PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 27770422-3 2017 Ferrocene-modified linear poly(ethylenimine) (Fc-LPEI) redox polymers have been designed to simultaneously immobilize glucose oxidase (GOx) at an electrode and mediate electron transfer from their flavin adenine dinucleotide (FAD) active site to the electrode surface. Flavin-Adenine Dinucleotide 197-224 hydroxyacid oxidase 1 Homo sapiens 135-138 28106225-3 2017 According to the measurements of the current density peak of the flavin adenine dinucleotide (FAD) redox reaction, electron transfer rate, Michaelis-Menten constants and sensitivity, CNT/PEI/(GOx-Cat) shows the best values, and this is attributed to the excellent catalytic activity of GOx and the H2O2 decomposition capability of the catalase. Flavin-Adenine Dinucleotide 94-97 hydroxyacid oxidase 1 Homo sapiens 286-289 27770422-3 2017 Ferrocene-modified linear poly(ethylenimine) (Fc-LPEI) redox polymers have been designed to simultaneously immobilize glucose oxidase (GOx) at an electrode and mediate electron transfer from their flavin adenine dinucleotide (FAD) active site to the electrode surface. Flavin-Adenine Dinucleotide 226-229 hydroxyacid oxidase 1 Homo sapiens 135-138 22641400-5 2012 The interaction of GOx with GO could induce the exposure of the FAD (flavin adenine dinucleotide) moiety to solvent and transfer tryptophan (Trp) residues to a more hydrophobic environment. Flavin-Adenine Dinucleotide 64-67 hydroxyacid oxidase 1 Homo sapiens 19-22 28192293-3 2016 The second section discusses how the properties of FAD fluorescence changes in flavoenzymes (FvEs), again considering the different chemical and structural forms; the glucose oxidase (GOx) and the choline oxidase (ChOx) cases will be commented. Flavin-Adenine Dinucleotide 51-54 hydroxyacid oxidase 1 Homo sapiens 167-182 28192293-3 2016 The second section discusses how the properties of FAD fluorescence changes in flavoenzymes (FvEs), again considering the different chemical and structural forms; the glucose oxidase (GOx) and the choline oxidase (ChOx) cases will be commented. Flavin-Adenine Dinucleotide 51-54 hydroxyacid oxidase 1 Homo sapiens 184-187 27518716-1 2016 Glucose oxidase (GOx) possessing a Raman-active chromophore (flavin adenine dinucleotide) is used as a signal reporter for constructing a highly specific "turn off" surface-enhanced Raman scattering (SERS) sensor for glucose. Flavin-Adenine Dinucleotide 61-88 hydroxyacid oxidase 1 Homo sapiens 0-15 27518716-1 2016 Glucose oxidase (GOx) possessing a Raman-active chromophore (flavin adenine dinucleotide) is used as a signal reporter for constructing a highly specific "turn off" surface-enhanced Raman scattering (SERS) sensor for glucose. Flavin-Adenine Dinucleotide 61-88 hydroxyacid oxidase 1 Homo sapiens 17-20 25890695-1 2015 Flavin adenine dinucleotide-dependent glucose dehydrogenase (FAD-GDH) is emerging as an oxygen-insensitive alternative to glucose oxidase (GOx) as the biocatalyst for bioelectrodes and bioanodes in glucose sensing and glucose enzymatic fuel cells (EFCs). Flavin-Adenine Dinucleotide 0-27 hydroxyacid oxidase 1 Homo sapiens 122-137 25890695-1 2015 Flavin adenine dinucleotide-dependent glucose dehydrogenase (FAD-GDH) is emerging as an oxygen-insensitive alternative to glucose oxidase (GOx) as the biocatalyst for bioelectrodes and bioanodes in glucose sensing and glucose enzymatic fuel cells (EFCs). Flavin-Adenine Dinucleotide 0-27 hydroxyacid oxidase 1 Homo sapiens 139-142 22975425-1 2012 The reconstitution of apo-glucose oxidase (apo-GOx) on single-walled carbon nanotubes (SWNTs) functionalized with the cofactor, flavin adenine dinucleotide (FAD), greatly improved electron transfer turnover rate of the redox reactions in glucose sensing with glucose sensors. Flavin-Adenine Dinucleotide 128-155 hydroxyacid oxidase 1 Homo sapiens 47-50 22975425-1 2012 The reconstitution of apo-glucose oxidase (apo-GOx) on single-walled carbon nanotubes (SWNTs) functionalized with the cofactor, flavin adenine dinucleotide (FAD), greatly improved electron transfer turnover rate of the redox reactions in glucose sensing with glucose sensors. Flavin-Adenine Dinucleotide 157-160 hydroxyacid oxidase 1 Homo sapiens 47-50 22641400-5 2012 The interaction of GOx with GO could induce the exposure of the FAD (flavin adenine dinucleotide) moiety to solvent and transfer tryptophan (Trp) residues to a more hydrophobic environment. Flavin-Adenine Dinucleotide 69-96 hydroxyacid oxidase 1 Homo sapiens 19-22 21146394-5 2011 The PPMH/GC-electrode showed superior DET to/from flavine adenine dinucleotide cofactor of GOx, while some redox-compounds including ferrocene and K(3)[Fe(CN)(6)] were completely electrochemically inactive on the PPMH/GC-electrode. Flavin-Adenine Dinucleotide 50-78 hydroxyacid oxidase 1 Homo sapiens 91-94 22415204-4 2012 The interaction of GOx with the chemical denaturant resulted in a disturbance of the structure of the flavin prosthetic group (FAD moiety) that induced the moiety to become less exposed to solvent than that in the native protein molecule. Flavin-Adenine Dinucleotide 127-130 hydroxyacid oxidase 1 Homo sapiens 19-22 22415204-6 2012 MD simulations and DFT calculations revealed that Gdm(+) ions could enter the active pocket of the GOx molecule and interact with the FAD group, leading to a significant alteration in the structural characteristics and hydrogen bond networks formed between FAD and the surrounding amino acid residues. Flavin-Adenine Dinucleotide 134-137 hydroxyacid oxidase 1 Homo sapiens 99-102 22415204-6 2012 MD simulations and DFT calculations revealed that Gdm(+) ions could enter the active pocket of the GOx molecule and interact with the FAD group, leading to a significant alteration in the structural characteristics and hydrogen bond networks formed between FAD and the surrounding amino acid residues. Flavin-Adenine Dinucleotide 257-260 hydroxyacid oxidase 1 Homo sapiens 99-102 22027303-8 2011 CONCLUSION: Glucose dehydrogenase flavin adenine dinucleotide compares favorably with GOx in many sensor-relevant attributes and may enable measurement of glucose concentrations both higher and lower than those measurable by GOx. Flavin-Adenine Dinucleotide 34-61 hydroxyacid oxidase 1 Homo sapiens 225-228 20843096-7 2010 Molecular dynamics (MD) simulations and density functional theory (DFT) calculations revealed that thermal treatment could significantly alter the electronic characteristics and the intramolecular electron transfer ability of FAD (flavin adenine dinucleotide), and hydrogen bond networks formed between FAD and the amino acid residues around the cofactor, leading to the change of the secondary structure and the catalytic activity of GOx. Flavin-Adenine Dinucleotide 226-229 hydroxyacid oxidase 1 Homo sapiens 435-438 20843096-7 2010 Molecular dynamics (MD) simulations and density functional theory (DFT) calculations revealed that thermal treatment could significantly alter the electronic characteristics and the intramolecular electron transfer ability of FAD (flavin adenine dinucleotide), and hydrogen bond networks formed between FAD and the amino acid residues around the cofactor, leading to the change of the secondary structure and the catalytic activity of GOx. Flavin-Adenine Dinucleotide 303-306 hydroxyacid oxidase 1 Homo sapiens 435-438 15174885-1 2004 The enzyme glucose oxidase (GOx) is reconstituted on a flavin adenin dinucleotide (FAD, 1) cofactor-functionalized Au-nanoparticle (Au-NP), 1.4 nm, and the GOx/Au-NP hybrid is linked to a bulk Au-electrode by a short dithiol, 1,4-benzenedithiol (2), or a long dithiol, 1,9-nonanedithiol (3), monolayer. Flavin-Adenine Dinucleotide 55-81 hydroxyacid oxidase 1 Homo sapiens 11-26 27873995-2 2008 Since Flavin Adenine Dinucleotide (FAD), a coenzyme of glucose oxidase (GOx), is the active center of the catalytic site, conformation of which could determine the activity of enzyme, it is important to understand the dynamic mechanism of its conformational mobility while GOx is adsorbed on SWCNTs with multiple orientations. Flavin-Adenine Dinucleotide 6-33 hydroxyacid oxidase 1 Homo sapiens 273-276 27873995-2 2008 Since Flavin Adenine Dinucleotide (FAD), a coenzyme of glucose oxidase (GOx), is the active center of the catalytic site, conformation of which could determine the activity of enzyme, it is important to understand the dynamic mechanism of its conformational mobility while GOx is adsorbed on SWCNTs with multiple orientations. Flavin-Adenine Dinucleotide 35-38 hydroxyacid oxidase 1 Homo sapiens 55-70 27873995-2 2008 Since Flavin Adenine Dinucleotide (FAD), a coenzyme of glucose oxidase (GOx), is the active center of the catalytic site, conformation of which could determine the activity of enzyme, it is important to understand the dynamic mechanism of its conformational mobility while GOx is adsorbed on SWCNTs with multiple orientations. Flavin-Adenine Dinucleotide 35-38 hydroxyacid oxidase 1 Homo sapiens 72-75 27873995-2 2008 Since Flavin Adenine Dinucleotide (FAD), a coenzyme of glucose oxidase (GOx), is the active center of the catalytic site, conformation of which could determine the activity of enzyme, it is important to understand the dynamic mechanism of its conformational mobility while GOx is adsorbed on SWCNTs with multiple orientations. Flavin-Adenine Dinucleotide 35-38 hydroxyacid oxidase 1 Homo sapiens 273-276 16750941-3 2007 The enzymes, glucose oxidase, GOx, and glucose dehydrogenase, GDH, are electrically contacted with the electrodes by the reconstitution of the corresponding apo-proteins on flavin adenine dinucleotide (FAD) or pyrroloquinoline quinone (PQQ)-functionalized Au-NPs (1.4 nm) associated with electrodes, respectively. Flavin-Adenine Dinucleotide 173-200 hydroxyacid oxidase 1 Homo sapiens 30-33 16750941-3 2007 The enzymes, glucose oxidase, GOx, and glucose dehydrogenase, GDH, are electrically contacted with the electrodes by the reconstitution of the corresponding apo-proteins on flavin adenine dinucleotide (FAD) or pyrroloquinoline quinone (PQQ)-functionalized Au-NPs (1.4 nm) associated with electrodes, respectively. Flavin-Adenine Dinucleotide 202-205 hydroxyacid oxidase 1 Homo sapiens 30-33 15174885-1 2004 The enzyme glucose oxidase (GOx) is reconstituted on a flavin adenin dinucleotide (FAD, 1) cofactor-functionalized Au-nanoparticle (Au-NP), 1.4 nm, and the GOx/Au-NP hybrid is linked to a bulk Au-electrode by a short dithiol, 1,4-benzenedithiol (2), or a long dithiol, 1,9-nonanedithiol (3), monolayer. Flavin-Adenine Dinucleotide 83-86 hydroxyacid oxidase 1 Homo sapiens 11-26 15174885-1 2004 The enzyme glucose oxidase (GOx) is reconstituted on a flavin adenin dinucleotide (FAD, 1) cofactor-functionalized Au-nanoparticle (Au-NP), 1.4 nm, and the GOx/Au-NP hybrid is linked to a bulk Au-electrode by a short dithiol, 1,4-benzenedithiol (2), or a long dithiol, 1,9-nonanedithiol (3), monolayer. Flavin-Adenine Dinucleotide 83-86 hydroxyacid oxidase 1 Homo sapiens 28-31 15174885-1 2004 The enzyme glucose oxidase (GOx) is reconstituted on a flavin adenin dinucleotide (FAD, 1) cofactor-functionalized Au-nanoparticle (Au-NP), 1.4 nm, and the GOx/Au-NP hybrid is linked to a bulk Au-electrode by a short dithiol, 1,4-benzenedithiol (2), or a long dithiol, 1,9-nonanedithiol (3), monolayer. Flavin-Adenine Dinucleotide 83-86 hydroxyacid oxidase 1 Homo sapiens 156-159 19964045-2 2009 Since Flavin Adenine Dinucleotide (FAD) along with other amino residues, including His559, Glu412 and His516, constitute the active center of the catalytic site conformation of which could determine the activity of enzyme, it is important to understand the molecular mechanism of their mobility and the potential impact on the catalytic activity while GOx is immobilized on SWCNTs. Flavin-Adenine Dinucleotide 6-33 hydroxyacid oxidase 1 Homo sapiens 352-355 19964045-2 2009 Since Flavin Adenine Dinucleotide (FAD) along with other amino residues, including His559, Glu412 and His516, constitute the active center of the catalytic site conformation of which could determine the activity of enzyme, it is important to understand the molecular mechanism of their mobility and the potential impact on the catalytic activity while GOx is immobilized on SWCNTs. Flavin-Adenine Dinucleotide 35-38 hydroxyacid oxidase 1 Homo sapiens 352-355 27873995-2 2008 Since Flavin Adenine Dinucleotide (FAD), a coenzyme of glucose oxidase (GOx), is the active center of the catalytic site, conformation of which could determine the activity of enzyme, it is important to understand the dynamic mechanism of its conformational mobility while GOx is adsorbed on SWCNTs with multiple orientations. Flavin-Adenine Dinucleotide 6-33 hydroxyacid oxidase 1 Homo sapiens 55-70 27873995-2 2008 Since Flavin Adenine Dinucleotide (FAD), a coenzyme of glucose oxidase (GOx), is the active center of the catalytic site, conformation of which could determine the activity of enzyme, it is important to understand the dynamic mechanism of its conformational mobility while GOx is adsorbed on SWCNTs with multiple orientations. Flavin-Adenine Dinucleotide 6-33 hydroxyacid oxidase 1 Homo sapiens 72-75 15174885-1 2004 The enzyme glucose oxidase (GOx) is reconstituted on a flavin adenin dinucleotide (FAD, 1) cofactor-functionalized Au-nanoparticle (Au-NP), 1.4 nm, and the GOx/Au-NP hybrid is linked to a bulk Au-electrode by a short dithiol, 1,4-benzenedithiol (2), or a long dithiol, 1,9-nonanedithiol (3), monolayer. Flavin-Adenine Dinucleotide 55-81 hydroxyacid oxidase 1 Homo sapiens 28-31 10093498-1 1999 We report on the steady-state and time-resolved fluorescence from the redox active site flavine adenine dinucleotides (FADs) that are bound to glucose oxidase (GOx) when this enzyme is dissolved in aqueous solution or sequestered within a sol-gel-derived glass. Flavin-Adenine Dinucleotide 88-117 hydroxyacid oxidase 1 Homo sapiens 143-158 10585957-2 1999 Resonant SSHG experiments were achieved by probing the pi-pi* transition of the flavin adenine dinucleotide (FAD) chromophores embedded in the GOx protein. Flavin-Adenine Dinucleotide 80-107 hydroxyacid oxidase 1 Homo sapiens 143-146 10585957-2 1999 Resonant SSHG experiments were achieved by probing the pi-pi* transition of the flavin adenine dinucleotide (FAD) chromophores embedded in the GOx protein. Flavin-Adenine Dinucleotide 109-112 hydroxyacid oxidase 1 Homo sapiens 143-146 10093498-1 1999 We report on the steady-state and time-resolved fluorescence from the redox active site flavine adenine dinucleotides (FADs) that are bound to glucose oxidase (GOx) when this enzyme is dissolved in aqueous solution or sequestered within a sol-gel-derived glass. Flavin-Adenine Dinucleotide 88-117 hydroxyacid oxidase 1 Homo sapiens 160-163 10093498-1 1999 We report on the steady-state and time-resolved fluorescence from the redox active site flavine adenine dinucleotides (FADs) that are bound to glucose oxidase (GOx) when this enzyme is dissolved in aqueous solution or sequestered within a sol-gel-derived glass. Flavin-Adenine Dinucleotide 119-123 hydroxyacid oxidase 1 Homo sapiens 143-158 10093498-1 1999 We report on the steady-state and time-resolved fluorescence from the redox active site flavine adenine dinucleotides (FADs) that are bound to glucose oxidase (GOx) when this enzyme is dissolved in aqueous solution or sequestered within a sol-gel-derived glass. Flavin-Adenine Dinucleotide 119-123 hydroxyacid oxidase 1 Homo sapiens 160-163 10093498-4 1999 The intramolecular exciplex formation event (i.e., excited-state FAD residue folding/unfolding) is completely arrested for the GOx-bound FAD if the enzyme is sequestered within a glass in the absence of glucose. Flavin-Adenine Dinucleotide 65-68 hydroxyacid oxidase 1 Homo sapiens 127-130 10093498-4 1999 The intramolecular exciplex formation event (i.e., excited-state FAD residue folding/unfolding) is completely arrested for the GOx-bound FAD if the enzyme is sequestered within a glass in the absence of glucose. Flavin-Adenine Dinucleotide 137-140 hydroxyacid oxidase 1 Homo sapiens 127-130 10093498-8 1999 Finally, we present preliminary analytical results for film-based sol-gel-derived biosensors that contain GOx, L-amino acid oxidase or cholesterol oxidase wherein the intrinsic FAD fluorescence produces the analytical signal. Flavin-Adenine Dinucleotide 177-180 hydroxyacid oxidase 1 Homo sapiens 106-109 34443722-5 2021 In addition to the well-known electroactivity of free flavin adenine dinucleotide (FAD), the cofactor of GOx, at the expected half-wave potential of -0.490 V vs. Ag/AgCl (1 M KCl), a new well-defined redox pair at 0.155 V is observed and shown to be related to LIG/GOx interaction. Flavin-Adenine Dinucleotide 54-81 hydroxyacid oxidase 1 Homo sapiens 105-108 9606155-8 1998 FAD, a cofactor for a number of oxidase enzymes, then converts inactive apo-GOx to holo-GOx, the activity of which is monitored by the chemiluminescent endpoint and facilitates detection of ALP over the range 10(-15) to 4.1 x 10(-19) mol. Flavin-Adenine Dinucleotide 0-3 hydroxyacid oxidase 1 Homo sapiens 76-79 9606155-8 1998 FAD, a cofactor for a number of oxidase enzymes, then converts inactive apo-GOx to holo-GOx, the activity of which is monitored by the chemiluminescent endpoint and facilitates detection of ALP over the range 10(-15) to 4.1 x 10(-19) mol. Flavin-Adenine Dinucleotide 0-3 hydroxyacid oxidase 1 Homo sapiens 88-91 8797376-7 1996 Two kinds of redox-modified "electrically wired" GOx are applied: GOx modified by N-(ferrocenylmethyl)caproic acid, Fc-GOx, and a novel electrobiocatalyst generated by reconstitution of apo-GOx with a ferrocene-modified FAD semisynthetic cofactor. Flavin-Adenine Dinucleotide 220-223 hydroxyacid oxidase 1 Homo sapiens 49-52 34443722-5 2021 In addition to the well-known electroactivity of free flavin adenine dinucleotide (FAD), the cofactor of GOx, at the expected half-wave potential of -0.490 V vs. Ag/AgCl (1 M KCl), a new well-defined redox pair at 0.155 V is observed and shown to be related to LIG/GOx interaction. Flavin-Adenine Dinucleotide 54-81 hydroxyacid oxidase 1 Homo sapiens 265-268 34443722-5 2021 In addition to the well-known electroactivity of free flavin adenine dinucleotide (FAD), the cofactor of GOx, at the expected half-wave potential of -0.490 V vs. Ag/AgCl (1 M KCl), a new well-defined redox pair at 0.155 V is observed and shown to be related to LIG/GOx interaction. Flavin-Adenine Dinucleotide 83-86 hydroxyacid oxidase 1 Homo sapiens 105-108 34443722-5 2021 In addition to the well-known electroactivity of free flavin adenine dinucleotide (FAD), the cofactor of GOx, at the expected half-wave potential of -0.490 V vs. Ag/AgCl (1 M KCl), a new well-defined redox pair at 0.155 V is observed and shown to be related to LIG/GOx interaction. Flavin-Adenine Dinucleotide 83-86 hydroxyacid oxidase 1 Homo sapiens 265-268 34443722-7 2021 Two protons and two electrons are involved in this reaction, which is shown to be sensitive to the concentration of glucose, restraining its origin to the electron transfer from FAD in the active site of GOx to the electrode via direct or mediated by quinone derivatives acting as mediators. Flavin-Adenine Dinucleotide 178-181 hydroxyacid oxidase 1 Homo sapiens 204-207 32629055-3 2020 In this research fluorescence properties of GOx in different acidic media have been estimated by the evaluation of redox states of active center that is flavine adenine dinucleotide (FAD). Flavin-Adenine Dinucleotide 153-181 hydroxyacid oxidase 1 Homo sapiens 44-47 32629055-3 2020 In this research fluorescence properties of GOx in different acidic media have been estimated by the evaluation of redox states of active center that is flavine adenine dinucleotide (FAD). Flavin-Adenine Dinucleotide 183-186 hydroxyacid oxidase 1 Homo sapiens 44-47 33257186-3 2021 Herein, glucose oxidase (GOx) was chosen as a model enzyme, and according to the chemical structure of GOx cofactor (flavin adenine dinucleotide, FAD), we customize a biomimetic cofactor containing vinyl group (SFAD) for GOx, and prepared an GOx nanocapsule via in-situ polymerization. Flavin-Adenine Dinucleotide 117-144 hydroxyacid oxidase 1 Homo sapiens 8-23 33257186-3 2021 Herein, glucose oxidase (GOx) was chosen as a model enzyme, and according to the chemical structure of GOx cofactor (flavin adenine dinucleotide, FAD), we customize a biomimetic cofactor containing vinyl group (SFAD) for GOx, and prepared an GOx nanocapsule via in-situ polymerization. Flavin-Adenine Dinucleotide 117-144 hydroxyacid oxidase 1 Homo sapiens 25-28 33257186-3 2021 Herein, glucose oxidase (GOx) was chosen as a model enzyme, and according to the chemical structure of GOx cofactor (flavin adenine dinucleotide, FAD), we customize a biomimetic cofactor containing vinyl group (SFAD) for GOx, and prepared an GOx nanocapsule via in-situ polymerization. Flavin-Adenine Dinucleotide 117-144 hydroxyacid oxidase 1 Homo sapiens 103-106 33257186-3 2021 Herein, glucose oxidase (GOx) was chosen as a model enzyme, and according to the chemical structure of GOx cofactor (flavin adenine dinucleotide, FAD), we customize a biomimetic cofactor containing vinyl group (SFAD) for GOx, and prepared an GOx nanocapsule via in-situ polymerization. Flavin-Adenine Dinucleotide 117-144 hydroxyacid oxidase 1 Homo sapiens 103-106 33257186-3 2021 Herein, glucose oxidase (GOx) was chosen as a model enzyme, and according to the chemical structure of GOx cofactor (flavin adenine dinucleotide, FAD), we customize a biomimetic cofactor containing vinyl group (SFAD) for GOx, and prepared an GOx nanocapsule via in-situ polymerization. Flavin-Adenine Dinucleotide 117-144 hydroxyacid oxidase 1 Homo sapiens 103-106 33257186-3 2021 Herein, glucose oxidase (GOx) was chosen as a model enzyme, and according to the chemical structure of GOx cofactor (flavin adenine dinucleotide, FAD), we customize a biomimetic cofactor containing vinyl group (SFAD) for GOx, and prepared an GOx nanocapsule via in-situ polymerization. Flavin-Adenine Dinucleotide 146-149 hydroxyacid oxidase 1 Homo sapiens 8-23 33257186-3 2021 Herein, glucose oxidase (GOx) was chosen as a model enzyme, and according to the chemical structure of GOx cofactor (flavin adenine dinucleotide, FAD), we customize a biomimetic cofactor containing vinyl group (SFAD) for GOx, and prepared an GOx nanocapsule via in-situ polymerization. Flavin-Adenine Dinucleotide 146-149 hydroxyacid oxidase 1 Homo sapiens 25-28 33257186-3 2021 Herein, glucose oxidase (GOx) was chosen as a model enzyme, and according to the chemical structure of GOx cofactor (flavin adenine dinucleotide, FAD), we customize a biomimetic cofactor containing vinyl group (SFAD) for GOx, and prepared an GOx nanocapsule via in-situ polymerization. Flavin-Adenine Dinucleotide 146-149 hydroxyacid oxidase 1 Homo sapiens 103-106 33257186-3 2021 Herein, glucose oxidase (GOx) was chosen as a model enzyme, and according to the chemical structure of GOx cofactor (flavin adenine dinucleotide, FAD), we customize a biomimetic cofactor containing vinyl group (SFAD) for GOx, and prepared an GOx nanocapsule via in-situ polymerization. Flavin-Adenine Dinucleotide 146-149 hydroxyacid oxidase 1 Homo sapiens 103-106 33257186-3 2021 Herein, glucose oxidase (GOx) was chosen as a model enzyme, and according to the chemical structure of GOx cofactor (flavin adenine dinucleotide, FAD), we customize a biomimetic cofactor containing vinyl group (SFAD) for GOx, and prepared an GOx nanocapsule via in-situ polymerization. Flavin-Adenine Dinucleotide 146-149 hydroxyacid oxidase 1 Homo sapiens 103-106