay for the determination of glucose was developed based on the utilization of this thermostable enzyme. Taken together, our results show that enzymes which use glucose as their substrate can be used as reversible and non-consuming glucose biosensors in the absence of required co-factors. Moreover, the possibility of using inactive apo-enzymes for a reversible sensor greatly expands the range of proteins which can be used as sensors, not only for glucose, but for a wide variety of biochemically relevant analytes.
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PMID:Protein-based biosensors for diabetic patients. 1561 57

About twenty years ago, the cofactor pyrroloquinoline quinone, PQQ, was discovered. Here the author gives his personal view on the reasons why this cofactor was so lately discovered and how the steps in its identification were made. The discovery not only led to subsequent studies on the physiological significance of PQQ but also initiated investigations on other enzymes where the presence of PQQ was expected, resulting in the discovery of three other quinone cofactors, TPQ, TTQ, and LTQ, which differ from PQQ as they are part of the protein chain of the enzyme to which they belong. Enzymes using quinone cofactors, the so-called quinoproteins, copper-quinoproteins, and quinohemoproteins, are mainly involved in the direct oxidation of alcohols, sugars, and amines. Some of the PQQ-containing ones participate in incomplete bacterial oxidation processes like the conversion of ethanol into vinegar and of D-glucose into (5-keto)gluconic acid. Soluble glucose dehydrogenase is the sensor in diagnostic test strips used for glucose determination in blood samples of diabetic patients. Quinohemoprotein alcohol dehydrogenases have an enantiospecificity suited for the kinetic resolution of racemic alcohols to their enantiomerically pure form, certain enantiomers being interesting candidates as building block for synthesis of high-value-added chemicals. Making up for balance after twenty years of quinoprotein research, the following conclusions can be drawn: since quinoproteins do not catalyze unique reactions, we know now that there are more enzymes which catalyze one and the same reaction than we did before, but do not understand the reason for this (compare e.g. NAD/NADP-dependent glucose dehydrogenases, flavoprotein glucose oxidase/dehydrogenase, and soluble/membrane-bound, PQQ-containing glucose dehydrogenases, enzymes all catalyzing the oxidation of beta-D-glucose to delta-gluconolactone but being quite different from each other); however, taking a pragmatic point of view, the foregoing can also be regarded as a positive development since as illustrated by the examples given above, the enlargement of the catalytic arsenal with quinoprotein enzymes provides in more possibilities for enzyme applications; the hopes that PQQ could be a new vitamin have diminished strongly after it has become clear that its occurrence is restricted to bacteria; the impact factor is broader than just the development of the field of quinoproteins, since together with that of enzymes containing a one-electron oxidized amino acid residue as cofactor, it has emphasized that cofactors not only derive from nucleotides (e.g. FAD, NAD) but also from amino acids. Finally, strong indications exist to assume that this is not the end of the story since other quinone cofactors seem awaiting their discovery.
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PMID:The PQQ story. 1623 4

The thermostable glucose dehydrogenase (GDH) from Burkholderia cepacia sp. SM4 is composed of a catalytic subunit (alpha), an electron transfer subunit (beta), and a small gamma subunit of unknown function. We cloned a 1428-nucleotide gene encoding the beta subunit located immediately downstream of the alpha subunit. This completes the isolation of the genes encoding the three components of the GDH complex, which are clustered very close together with the same transcription polarity in the order gammaalphabeta. The deduced beta subunit amino acid sequence contains three typical heme-binding motifs and was 44-49% identical to the cytochrome c subunits of other FAD-dependent dehydrogenase complexes. The GDHgammaalphabeta complex of B. cepacia was successfully expressed in a fully active form in Escherichia coli by co-expression with cytochrome c maturation genes. Recombinant expression of the GDH complex was also found to restore glucose-dependent respiration in a GDH mutant of E. coli.
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PMID:Cloning and functional expression of glucose dehydrogenase complex of Burkholderia cepacia in Escherichia coli. 1633

A novel FAD-dependent glucose dehydrogenase (FAD-GDH) was found and its enzymatic property for glucose sensing was characterized. FAD-GDH oxidized glucose in the presence of some artificial electron acceptors, except for O2, and exhibited thermostability, high substrate specificity and a large Michaelis constant for glucose. FAD-GDH was applied to an amperometric glucose sensor with Fe(CN)6(3-) as a soluble mediator. The use of a relatively high concentration of Fe(CN)6(3-) resulted in a good linearity between the current response and the glucose concentration, taking into account a large Michaelis constant for Fe(CN)6(3-). The glucose sensor was completely insensitive to O2 and responded linearly to glucose up to 30 mM. Compared to glucose, the response to other saccharides was negligible. The sensor can be stored at room temperature in a desiccator for at least one month without any change in the response or activity.
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PMID:Novel FAD-dependent glucose dehydrogenase for a dioxygen-insensitive glucose biosensor. 1655 81

This paper describes the construction and characterization of a batch-type coulometric system for the detection of D-glucose using a novel FAD-dependent glucose dehydrogenase. In order to overcome the problem of interferents, such as ascorbate and urate, a potential-step method was proposed to separate the electrolysis reactions of interferents and D-glucose by selecting a mediator possessing an appropriate formal potential. The rapid oxidative consumption of the interferents proceeded in the first step, whereas the mediator and glucose remained reduced. In the second step, the mediator was immediately oxidized, and subsequent bioelectrocatalytic oxidation of D-glucose occurred with the aid of aldose 1-epimerase. In this study, potassium octacyanomolybdate (IV) with a formal potential of 0.6 V vs. Ag|AgCl was chosen as a mediator, and the first and second electrolysis potentials were set at 0.4 V and 0.8 V, respectively, by considering the heterogeneous electron-transfer kinetics and the potential window. The background-corrected response in charge corresponded to 99+/-2 % efficiency in terms of the amount of D-glucose.
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PMID:Potential-step coulometry of D-glucose using a novel FAD-dependent glucose dehydrogenase. 1693 93

In this paper we present a novel wireless glucose biosensing system employing direct electron transfer principle based enzyme fuel cell. Using the glucose dehydrogenase complex, which is composed of a catalytic subunit containing FAD, the cytochrome c subunit that harbors heme c as the electron transfer subunit, and chaperone-like subunit, a direct electron transfer-type glucose enzyme fuel cell was constructed. The enzyme glucose fuel cell generated electric power, and the open-circuit voltage showed glucose concentration dependence, which suggests potential applications for this glucose-sensing system. We constructed a miniaturized "all-in-one" glucose enzyme fuel cell, which represents a compartmentless fuel that is based on the direct electron transfer principle. This involved the combination of a wireless transmitter system and a simple and miniaturized continuous glucose monitoring system, which operated continuously for about 3 days with stable response. This is the first demonstration of an enzyme-based direct electron transfer-type enzyme fuel cell and fuel cell-type glucose sensor which can be utilized as a subcutaneously implantable system for continuous glucose monitoring.
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PMID:A novel wireless glucose sensor employing direct electron transfer principle based enzyme fuel cell. 1716 11

Conversion of glucose to pyruvate via reactions homologous to the non-phosphorylated Entner-Doudoroff (non-P ED) pathway could be achieved in the presence of two amino acid catalysts, cysteine and histidine: cystine oxidizes glucose to gluconic acid by the reaction homologous to glucose dehydrogenase and histidine changes gluconic acid to 2-keto-3-deoxy gluconic acid, then to pyruvate by the reaction homologous to gluconic acid dehydratase and 2-keto-3-deoxy gluconate aldolase, respectively. Pyruvate can be converted to acetyl CoA by the reaction with CoA, TPP and FAD in the presence of cysteine and histidine, which resembles pyruvate dehydrogenase reaction. It was found that gluconic acid dehydration alone is non-specific, in contrast to other reactions. The non-P ED pathway is used by some extreme thermophiles in bacteria and archaea, usually thought as the oldest among the contemporary organisms. This study suggests the possible contribution of amino acid to the origin of the glycolytic pathway.
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PMID:Prebiotic origin of glycolytic metabolism: histidine and cysteine can produce acetyl CoA from glucose via reactions homologous to non-phosphorylated Entner-Doudoroff pathway. 1851 57


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