PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 2023912-1 1991 Monoamine oxidases A and B [MAOA and MAOB; amine:oxygen oxidoreductase (deaminating) (flavin-containing), EC 1.4.3.4] play important roles in the metabolism of neuroactive, vasoactive amines and the Parkinsonism-producing neurotoxin 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP). 4,6-dinitro-o-cresol 86-92 monoamine oxidase A Homo sapiens 0-26 7931244-3 1994 The calculation using ab initio molecular orbital methods of the electronic properties of flavin and befloxatone, a reversible inhibitor of MAO A, led to a description of the interaction between aryl-oxazolidinones and the cofactor of the enzyme. 4,6-dinitro-o-cresol 90-96 monoamine oxidase A Homo sapiens 140-145 8443155-1 1993 Monoamine oxidases A and B have identical flavin sites but different, although overlapping, amine substrate specificity. 4,6-dinitro-o-cresol 42-48 monoamine oxidase A Homo sapiens 0-26 2023912-1 1991 Monoamine oxidases A and B [MAOA and MAOB; amine:oxygen oxidoreductase (deaminating) (flavin-containing), EC 1.4.3.4] play important roles in the metabolism of neuroactive, vasoactive amines and the Parkinsonism-producing neurotoxin 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP). 4,6-dinitro-o-cresol 86-92 monoamine oxidase A Homo sapiens 28-32 2747630-1 1989 Monoamine oxidases (MAOs) A and B, flavin-containing enzymes found in the outer mitochondrial membrane, oxidize many important biogenic and xenobiotic amines. 4,6-dinitro-o-cresol 35-41 monoamine oxidase A Homo sapiens 0-33 7196439-8 1981 This evidence indicates that the structural gene for the flavin polypeptide of MAO-A is on the human X chromosome. 4,6-dinitro-o-cresol 57-63 monoamine oxidase A Homo sapiens 79-84 27734680-3 2016 In this work, we present atomistic empirical valence bond simulations of the rate-limiting step of the MAO-A-catalyzed NA (norepinephrine) degradation, involving hydride transfer from the substrate alpha-methylene group to the flavin moiety of the flavin adenine dinucleotide prosthetic group, employing the full dimensionality and thermal fluctuations of the hydrated enzyme, with extensive configurational sampling. 4,6-dinitro-o-cresol 227-233 monoamine oxidase A Homo sapiens 103-108 21476070-12 2011 The results are contrary to the previous kinetic experiments and the computational study on the effect of p-substituents in the flavin reduction of MAO A by p-substituted benzylamine analogs. 4,6-dinitro-o-cresol 128-134 monoamine oxidase A Homo sapiens 148-153 25755053-7 2015 Spectral changes during inactivation of MAO A included bleaching at 456 nm and an increased absorbance at 400 nm, consistent with flavin modification. 4,6-dinitro-o-cresol 130-136 monoamine oxidase A Homo sapiens 40-45 17480205-6 2007 Agmatine, a putative endogenous ligand for some imidazoline sites, reduced monoamine oxidase A under anaerobic conditions, indicating that it binds close to the flavin in the active site. 4,6-dinitro-o-cresol 161-167 monoamine oxidase A Homo sapiens 75-94 19645722-7 2009 Compared to purified wild-type and Ser209Ala MAO A proteins, the Ser209Glu MAO A mutant shows significant differences in covalent flavin fluorescence yield, CD spectra and thermal stability. 4,6-dinitro-o-cresol 130-136 monoamine oxidase A Homo sapiens 75-80 18044898-12 2007 DAAO contains a noncovalently bound flavin whereas MAO A contains a flavin covalently bound to a cysteinyl residue at C8alpha. 4,6-dinitro-o-cresol 68-74 monoamine oxidase A Homo sapiens 51-56 14697881-7 2004 This structural information is then used to explain previous studies on flavin analog incorporation into either MAO B or into MAO A. 4,6-dinitro-o-cresol 72-78 monoamine oxidase A Homo sapiens 126-131 16605246-1 2006 Current structural results of several flavin-dependent amine oxidizing enzymes including human monoamine oxidases A and B (MAO A and MAO B) show aromatic amino acid residues oriented approximately perpendicular to the flavin ring, suggesting a functional role in catalysis. 4,6-dinitro-o-cresol 38-44 monoamine oxidase A Homo sapiens 95-121 16605246-1 2006 Current structural results of several flavin-dependent amine oxidizing enzymes including human monoamine oxidases A and B (MAO A and MAO B) show aromatic amino acid residues oriented approximately perpendicular to the flavin ring, suggesting a functional role in catalysis. 4,6-dinitro-o-cresol 38-44 monoamine oxidase A Homo sapiens 123-128 16467939-7 2006 In addition, the calculated rate constants showed a correlation with the rate of reduction of the flavin in MAO-A. 4,6-dinitro-o-cresol 98-104 monoamine oxidase A Homo sapiens 108-113 17401535-5 2007 Decreased pH induced a blue shift in the spectral maximum of MAO-A indicative of a more hydrophobic environment around the flavin, and also influenced the redox properties of the flavin. 4,6-dinitro-o-cresol 123-129 monoamine oxidase A Homo sapiens 61-66 17401535-5 2007 Decreased pH induced a blue shift in the spectral maximum of MAO-A indicative of a more hydrophobic environment around the flavin, and also influenced the redox properties of the flavin. 4,6-dinitro-o-cresol 179-185 monoamine oxidase A Homo sapiens 61-66 15950194-3 2005 Two types of spectral changes, either increasing the absorbance at 510 nm or decreasing it at 495 nm depending on the group nearest to the flavin cofactor, were seen on ligand binding to MAO A. 4,6-dinitro-o-cresol 139-145 monoamine oxidase A Homo sapiens 187-192 11761328-4 2001 Current knowledge on the mechanism of covalent flavin attachment is discussed based on studies on the 8alpha-S-cysteinylFAD of monoamine oxidases A and B, as well as studies on other flavoenzymes. 4,6-dinitro-o-cresol 47-53 monoamine oxidase A Homo sapiens 127-153 12445480-5 2002 The inhibitors, D-amphetamine, harmine, tetrindole, and befloxatone all induce similar (but not identical) changes in the spectrum of MAO A, consistent with stacking of inhibitor with the flavin in the active site. 4,6-dinitro-o-cresol 188-194 monoamine oxidase A Homo sapiens 134-139 12781338-9 2003 These results indicate that the active site of MAO A is far more sensitive to structural variation than would be predicted by the simple flavin stacking model. 4,6-dinitro-o-cresol 137-143 monoamine oxidase A Homo sapiens 47-52 10438531-10 1999 MAO A partially purified from yeast grown on 8-nor-8-chlororiboflavin exhibited an absorption spectrum indicating the covalent flavin is an 8-nor-8-S-thioflavin, suggesting a nucleophilic displacement mechanism that supports the quinone-methide mechanism previously suggested as a general mechanism for covalent flavin attachment. 4,6-dinitro-o-cresol 63-69 monoamine oxidase A Homo sapiens 0-5 10438531-0 1999 Influence of flavin analogue structure on the catalytic activities and flavinylation reactions of recombinant human liver monoamine oxidases A and B. 4,6-dinitro-o-cresol 13-19 monoamine oxidase A Homo sapiens 122-148 10438531-6 1999 The selectivities of MAO A and MAO B for flavin analogue incorporation are found to be similar, although 8alpha-methylation of the flavin resulted in a higher level of catalytic activity for MAO B than for MAO A. 4,6-dinitro-o-cresol 41-47 monoamine oxidase A Homo sapiens 21-26 10438531-6 1999 The selectivities of MAO A and MAO B for flavin analogue incorporation are found to be similar, although 8alpha-methylation of the flavin resulted in a higher level of catalytic activity for MAO B than for MAO A. 4,6-dinitro-o-cresol 131-137 monoamine oxidase A Homo sapiens 21-26 10438531-6 1999 The selectivities of MAO A and MAO B for flavin analogue incorporation are found to be similar, although 8alpha-methylation of the flavin resulted in a higher level of catalytic activity for MAO B than for MAO A. 4,6-dinitro-o-cresol 131-137 monoamine oxidase A Homo sapiens 206-211 10606764-0 2000 The FAD binding sites of human liver monoamine oxidases A and B: investigation of the role of flavin ribityl side chain hydroxyl groups in the covalent flavinylation reaction and catalytic activities. 4,6-dinitro-o-cresol 94-100 monoamine oxidase A Homo sapiens 37-63 10606764-1 2000 The role of ribityl side chain hydroxyl groups of the flavin moiety in the covalent flavinylation reaction and catalytic activities of recombinant human liver monoamine oxidases (MAO) A and B have been investigated using the riboflavin analogue: N(10)-omega-hydroxypentyl-isoalloxazine. 4,6-dinitro-o-cresol 54-60 monoamine oxidase A Homo sapiens 159-191 10438531-10 1999 MAO A partially purified from yeast grown on 8-nor-8-chlororiboflavin exhibited an absorption spectrum indicating the covalent flavin is an 8-nor-8-S-thioflavin, suggesting a nucleophilic displacement mechanism that supports the quinone-methide mechanism previously suggested as a general mechanism for covalent flavin attachment. 4,6-dinitro-o-cresol 127-133 monoamine oxidase A Homo sapiens 0-5