Tryptophan distribution in yeast hexokinase isoenzyme B

Kramp, Douglas C.; Feldman, Isaac

doi:10.1016/0005-2795(78)90525-1

Cited by 12 publications

(2 citation statements)

References 16 publications

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“…3 Structure of the hexokinase from Saccharomyces cerevisiae residue) and one trp residue is buried in the protein matrix. The maximal quenching induced by glucose was about 25% and the concentration of glucose at half-maximal quenching was 0.4 mM for the monomeric form and 3.4 mM for the dimeric one (Feldman and Norton 1980;Kramp and Feldman 1978).…”

Section: Thermostable Glucose Dehydrogenase From Thermoplasma Acidophmentioning

confidence: 99%

Thermostable Proteins as Probe for the Design of Advanced Fluorescence Biosensors

Champdoré

Staiano

Aurilia

et al. 2006

Rev Environ Sci Biotechnol

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In this review we explore the advantages deriving from the use of either enzymes or sugar binding proteins isolated from thermophilic organisms to develop stable fluorescence biosensors. We report on a novel approach to address the consumption of the analyte by enzyme-based biosensors, namely the utilization of apo-enzymes as non-active forms of proteins which are still able to bind the ligand but cannot transform it into product. We also report recent studies in which the fluorescence labeling of a naturally thermostable binding protein allows a quantitative determination of glucose. Abbreviations IAANS 2-(4¢-(iodoacetamido)anilino)naphthalene-6-sulfonic acid (IAANS) ANS 1-(anilino)-naphtalene-8-sulfonate FRET fluorescence resonance energy transfer LED light emitting diode GD glucose dehydrogenase BSGK glucokinase from Bacillus stearothermophilus Ph-SBP sugar-binding protein from Pyrococcus horikoshii M. de Champdoré AE M. Staiano AE V. Aurilia AE

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Section: Thermostable Glucose Dehydrogenase From Thermoplasma Acidophmentioning

confidence: 99%

Thermostable Proteins as Probe for the Design of Advanced Fluorescence Biosensors

Champdoré

Staiano

Aurilia

et al. 2006

Rev Environ Sci Biotechnol

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“…This enzyme possesses four tryptophan residues that can be classified as two surface residues, one glucose-quenchable residue in the cleft and one buried. The maximal quenching induced by glucose was about 25% and the concentration of glucose at half-maximal quenching was 0.4 mM for the monomeric form and 3.4 mM for the dimeric one (50,51).…”

Section: Structure and Mechanism Of Glucose Binding Of Hexokinasementioning

confidence: 99%

A Novel Fluorescence Competitive Assay for Glucose Determinations by Using a Thermostable Glucokinase from the Thermophilic Microorganism Bacillus stearothermophilus

D’Auria

DiCesare

Staiano

et al. 2002

Analytical Biochemistry

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We describe the use of a thermostable glucokinase in a novel competitive fluorescence assay for glucose. Glucokinase from Bacillus stearothermophilus (BSGK) was found to retain enzymatic activity in solution for over 20 days. The single cysteine residue in BSGK, which is near the active site, was labeled with a fluorescent probe, 2-(4-iodoacetamidoanilino)naphthalene-6-sulfonic acid. The ANS-labeled BSGK displayed a modest 25% decrease in the emission intensity upon binding glucose but no change in lifetime. To obtain a larger spectral change we developed a competitive assay for glucose using the intrinsic tryptophan fluorescence from BSGK and a resonance energy transfer (RET) acceptor-labeled sugar. The sugar-labeled acceptor quenched the BSGK tryptophan emission, and the quenching was reversed upon addition of glucose. The use of RET as the sensing mechanism can be easily extended to longer wavelengths for a more practical glucose sensor.

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Thermostable proteins as probe for the design of advanced fluorescence biosensors

Champdoré¹,

Staiano²,

Aurilia³

et al. 2006

Life in Extreme Environments

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Tryptophan distribution in yeast hexokinase isoenzyme B

Cited by 12 publications

References 16 publications

Thermostable Proteins as Probe for the Design of Advanced Fluorescence Biosensors

Thermostable Proteins as Probe for the Design of Advanced Fluorescence Biosensors

A Novel Fluorescence Competitive Assay for Glucose Determinations by Using a Thermostable Glucokinase from the Thermophilic Microorganism Bacillus stearothermophilus

Thermostable proteins as probe for the design of advanced fluorescence biosensors

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