Enzymes used for the determination of HbA1C

Hirokawa, Kozo; Nakamura, Kazuo; Kajiyama, Naoki

doi:10.1016/j.femsle.2004.04.027

Cited by 5 publications

(3 citation statements)

References 20 publications

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“…For this purpose, the fpox gene from E . terrenum has been cloned and expressed in an Escherichia coli host and determined its activity in different studies 4,7,8 . An engineered FPOX was applied by Shahbazmohammadi et al 7 as a diagnostic enzyme for diabetes mellitus.…”

Section: Introductionmentioning

confidence: 99%

“…7 For this purpose, the fpox gene from E. terrenum has been cloned and expressed in an Escherichia coli host and determined its activity in different studies. 4,7,8 An engineered FPOX was applied by Shahbazmohammadi et al 7 as a diagnostic enzyme for diabetes mellitus. But, unglycated amino acids, glucosone, and hydrogen peroxide can be produced by FPOX from different fructosyl amino acids, which causes to attain a less precise diagnosis.…”

Section: Introductionmentioning

confidence: 99%

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In silico characterization of fructosyl peptide oxidase properties from Eupenicillium terrenum

Rahmatabadi¹,

Mobini

Askari³

et al. 2022

J of Molecular Recognition

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Fructosyl peptide oxidase (FPOX) enzyme from Eupenicillium terrenum has a high potential to be applied as a diagnostic enzyme. The aim of the present study is the characterization of FPOX from E. terrenum using different bioinformatics tools. The computational prediction of the RNA and protein secondary structures of FPOX, solubility profile in Escherichia coli, stability, domains, and functional properties were performed. In the FPOX protein, six motifs were detected. The d‐amino acid oxidase motif was found as the most important motif that is a FAD‐dependent oxidoreductase. The cysteines including 97, 154, 234, 280, and 360 showed a lower score than −10 that have a low possibility for participitation in the formation of the SS bond. The 56.52% of FPOX amino acids are nonpolar. Random coils are dominant in the FPOX sequence, followed by alpha‐helix and extended strand. The fpox gene is capable of generating a stable RNA secondary structure (−423.90 kcal/mol) in E. coli. FPOX has a large number of hydrophobic amino acids. FPOX showed a low solubility in E. coli which has several aggregation‐prone sites in its 3‐D structure. According to the scores, the best mutation candidate for increasing solubility was the conversion of methionine 302 to arginine. The melting temperature of FPOX based on its amino acid sequence was 55°C to 65°C. The amounts of thermodynamic parameters for the FPOX enzyme were −137.4 kcal/mol, −3.59 kcal/(mol K), and −6.8 kcal/mol for standard folding enthalpy, heat capacity, and folding free energy, respectively. In conclusion, the in silico study of proteins can provide a valuable method for better understanding the protein properties and functions for use in our purposes.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

In silico characterization of fructosyl peptide oxidase properties from Eupenicillium terrenum

Rahmatabadi¹,

Mobini

Askari³

et al. 2022

J of Molecular Recognition

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“…Fructosyl‐amino acid oxidase (FAOD) catalyzes the oxidative deglycation of the glycated amino acid to produce the corresponding amino acid, glucosone, and H 2 O 2 . The FAODs have been detected in various microorganisms [1–7] and several have been used for enzymatic assay for glycated proteins which are good indices of diabetic mellitus [8–10]. The FAODs can be divided into four groups based on the substrate specificities as follows: (i) the enzymes that show high activities for α‐glycated amino acids.…”

Section: Introductionmentioning

confidence: 99%

Fructosyl-amino acid oxidases ofAspergillus oryzaeare induced by the reaction product, glucosone

Yoshida¹,

Akazawa²,

Kuwahara³

et al. 2005

FEMS Microbiology Letters

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Aspergillus oryzae has two fructosyl-amino acid oxidase (FAOD) isozymes (AoFao1 and AoFao2), which are different in the substrate specificities. Northern blot analysis showed both FAO genes were induced by autoclave-browned medium containing l-lysine or l-valine. Studies with a mutant, that had a disrupted AoFAO2 gene, revealed that the expression of AoFAO1 by fructosyl l-valine depended on the expression of AoFAO2. Both genes were also induced by one of the FAOD-reaction products, glucosone. In contrast, other alpha-dicarbonyl compounds, which display a similar structure to that of glucosone were not able to induce the genes expression. These results imply that glucosone may contribute to the expression of FAO genes.

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Advancing the Development of Glycated Protein Biosensing Technology

Kameya

Sakaguchi-Mikami

Ferri

et al. 2015

J Diabetes Sci Technol

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Research advances in biochemical molecules have led to the development of convenient and reproducible biosensing molecules for glycated proteins, such as those based on the enzymes fructosyl amino acid oxidase (FAOX) or fructosyl peptide oxidase (FPOX). Recently, more attractive biosensing molecules with potential applications in next-generation biosensing of glycated proteins have been aggressively reported. We review 2 such molecules, fructosamine 6-kinase (FN6K) and fructosyl amino acid-binding protein, as well as their recent applications in the development of glycated protein biosensing systems. Research on FN6K and fructosyl amino acid-binding protein has been opening up new possibilities for the development of highly sensitive and proteolytic-digestion-free biosensing systems for glycated proteins.

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Enzymes used for the determination of HbA1C

Cited by 5 publications

References 20 publications

In silico characterization of fructosyl peptide oxidase properties from Eupenicillium terrenum

In silico characterization of fructosyl peptide oxidase properties from Eupenicillium terrenum

Fructosyl-amino acid oxidases ofAspergillus oryzaeare induced by the reaction product, glucosone

Advancing the Development of Glycated Protein Biosensing Technology

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