flavin adenine dinucleotide binding

flavin adenine dinucleotide binding

Item
http://www.wikidata.org/entity/Q14599303
Xanthine dehydrogenase24-dehydrocholesterol reductaseMethylenetetrahydrofolate reductaseCytochrome b-245, beta polypeptideGlutathione reductaseMonoamine oxidase ASuccinate dehydrogenase complex, subunit A, flavoprotein (Fp)Dihydrolipoamide dehydrogenaseP450 (cytochrome) oxidoreductaseSqualene epoxidaseFlavin containing monooxygenase 3Nitric oxide synthase 3, endothelial cellXanthine dehydrogenaseglutathione reductaseAcyl-CoA oxidase 3, pristanoylAcyl-CoA oxidase 1Acyl-CoA oxidase 2Acyl-CoA oxidase likePutative dimethylaniline monooxygenase [N-oxide-forming] 6Flavin containing dimethylaniline monoxygenase 4Flavin containing dimethylaniline monoxygenase 5Flavin containing dimethylaniline monoxygenase 1Flavin containing dimethylaniline monoxygenase 2Acyl-CoA dehydrogenase short/branched chainD-2-hydroxyglutarate dehydrogenaseThioredoxin reductase 1Dihydrouridine synthase 4 likeDihydrouridine synthase 1 likeDihydrouridine synthase 3 likeDihydrouridine synthase 2Lysine demethylase 1AAcyl-CoA dehydrogenase family member 10Acyl-CoA dehydrogenase family member 11Monoamine oxidase BGrowth factor, augmenter of liver regenerationCoenzyme Q6, monooxygenaseElectron transfer flavoprotein dehydrogenaseFAD dependent oxidoreductase domain containing 2Acyl-CoA dehydrogenase medium chainAcyl-CoA dehydrogenase short chain
P680
Mutation at histidine 338 of gp91(phox) depletes FAD and affects expression of cytochrome b558 of the human NADPH oxidaseThe intraflavin hydrogen bond in human electron transfer flavoprotein modulates redox potentials and may participate in electron transferMechanism of coenzyme binding to human methionine synthase reductase revealed through the crystal structure of the FNR-like module and isothermal titration calorimetryCharacterization of mutations in severe methylenetetrahydrofolate reductase deficiency reveals an FAD-responsive mutationAn electron-transfer path through an extended disulfide relay system: the case of the redox protein ALRThe human apoptosis-inducing protein AMID is an oxidoreductase with a modified flavin cofactor and DNA binding activityStructure of electron transfer flavoprotein-ubiquinone oxidoreductase and electron transfer to the mitochondrial ubiquinone poolA luminal flavoprotein in endoplasmic reticulum-associated degradationExpression and characterization of two pathogenic mutations in human electron transfer flavoproteinHistone demethylation mediated by the nuclear amine oxidase homolog LSD1
P921
Q1436420-821040F3-734B-4D8F-8054-7A5FD213F5C1Q1436420-C7F29009-3680-4037-A469-8250B8949C97Q14599665-EC1DE70E-3629-427E-B597-F2A439F042C2Q14864925-EFEC76D7-B8E8-4CA3-8917-ACBBB636698EQ14875845-58A0F366-43E4-43E7-92DD-619D677A5E44Q14878284-6747048C-B383-4EF8-A8FB-676A53479296Q14878284-9612979C-A8AA-4918-9988-7995BD67719CQ14888440-B7E33F31-97A0-4F8B-97FD-A42B142746F4Q14907258-4349EA80-70BF-40C5-A51B-8C03CD76C80FQ14907258-95B064AF-F3DB-4267-B506-74514F58A0B0Q14909061-1C546BE1-79CF-4B3F-917B-2C001B066EA9Q14909061-E45E4423-6EFC-4502-88B4-E1BAF306C083Q14909447-0D3B57E0-C633-422D-A176-29431F14B097Q14909447-64032544-B02C-48EA-9E4F-7A034AE0B49EQ14912992-CFE06210-FBF3-455E-9120-6384F6F4D2C3Q14914446-16FC5D8E-0BE8-419A-9B77-3F678B96DD03Q15328616-1ACC39FA-5603-493F-B7A4-E5AFEE2C351CQ15328616-F6B1898F-D3DF-41DC-9215-4DC99DF7E427Q15330879-274E5DBD-48D4-42E7-926B-7474F7E61AC5Q18972343-4C546B02-A497-446D-AF08-98A40A3F8D66Q21096281-2F2CDB27-4E25-4E41-89DB-DDF140B81A15Q21096281-95C31A51-BE11-4199-B0AF-66F9B80F56E0Q21096304-8D075689-251E-4E59-9A83-8799FDA368BCQ21096342-1E771D22-1AFE-4531-A85C-1E3DE9F4B920Q21096344-1209BC0C-35AE-4D81-971D-D3A0F88D8448Q21101448-7100F7E7-D524-49C4-AA71-A71E1AAB048BQ21101453-EFDAE8A0-CB8C-459E-B778-8E11C07D8BEEQ21101457-D3B06BA2-1170-49D7-BF15-FF83D36F6221Q21101459-247E2B18-E5E5-4DBD-B8A6-C17164D568FEQ21101467-36442EAC-7506-4B37-B54F-B5657C8180B7Q21104908-1358C6EC-A378-4734-BA0E-6566C1C1D14CQ21105749-582B95F6-DD04-4F27-AA98-79C780B00FDEQ21106751-03087C39-2317-4838-A73E-F8859ED41E01Q21107141-E99D6C94-4252-4BE2-A443-6FC853FC2CE0Q21107185-9329F102-A718-4987-AB34-48B4C5CFB24EQ21107192-CC2A037E-32FA-4575-A208-25B7C6FD242CQ21107237-D0A70AB0-A29F-47AD-9AAE-A5CD6CB4C499Q21108161-8D4053B0-B6E7-4F20-9720-4300DEDB732AQ21108161-CD79A693-BA5B-4526-B3EE-80EB5D4D19AAQ21109382-EA2EF444-807C-4749-B21D-C194349C864D
P680

flavin adenine dinucleotide binding

Item
http://www.wikidata.org/entity/Q14599303
description
Interacting selectively and no ...... D, or the reduced form, FADH2.
@en
moleculaire functie
@nl
name
flavin adenine dinucleotide binding
@en
legare a dinucleotidei flavină adenină
@ro
type
label
flavin adenine dinucleotide binding
@en
legare a dinucleotidei flavină adenină
@ro
altLabel
FAD or FADH2 binding
@en
GO:0050660
@en
flavine-adenine dinucleotide binding
@en
legarea FAD sau FADH2
@ro
prefLabel
flavin adenine dinucleotide binding
@en
legare a dinucleotidei flavină adenină
@ro
P279
P2888
P31
P527
P686
P279
P2888
P31
P527
P686