PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 31407761-2 2019 DAAO catalyses hydride transfer from the substrate to the flavin in the reductive half-reaction, and the flavin is reoxidized by O2 in the oxidative half-reaction. Oxygen 129-131 D-amino acid oxidase Homo sapiens 0-4 35510396-0 2022 Monitoring and control of the release of soluble O2 from H2 O2 inside porous enzyme carrier for O2 supply to an immobilized D-amino acid oxidase. Oxygen 49-51 D-amino acid oxidase Homo sapiens 124-144 35510396-0 2022 Monitoring and control of the release of soluble O2 from H2 O2 inside porous enzyme carrier for O2 supply to an immobilized D-amino acid oxidase. Oxygen 96-98 D-amino acid oxidase Homo sapiens 124-144 35510396-5 2022 The internally released O2 is used to drive the reaction of D-amino acid oxidase (oxidation of D-methionine) that is co-immobilized with the catalase in the same carrier. Oxygen 24-26 D-amino acid oxidase Homo sapiens 60-80 2874262-5 1986 A monooxygenase-like enzymatic activity of D-amino acid oxidase with these novel substrates is considered, for which the final products are hypothesized to be protein alpha-carbon hydroxyls resulting from the incorporation of one atom of oxygen into the substrate, the other being reduced to water. Oxygen 6-12 D-amino acid oxidase Homo sapiens 43-63 33540681-6 2021 Besides, we compared the effect induced by CLytA-DAAO with the direct addition of hydrogen peroxide, demonstrating that the progressive generation of reactive oxygen species by CLytA-DAAO is more effective in inducing cytotoxicity than the direct addition of H2O2. Oxygen 159-165 D-amino acid oxidase Homo sapiens 49-53 33540681-6 2021 Besides, we compared the effect induced by CLytA-DAAO with the direct addition of hydrogen peroxide, demonstrating that the progressive generation of reactive oxygen species by CLytA-DAAO is more effective in inducing cytotoxicity than the direct addition of H2O2. Oxygen 159-165 D-amino acid oxidase Homo sapiens 183-187 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. Oxygen 268-274 D-amino acid oxidase Homo sapiens 147-152 32028649-1 2020 D-amino acid oxidase (DAAO) catalyzes the oxidation of D-amino acids generating hydrogen peroxide, a potential producer of reactive oxygen species. Oxygen 132-138 D-amino acid oxidase Homo sapiens 0-20 32028649-1 2020 D-amino acid oxidase (DAAO) catalyzes the oxidation of D-amino acids generating hydrogen peroxide, a potential producer of reactive oxygen species. Oxygen 132-138 D-amino acid oxidase Homo sapiens 22-26 30959013-6 2019 In addition, inverse correlations also existed in the reconstructed group between distensibility of the DAo and the exercise variables such as peak oxygen pulse (R = 0.56, p = 0.02), peak oxygen consumption (R = 0.63, p = 0.008), oxygen consumption at ventilatory anaerobic threshold (R = 0.48, p = 0.04), and peak work (R = 0.54, p = 0.02). Oxygen 148-154 D-amino acid oxidase Homo sapiens 104-107 30959013-6 2019 In addition, inverse correlations also existed in the reconstructed group between distensibility of the DAo and the exercise variables such as peak oxygen pulse (R = 0.56, p = 0.02), peak oxygen consumption (R = 0.63, p = 0.008), oxygen consumption at ventilatory anaerobic threshold (R = 0.48, p = 0.04), and peak work (R = 0.54, p = 0.02). Oxygen 188-194 D-amino acid oxidase Homo sapiens 104-107 30959013-6 2019 In addition, inverse correlations also existed in the reconstructed group between distensibility of the DAo and the exercise variables such as peak oxygen pulse (R = 0.56, p = 0.02), peak oxygen consumption (R = 0.63, p = 0.008), oxygen consumption at ventilatory anaerobic threshold (R = 0.48, p = 0.04), and peak work (R = 0.54, p = 0.02). Oxygen 188-194 D-amino acid oxidase Homo sapiens 104-107 22715431-4 2012 Here, we used polyethylene glycol-conjugated D-amino acid oxidase (PEG-DAO) as an H(2)O(2) source. Oxygen 85-90 D-amino acid oxidase Homo sapiens 71-74 28412161-1 2017 OBJECTIVES: We sought to examine the physiological impact the apneic period has on the respiratory physiology of patients undergoing intubation in the emergency department and whether DAO, the delivery of 15L oxygen by nasal cannula during apnea, can affect the development of respiratory acidosis. Oxygen 209-215 D-amino acid oxidase Homo sapiens 184-187 28191958-8 2017 The reduced cofactors of the DAAO subunits were reoxidized by the evolved molecular oxygen around. Oxygen 84-90 D-amino acid oxidase Homo sapiens 29-33 28159615-7 2017 On the other hand, the generated H2O2 of ELP-DAAO was decomposed by the MnO2 nanorods, and the evolved oxygen oxidized the reduced cofactors of ELP-DAAO. Oxygen 103-109 D-amino acid oxidase Homo sapiens 45-49 28159615-7 2017 On the other hand, the generated H2O2 of ELP-DAAO was decomposed by the MnO2 nanorods, and the evolved oxygen oxidized the reduced cofactors of ELP-DAAO. Oxygen 103-109 D-amino acid oxidase Homo sapiens 148-152 22715431-5 2012 The enzyme DAO generates H(2)O(2) by using D-amino acid and oxygen as substrates. Oxygen 60-66 D-amino acid oxidase Homo sapiens 11-14 12632405-4 2003 In the scaled-up bioprocess with a 5-L bioreactor, immobilized VHb-DAO (2500 U/L) resulted in 99% bioconversion of 120 mM cephalosporin C within 60 min at an oxygen flow rate of 0.2 (v/v) x min. Oxygen 158-164 D-amino acid oxidase Homo sapiens 67-70 21397351-1 2011 D-Amino acid oxidase (DAAO) is a well-known flavoenzyme that catalyzes the oxygen-dependent oxidative deamination of amino acid D-isomers with absolute stereospecificity, which results in alpha-keto acids, ammonia and hydrogen peroxide. Oxygen 75-81 D-amino acid oxidase Homo sapiens 0-20 21397351-1 2011 D-Amino acid oxidase (DAAO) is a well-known flavoenzyme that catalyzes the oxygen-dependent oxidative deamination of amino acid D-isomers with absolute stereospecificity, which results in alpha-keto acids, ammonia and hydrogen peroxide. Oxygen 75-81 D-amino acid oxidase Homo sapiens 22-26 21397351-3 2011 Protein engineering has allowed for a redesign of DAAO substrate specificity, oxygen affinity, cofactor binding, stability, and oligomeric state. Oxygen 78-84 D-amino acid oxidase Homo sapiens 50-54 21182588-0 2011 On the reaction of D-amino acid oxidase with dioxygen: O2 diffusion pathways and enhancement of reactivity. Oxygen 45-53 D-amino acid oxidase Homo sapiens 19-39 21182588-0 2011 On the reaction of D-amino acid oxidase with dioxygen: O2 diffusion pathways and enhancement of reactivity. Oxygen 55-57 D-amino acid oxidase Homo sapiens 19-39 21182588-2 2011 We also have recently described channels that might allow access of oxygen to pockets at the active site of the flavoprotein D-amino acid oxidase (DAAO) that have a high affinity for dioxygen and are in close proximity to the flavin. Oxygen 68-74 D-amino acid oxidase Homo sapiens 125-145 21182588-2 2011 We also have recently described channels that might allow access of oxygen to pockets at the active site of the flavoprotein D-amino acid oxidase (DAAO) that have a high affinity for dioxygen and are in close proximity to the flavin. Oxygen 68-74 D-amino acid oxidase Homo sapiens 147-151 21182588-2 2011 We also have recently described channels that might allow access of oxygen to pockets at the active site of the flavoprotein D-amino acid oxidase (DAAO) that have a high affinity for dioxygen and are in close proximity to the flavin. Oxygen 183-191 D-amino acid oxidase Homo sapiens 125-145 21182588-2 2011 We also have recently described channels that might allow access of oxygen to pockets at the active site of the flavoprotein D-amino acid oxidase (DAAO) that have a high affinity for dioxygen and are in close proximity to the flavin. Oxygen 183-191 D-amino acid oxidase Homo sapiens 147-151 21182588-3 2011 With the goal of enhancing the reactivity of DAAO with oxygen, we have performed site-saturation mutagenesis at three positions that flank the putative oxygen channels and high-affinity sites. Oxygen 55-61 D-amino acid oxidase Homo sapiens 45-49 21182588-5 2011 The biochemical properties of these variants have been studied and compared with those of wild-type DAAO, with emphasis on the reactivity of the reduced enzyme species with dioxygen. Oxygen 173-181 D-amino acid oxidase Homo sapiens 100-104 21182588-9 2011 The increase in O(2) reactivity observed for T201L DAAO is of great interest for designing new flavoenzymes for biotechnological applications. Oxygen 16-20 D-amino acid oxidase Homo sapiens 51-55 20498362-1 2010 Molecular dynamics simulations and implicit ligand sampling methods have identified trajectories and sites of high affinity for O(2) in the protein framework of the flavoprotein D-amino-acid oxidase (DAAO). Oxygen 128-132 D-amino acid oxidase Homo sapiens 178-198 20498362-1 2010 Molecular dynamics simulations and implicit ligand sampling methods have identified trajectories and sites of high affinity for O(2) in the protein framework of the flavoprotein D-amino-acid oxidase (DAAO). Oxygen 128-132 D-amino acid oxidase Homo sapiens 200-204 19694805-4 2009 Using the directed evolution approach, one DAAO mutant was identified that has increased activity at low O2 and D-Ala concentrations and a 10-fold lower K(m) for O2. Oxygen 105-107 D-amino acid oxidase Homo sapiens 43-47 19694805-4 2009 Using the directed evolution approach, one DAAO mutant was identified that has increased activity at low O2 and D-Ala concentrations and a 10-fold lower K(m) for O2. Oxygen 162-164 D-amino acid oxidase Homo sapiens 43-47 7908225-1 1994 D-Amino acid oxidase catalyzes the oxidation of D-amino acids to imino acids with subsequent transfer of the electrons to molecular oxygen. Oxygen 132-138 D-amino acid oxidase Homo sapiens 0-20 10920257-6 2000 The low affinity of homarine (N-methylpicolinate) for oxidized DAO, as in the case of o-methylbenzoate, is due to steric hindrance: one of the ortho carbons of benzoate is near the phenol carbons of Tyr228 and the other ortho carbon is near the carbonyl oxygen of Gly313. Oxygen 254-260 D-amino acid oxidase Homo sapiens 63-66 10704992-3 1999 Optimum pH, optimum temperature and K(m)95% was achieved by using 3% (w/v) solution of ceph C, 48 U of DAAO per g of ceph C, keeping dissolved oxygen level above 50%, maintaining the pH between 7.6 and 7.8 and temperature at 24 degrees C. The immobilized DAAO was used for 60 cycles in a stirred tank reactor. Oxygen 143-149 D-amino acid oxidase Homo sapiens 103-107