PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 23603133-4 2013 The stability of DAAO was improved by adding free flavin adenine dinucleotide and the electrode composition was optimized for the detection of d-alanine. Flavin-Adenine Dinucleotide 50-77 D-amino acid oxidase Homo sapiens 17-21 23219954-7 2013 While these effects for the substitution at position 31 cannot be structurally explained, the R279A mutation might affect the hDAAO FAD-binding affinity by altering the "structurally ambivalent" peptide V47-L51. Flavin-Adenine Dinucleotide 132-135 D-amino acid oxidase Homo sapiens 126-131 23199733-8 2013 Furthermore, the thermal denaturation of DAO and dissociation of flavin adenine dinucleotide (FAD) from the subunits of enzyme were prevented in the aqueous phase formed between the bilayers of OV-DAO. Flavin-Adenine Dinucleotide 65-92 D-amino acid oxidase Homo sapiens 197-200 23199733-8 2013 Furthermore, the thermal denaturation of DAO and dissociation of flavin adenine dinucleotide (FAD) from the subunits of enzyme were prevented in the aqueous phase formed between the bilayers of OV-DAO. Flavin-Adenine Dinucleotide 94-97 D-amino acid oxidase Homo sapiens 197-200 20521334-6 2010 Interestingly, the apoprotein form of hDAAO binds the substrate D-serine: this interaction increases FAD binding thus increasing the amount of active holoenzyme in solution. Flavin-Adenine Dinucleotide 101-104 D-amino acid oxidase Homo sapiens 38-43 21956578-1 2012 D-Amino acid oxidase and D-aspartate oxidase are two well-known FAD-containing flavooxidases that catalyze the same reaction (the oxidative deamination) on different D-amino acids. Flavin-Adenine Dinucleotide 64-67 D-amino acid oxidase Homo sapiens 0-20 17924443-6 2007 In addition, biochemical characterization of human DAO indicates that it binds FAD more weakly than does porcine D-amino acid oxidase (pDAO) and exists as a stable homodimer, even in the apoprotein form. Flavin-Adenine Dinucleotide 79-82 D-amino acid oxidase Homo sapiens 51-54 18220846-1 2007 D-amino acid oxidase (DAAO) is a FAD-containing flavoprotein that dehydrogenates the D-isomer of amino acids to the corresponding imino acids, coupled with the reduction of FAD. Flavin-Adenine Dinucleotide 33-36 D-amino acid oxidase Homo sapiens 0-20 18220846-1 2007 D-amino acid oxidase (DAAO) is a FAD-containing flavoprotein that dehydrogenates the D-isomer of amino acids to the corresponding imino acids, coupled with the reduction of FAD. Flavin-Adenine Dinucleotide 33-36 D-amino acid oxidase Homo sapiens 22-26 17396222-1 2007 D-Amino acid oxidase (DAAO) is a FAD-containing flavoenzyme that catalyzes the oxidative deamination of D-isomers of neutral and polar amino acids. Flavin-Adenine Dinucleotide 33-36 D-amino acid oxidase Homo sapiens 0-20 17396222-1 2007 D-Amino acid oxidase (DAAO) is a FAD-containing flavoenzyme that catalyzes the oxidative deamination of D-isomers of neutral and polar amino acids. Flavin-Adenine Dinucleotide 33-36 D-amino acid oxidase Homo sapiens 22-26 17088322-1 2006 In the brain, the extensively studied FAD-dependent enzyme D-amino acid oxidase (DAO) degrades the gliotransmitter D-serine, a potent activator of N-methyl-D-aspartate type glutamate receptors, and evidence suggests that DAO, together with its activator G72 protein, may play a key role in the pathophysiology of schizophrenia. Flavin-Adenine Dinucleotide 38-41 D-amino acid oxidase Homo sapiens 59-79 17088322-1 2006 In the brain, the extensively studied FAD-dependent enzyme D-amino acid oxidase (DAO) degrades the gliotransmitter D-serine, a potent activator of N-methyl-D-aspartate type glutamate receptors, and evidence suggests that DAO, together with its activator G72 protein, may play a key role in the pathophysiology of schizophrenia. Flavin-Adenine Dinucleotide 38-41 D-amino acid oxidase Homo sapiens 81-84 17088322-1 2006 In the brain, the extensively studied FAD-dependent enzyme D-amino acid oxidase (DAO) degrades the gliotransmitter D-serine, a potent activator of N-methyl-D-aspartate type glutamate receptors, and evidence suggests that DAO, together with its activator G72 protein, may play a key role in the pathophysiology of schizophrenia. Flavin-Adenine Dinucleotide 38-41 D-amino acid oxidase Homo sapiens 221-224 17088322-3 2006 We recently succeeded in purifying human DAO, and found that it weakly binds FAD and shows a significant slower rate of flavin reduction compared with porcine DAO. Flavin-Adenine Dinucleotide 77-80 D-amino acid oxidase Homo sapiens 41-44 11754736-2 2002 According to the three-dimensional structure of a porcine kidney D-amino acid oxidase-substrate (D-leucine) complex model, the G313 backbone carbonyl recognizes the substrate amino group by hydrogen bonding and the side-chain hydroxyl of T317 forms a hydrogen bond with C(2)=O of the flavin moiety of FAD [Miura et al. Flavin-Adenine Dinucleotide 301-304 D-amino acid oxidase Homo sapiens 65-85 12632405-5 2003 Ninety percent of the initial activity of immobilized VHb-DAO could be maintained at up to 50 cycles of the enzymatic reaction without exogenous addition of H(2)O(2) and flavin adenine dinucleotide (FAD). Flavin-Adenine Dinucleotide 170-197 D-amino acid oxidase Homo sapiens 58-61 12632405-5 2003 Ninety percent of the initial activity of immobilized VHb-DAO could be maintained at up to 50 cycles of the enzymatic reaction without exogenous addition of H(2)O(2) and flavin adenine dinucleotide (FAD). Flavin-Adenine Dinucleotide 199-202 D-amino acid oxidase Homo sapiens 58-61 12053066-4 2002 Moreover, CTN was shown to interact with flavin adenine dinucleotide (FAD), a coenzyme of DAO. Flavin-Adenine Dinucleotide 41-68 D-amino acid oxidase Homo sapiens 90-93 12053066-4 2002 Moreover, CTN was shown to interact with flavin adenine dinucleotide (FAD), a coenzyme of DAO. Flavin-Adenine Dinucleotide 70-73 D-amino acid oxidase Homo sapiens 90-93 12053066-5 2002 The UV spectral change of FAD bound to DAO was observed in the visible region by addition of CTN. Flavin-Adenine Dinucleotide 26-29 D-amino acid oxidase Homo sapiens 39-42 9644264-3 1998 The 1,605-cm-1 Raman band of the anionic reduced flavin in the purple intermediate of D-amino acid oxidase (DAO) with D-proline or D-alanine does not shift in DAO reconstituted with [4-carbonyl-18O]FAD, although it shifts with [4,10a-13C2]- or [4a-13C]FAD. Flavin-Adenine Dinucleotide 198-201 D-amino acid oxidase Homo sapiens 86-106 11686926-7 2001 This speculation was supported by the finding that the magnitude of the shift is smaller by 5 cm(-1) (observed at 1,680 cm(-1)) in the case of reduced DAO reconstituted with 7,8-Cl(2)-FAD, whose reduced form has lower electron-donating ability than natural reduced FAD. Flavin-Adenine Dinucleotide 184-187 D-amino acid oxidase Homo sapiens 151-154 9644264-3 1998 The 1,605-cm-1 Raman band of the anionic reduced flavin in the purple intermediate of D-amino acid oxidase (DAO) with D-proline or D-alanine does not shift in DAO reconstituted with [4-carbonyl-18O]FAD, although it shifts with [4,10a-13C2]- or [4a-13C]FAD. Flavin-Adenine Dinucleotide 198-201 D-amino acid oxidase Homo sapiens 108-111 9153426-5 1997 The FAD redox state of DAAO crystals was assessed by single-crystal polarized absorption microspectrophotometry. Flavin-Adenine Dinucleotide 4-7 D-amino acid oxidase Homo sapiens 23-27 6102996-1 1980 Conformational difference surrounding the coenzyme, FAD, of D-amino acid oxidase (D-amino-acid:O2 oxidoreductase (deaminating), EC 1.4.3.3) between its monomeric and dimeric forms were examined by observing fluorescence of FAD. Flavin-Adenine Dinucleotide 52-55 D-amino acid oxidase Homo sapiens 60-80 1975807-8 1990 In the catalysis of DAO, a similar mechanism may be involved, that is, the positive charge of a D-amino acid may interact repulsively with the 3-imino proton of the enzyme bound FAD, and this interaction may be important for the catalysis. Flavin-Adenine Dinucleotide 178-181 D-amino acid oxidase Homo sapiens 20-23 2574999-0 1989 Temperature-induced changes in the coenzyme environment of D-amino acid oxidase revealed by the multiple decays of FAD fluorescence. Flavin-Adenine Dinucleotide 115-118 D-amino acid oxidase Homo sapiens 59-79 2574999-1 1989 A temperature-dependent change in the microenvironment of the coenzyme, FAD, of D-amino acid oxidase was investigated by means of steady-state and picosecond time-resolved fluorescence spectroscopy. Flavin-Adenine Dinucleotide 72-75 D-amino acid oxidase Homo sapiens 80-100 2574999-2 1989 Relative emission quantum yields from FAD bound to D-amino acid oxidase revealed the temperature transition when concentration of the enzyme was lowered. Flavin-Adenine Dinucleotide 38-41 D-amino acid oxidase Homo sapiens 51-71 2897290-1 1988 D-Amino-acid oxidase is a flavoprotein using FAD as cofactor. Flavin-Adenine Dinucleotide 45-48 D-amino acid oxidase Homo sapiens 0-20 2897290-8 1988 The dependence of D-amino-acid oxidase on FAD concentration has been studied. Flavin-Adenine Dinucleotide 42-45 D-amino acid oxidase Homo sapiens 18-38 34995837-1 2022 d-Serine biosensing has been extensively reported based on enzyme sensors using flavin adenine dinucleotide (FAD) -dependent d-amino acid oxidase (DAAOx), based on the monitoring of hydrogen peroxide generated by the enzymatic reaction, which is affected by dissolved oxygen concentration in the measurement environment in in vivo use. Flavin-Adenine Dinucleotide 80-107 D-amino acid oxidase Homo sapiens 147-152 34995837-1 2022 d-Serine biosensing has been extensively reported based on enzyme sensors using flavin adenine dinucleotide (FAD) -dependent d-amino acid oxidase (DAAOx), based on the monitoring of hydrogen peroxide generated by the enzymatic reaction, which is affected by dissolved oxygen concentration in the measurement environment in in vivo use. Flavin-Adenine Dinucleotide 109-112 D-amino acid oxidase Homo sapiens 147-152 2896189-0 1987 13C-NMR studies on the reaction intermediates of porcine kidney D-amino acid oxidase reconstituted with 13C-enriched flavin adenine dinucleotide. Flavin-Adenine Dinucleotide 117-144 D-amino acid oxidase Homo sapiens 64-84 2896189-1 1987 The 13C-NMR spectra of the reaction intermediates of D-amino acid oxidase (DAO) were measured with DAO reconstituted with FAD in which the 2-, 4-, 4a-, and 10a-positions of the isoalloxazine moiety were selectively 13C-enriched. Flavin-Adenine Dinucleotide 122-125 D-amino acid oxidase Homo sapiens 53-73 2896189-1 1987 The 13C-NMR spectra of the reaction intermediates of D-amino acid oxidase (DAO) were measured with DAO reconstituted with FAD in which the 2-, 4-, 4a-, and 10a-positions of the isoalloxazine moiety were selectively 13C-enriched. Flavin-Adenine Dinucleotide 122-125 D-amino acid oxidase Homo sapiens 75-78 2896189-7 1987 Comparison of the 13C-resonances of reduced DAO with those of free reduced FMN in the neutral and anionic forms indicate that FAD in reduced DAO is in the anionic reduced form. Flavin-Adenine Dinucleotide 126-129 D-amino acid oxidase Homo sapiens 44-47 2896189-7 1987 Comparison of the 13C-resonances of reduced DAO with those of free reduced FMN in the neutral and anionic forms indicate that FAD in reduced DAO is in the anionic reduced form. Flavin-Adenine Dinucleotide 126-129 D-amino acid oxidase Homo sapiens 141-144 2896189-9 1987 Comparison of the 13C-resonances for the purple intermediates with those of reduced FMN and reduced DAO indicate unequivocally that FAD in the purple intermediate is in the anionic reduced state. Flavin-Adenine Dinucleotide 132-135 D-amino acid oxidase Homo sapiens 100-103 2885314-0 1987 13C-NMR studies of porcine kidney D-amino acid oxidase reconstituted with 13C-enriched flavin adenine dinucleotide. Flavin-Adenine Dinucleotide 87-114 D-amino acid oxidase Homo sapiens 34-54 2885314-2 1987 D-Amino acid oxidase (DAO) from porcine kidney was reconstituted with FAD"s which were enriched with 13C at the 2-, 4-, 4a-, and 10a-positions of the isoalloxazine moiety, and 13C-NMR spectra of the reconstituted DAO were measured in the absence and presence of various competitive inhibitors. Flavin-Adenine Dinucleotide 70-75 D-amino acid oxidase Homo sapiens 0-20 2885314-2 1987 D-Amino acid oxidase (DAO) from porcine kidney was reconstituted with FAD"s which were enriched with 13C at the 2-, 4-, 4a-, and 10a-positions of the isoalloxazine moiety, and 13C-NMR spectra of the reconstituted DAO were measured in the absence and presence of various competitive inhibitors. Flavin-Adenine Dinucleotide 70-75 D-amino acid oxidase Homo sapiens 22-25 2885314-2 1987 D-Amino acid oxidase (DAO) from porcine kidney was reconstituted with FAD"s which were enriched with 13C at the 2-, 4-, 4a-, and 10a-positions of the isoalloxazine moiety, and 13C-NMR spectra of the reconstituted DAO were measured in the absence and presence of various competitive inhibitors. Flavin-Adenine Dinucleotide 70-75 D-amino acid oxidase Homo sapiens 213-216 6142880-3 1983 RR spectra were also measured for the intermediates of DAO reconstituted with isotopically labeled FAD"s, i.e., [4a-13C]-, [4,10a-13C2]-, [2-13C]-, [5-15N]-, and [1,3-15N2]FAD in D2O. Flavin-Adenine Dinucleotide 99-102 D-amino acid oxidase Homo sapiens 55-58 6102996-1 1980 Conformational difference surrounding the coenzyme, FAD, of D-amino acid oxidase (D-amino-acid:O2 oxidoreductase (deaminating), EC 1.4.3.3) between its monomeric and dimeric forms were examined by observing fluorescence of FAD. Flavin-Adenine Dinucleotide 223-226 D-amino acid oxidase Homo sapiens 60-80 18229-0 1977 Thermodynamics of the binding of flavin adenine dinucleotide to D-amino acid oxidase. Flavin-Adenine Dinucleotide 33-60 D-amino acid oxidase Homo sapiens 64-84 19435-0 1977 Effect of halide anions on the binding of FAD to D-amino acid oxidase and the tryptophanyl fluorescence of the apoenzyme. Flavin-Adenine Dinucleotide 42-45 D-amino acid oxidase Homo sapiens 49-69 16661-2 1977 The holoenzyme of D-amino acid oxidase [D-amino acid: O2 oxidoreductase (deaminating), EC 1.4.3.3] was found to combine with 1-anilinonaphthalene-8-sulfonate without liberation of its coenzyme, FAD. Flavin-Adenine Dinucleotide 194-197 D-amino acid oxidase Homo sapiens 18-38 18229-1 1977 The enthalpy of binding, deltaHb, of flavin adenine dinucleotide to the apoenzyme of D-amino acid oxidase was determined by flow calorimetry at pH 8.5 to be +3.8, -4.1 and -11.0 kcal mol-1 at 10 degrees, 25 degrees and 38 degrees, respectively. Flavin-Adenine Dinucleotide 37-64 D-amino acid oxidase Homo sapiens 85-105 31868610-8 2020 The results showed that (i) flavin adenine dinucleotide (FAD, redox center of DAAO) was a direct electroactive substance that produced a reduction peak current; in the presence of O2, the amount of FAD increased leading to an increase of the reduction peak current. Flavin-Adenine Dinucleotide 28-55 D-amino acid oxidase Homo sapiens 78-82 4379503-0 1965 Coenzyme specificity of D-amino acid oxidase for the flavin moiety of FAD. Flavin-Adenine Dinucleotide 70-73 D-amino acid oxidase Homo sapiens 24-44 31868610-8 2020 The results showed that (i) flavin adenine dinucleotide (FAD, redox center of DAAO) was a direct electroactive substance that produced a reduction peak current; in the presence of O2, the amount of FAD increased leading to an increase of the reduction peak current. Flavin-Adenine Dinucleotide 57-60 D-amino acid oxidase Homo sapiens 78-82 31868610-8 2020 The results showed that (i) flavin adenine dinucleotide (FAD, redox center of DAAO) was a direct electroactive substance that produced a reduction peak current; in the presence of O2, the amount of FAD increased leading to an increase of the reduction peak current. Flavin-Adenine Dinucleotide 198-201 D-amino acid oxidase Homo sapiens 78-82 30206963-7 2018 Furthermore, binding free energy calculations show that DAO mutants have a lower binding affinity toward cofactor flavin adenine dinucleotide and substrate imino-serine than the wild-type. Flavin-Adenine Dinucleotide 114-141 D-amino acid oxidase Homo sapiens 56-59 31799256-0 2019 Substitution of Arginine 120 in Human D-Amino Acid Oxidase Favors FAD-Binding and Nuclear Mistargeting. Flavin-Adenine Dinucleotide 66-69 D-amino acid oxidase Homo sapiens 38-58 30659069-1 2019 d-amino acid oxidase (DAO) is a flavin adenine dinucleotide (FAD)-dependent oxidase metabolizing neutral and polar d-amino acids. Flavin-Adenine Dinucleotide 32-59 D-amino acid oxidase Homo sapiens 0-20 30659069-1 2019 d-amino acid oxidase (DAO) is a flavin adenine dinucleotide (FAD)-dependent oxidase metabolizing neutral and polar d-amino acids. Flavin-Adenine Dinucleotide 32-59 D-amino acid oxidase Homo sapiens 22-25 30659069-1 2019 d-amino acid oxidase (DAO) is a flavin adenine dinucleotide (FAD)-dependent oxidase metabolizing neutral and polar d-amino acids. Flavin-Adenine Dinucleotide 61-64 D-amino acid oxidase Homo sapiens 0-20 30659069-1 2019 d-amino acid oxidase (DAO) is a flavin adenine dinucleotide (FAD)-dependent oxidase metabolizing neutral and polar d-amino acids. Flavin-Adenine Dinucleotide 61-64 D-amino acid oxidase Homo sapiens 22-25 30547037-1 2018 D-Amino acid oxidase (DAAO) is an FAD-containing flavoenzyme that catalyzes with absolute stereoselectivity the oxidative deamination of all natural D-amino acids, the only exception being the acidic ones. Flavin-Adenine Dinucleotide 34-37 D-amino acid oxidase Homo sapiens 0-20 30547037-1 2018 D-Amino acid oxidase (DAAO) is an FAD-containing flavoenzyme that catalyzes with absolute stereoselectivity the oxidative deamination of all natural D-amino acids, the only exception being the acidic ones. Flavin-Adenine Dinucleotide 34-37 D-amino acid oxidase Homo sapiens 22-26 30547037-6 2018 Human DAAO possesses a weak interaction with the FAD cofactor; thus, in vivo it should be largely present in the inactive, apoprotein form. Flavin-Adenine Dinucleotide 49-52 D-amino acid oxidase Homo sapiens 6-10 31799256-6 2019 These results resemble the ones obtained substituting another residue located at the interface region (i.e., the W209R variant), indicating that substitutions at the monomer-monomer interface mainly affects the FAD binding in hDAAO. Flavin-Adenine Dinucleotide 211-214 D-amino acid oxidase Homo sapiens 226-231 30659069-6 2019 Furthermore, addition of d-amino acids and riboflavin, a metabolic precursor of FAD, to the medium potentiated the senescence-promoting effect of DAO. Flavin-Adenine Dinucleotide 80-83 D-amino acid oxidase Homo sapiens 146-149 29114206-11 2017 Our simulation experiments to demonstrate the interaction between DAOA and human DAO (hDAO) showed that hDAO holoenzyme [hDAO with flavine adenine dinucleotide (FAD)] becomes more flexible and misfolded in the presence of DAOA, whereas DAOA had no effect on hDAO apoprotein (hDAO without FAD), which indicate that DAOA inactivates hDAO holoenzyme. Flavin-Adenine Dinucleotide 131-159 D-amino acid oxidase Homo sapiens 66-69 29404340-1 2017 D-amino acid oxidase (DAAO) is a well-known flavoenzyme that catalyzes the oxidative FAD-dependent deamination of D-amino acids. Flavin-Adenine Dinucleotide 85-88 D-amino acid oxidase Homo sapiens 0-20 29404340-1 2017 D-amino acid oxidase (DAAO) is a well-known flavoenzyme that catalyzes the oxidative FAD-dependent deamination of D-amino acids. Flavin-Adenine Dinucleotide 85-88 D-amino acid oxidase Homo sapiens 22-26 29114206-11 2017 Our simulation experiments to demonstrate the interaction between DAOA and human DAO (hDAO) showed that hDAO holoenzyme [hDAO with flavine adenine dinucleotide (FAD)] becomes more flexible and misfolded in the presence of DAOA, whereas DAOA had no effect on hDAO apoprotein (hDAO without FAD), which indicate that DAOA inactivates hDAO holoenzyme. Flavin-Adenine Dinucleotide 161-164 D-amino acid oxidase Homo sapiens 66-69 29114206-11 2017 Our simulation experiments to demonstrate the interaction between DAOA and human DAO (hDAO) showed that hDAO holoenzyme [hDAO with flavine adenine dinucleotide (FAD)] becomes more flexible and misfolded in the presence of DAOA, whereas DAOA had no effect on hDAO apoprotein (hDAO without FAD), which indicate that DAOA inactivates hDAO holoenzyme. Flavin-Adenine Dinucleotide 288-291 D-amino acid oxidase Homo sapiens 66-69 28509930-1 2017 Because of the relevance of d-serine (d-Ser) to schizophrenia, inhibitors of d-amino acid oxidase (DAO), which catalyzes degradation of d-Ser in the presence of flavin adenine dinucleotide (FAD), are expected to be anti-schizophrenia therapeutics. Flavin-Adenine Dinucleotide 161-188 D-amino acid oxidase Homo sapiens 77-97 28509930-1 2017 Because of the relevance of d-serine (d-Ser) to schizophrenia, inhibitors of d-amino acid oxidase (DAO), which catalyzes degradation of d-Ser in the presence of flavin adenine dinucleotide (FAD), are expected to be anti-schizophrenia therapeutics. Flavin-Adenine Dinucleotide 161-188 D-amino acid oxidase Homo sapiens 99-102 28509930-1 2017 Because of the relevance of d-serine (d-Ser) to schizophrenia, inhibitors of d-amino acid oxidase (DAO), which catalyzes degradation of d-Ser in the presence of flavin adenine dinucleotide (FAD), are expected to be anti-schizophrenia therapeutics. Flavin-Adenine Dinucleotide 190-193 D-amino acid oxidase Homo sapiens 77-97 28509930-1 2017 Because of the relevance of d-serine (d-Ser) to schizophrenia, inhibitors of d-amino acid oxidase (DAO), which catalyzes degradation of d-Ser in the presence of flavin adenine dinucleotide (FAD), are expected to be anti-schizophrenia therapeutics. Flavin-Adenine Dinucleotide 190-193 D-amino acid oxidase Homo sapiens 99-102 28509930-3 2017 The results clearly demonstrated that there are two binding pockets: one is shared with d-Ser and FAD, and the other is an unexpected cleft between the subunits of a DAO dimer. Flavin-Adenine Dinucleotide 98-101 D-amino acid oxidase Homo sapiens 166-169