What's in a covalent bond? On the role and formation of covalently bound flavin cofactors.
about
SDH5, a gene required for flavination of succinate dehydrogenase, is mutated in paragangliomaSdhE is a conserved protein required for flavinylation of succinate dehydrogenase in bacteriaThe Crystal Structure and Mechanism of an Unusual Oxidoreductase, GilR, Involved in Gilvocarcin V BiosynthesisCatalytic and Structural Role of a Conserved Active Site Histidine in Berberine Bridge EnzymeRationally engineered flavin-dependent oxidase reveals steric control of dioxygen reductionDiscovery of a xylooligosaccharide oxidase from Myceliophthora thermophila C1Flavinylation and assembly of succinate dehydrogenase are dependent on the C-terminal tail of the flavoprotein subunit.UbiX is a flavin prenyltransferase required for bacterial ubiquinone biosynthesisBiochemical Characterization of Putative Adenylate Dimethylallyltransferase and Cytokinin Dehydrogenase from Nostoc sp. PCC 7120Structural and biochemical analyses reveal insights into covalent flavinylation of the Escherichia coli Complex II homolog quinol:fumarate reductase.Expression of zebrafish (Danio rerio) monoamine oxidase (MAO) in Pichia pastoris: purification and comparison with human MAO A and MAO B.Emerging concepts in the flavinylation of succinate dehydrogenaseComplexity generation in fungal peptidyl alkaloid biosynthesis: oxidation of fumiquinazoline A to the heptacyclic hemiaminal fumiquinazoline C by the flavoenzyme Af12070 from Aspergillus fumigatus.Evidence for Posttranslational Protein Flavinylation in the Syphilis Spirochete Treponema pallidum: Structural and Biochemical Insights from the Catalytic Core of a Periplasmic Flavin-Trafficking ProteinCatalytic Amine Oxidation under Ambient Aerobic Conditions: Mimicry of Monoamine Oxidase BCharacterization of a flavoprotein oxidase from opium poppy catalyzing the final steps in sanguinarine and papaverine biosynthesisRedox state of flavin adenine dinucleotide drives substrate binding and product release in Escherichia coli succinate dehydrogenase.Binding of the Covalent Flavin Assembly Factor to the Flavoprotein Subunit of Complex II.Molecular insights into the enzymatic diversity of flavin-trafficking protein (Ftp; formerly ApbE) in flavoprotein biogenesis in the bacterial periplasm.Cholesterol oxidase: biochemistry and structural features.Functional diversity of organic molecule enzyme cofactors.Riboflavin interactions with oxygen-a survey from the photochemical perspective.Reaction of pyranose dehydrogenase from Agaricus meleagris with its carbohydrate substrates.The Crystal Structure of RosB: Insights into the Reaction Mechanism of the First Member of a Family of Flavodoxin-like Enzymes.Pyranose Dehydrogenase from Agaricus campestris and Agaricus xanthoderma: Characterization and Applications in Carbohydrate Conversions.Alternative pyrimidine biosynthesis protein ApbE is a flavin transferase catalyzing covalent attachment of FMN to a threonine residue in bacterial flavoproteins.Spectroscopic characterization of radicals and radical pairs in fruit fly cryptochrome - protonated and nonprotonated flavin radical-states.A Remarkable Oxidative Cascade That Replaces the Riboflavin C8 Methyl with an Amino Group during Roseoflavin Biosynthesis.Secretory production of an FAD cofactor-containing cytosolic enzyme (sorbitol-xylitol oxidase from Streptomyces coelicolor) using the twin-arginine translocation (Tat) pathway of Corynebacterium glutamicum.Agaricus meleagris pyranose dehydrogenase: influence of covalent FAD linkage on catalysis and stability.Proline dehydrogenase from Thermus thermophilus does not discriminate between FAD and FMN as cofactor.Analysis of covalent flavinylation using thermostable succinate dehydrogenase from Thermus thermophilus and Sulfolobus tokodaii lacking SdhE homologs.The succinate dehydrogenase assembly factor, SdhE, is required for the flavinylation and activation of fumarate reductase in bacteria.Kinetic characterization of Vibrio cholerae ApbE: Substrate specificity and regulatory mechanisms.Characterization of Two VAO-Type Flavoprotein Oxidases from Myceliophthora thermophila.Why the Flavin Adenine Dinucleotide (FAD) Cofactor Needs To Be Covalently Linked to Complex II of the Electron-Transport Chain for the Conversion of FADH2 into FAD.ONIOM calculations on serotonin degradation by monoamine oxidase B: insight into the oxidation mechanism and covalent reversible inhibition.Bioorthogonal Catalytic Activation of Platinum and Ruthenium Anticancer Complexes by FAD and Flavoproteins.The role of conserved residues in Fdc decarboxylase in prenylated flavin mononucleotide oxidative maturation, cofactor isomerization, and catalysis.Crystal structure of bacterial succinate:quinone oxidoreductase flavoprotein SdhA in complex with its assembly factor SdhE.
P2860
Q24317137-A76FC7A6-74F9-4925-955E-E9C756948021Q24614194-7359D7DD-6F60-4D5B-9273-E344B6F8417AQ27667796-BF5F269A-911A-40A0-AA67-2CA8DD0A2E7FQ27670626-2D6AB070-7A8E-44D3-8884-45D6D95BD8FCQ27697651-4FF6D2BC-37D8-4E9D-9DB8-9150DCB04934Q27728067-33772700-0F42-4549-95A2-D72A10C2561AQ27939226-3FB5295F-BE70-4DBD-A1B2-AAA6EBCA4562Q28492798-5CDC0975-AD2A-4840-886D-76BA535A546AQ28548064-F8422FB8-3EE2-442C-B2CF-9FB63F0293C7Q30403072-0DDFD96D-09AA-4637-80F0-169EC28D5C8EQ33524624-C3E52E22-3F82-4438-AD40-7A3972616DF3Q34326128-11CEB375-EB7B-4FB2-8EF7-0851FFCE8FD8Q35355749-2D0BE115-08A5-4ED2-95F8-7305E88D0D9FQ35620143-8B91A5AD-D667-492F-94A0-5AF96B7D6C35Q35914850-34D9D77D-35BE-49D5-A207-9BA37FB7891BQ36466783-1B354884-5D64-4E21-8203-4C5252EA9E03Q36514689-75107353-F414-493A-BC38-BF19FB4FD0ADQ36548399-007224C4-98B5-49AA-82CF-131F8E37D7D6Q36618812-A7B533EF-D7D2-4D54-9F63-1F7F347F8CE7Q37618284-D796EE2C-9B6F-42E1-A3E9-2DEE948A4DDEQ38128203-DCF933CE-D570-4C94-B243-C55534170526Q38258793-3E6E86E3-CDF5-440F-9C65-52D5D85AC5FEQ38297015-F794CBAF-CBDB-4150-9DF5-7C40D1AAC668Q39095970-EE411D32-35C7-4C7E-9342-AB5B39AED181Q39871510-FF38EE04-F532-4E6C-8995-EA5D99D16C69Q40776425-9F4295A7-C3FE-487F-B02E-A359103E992AQ41065942-0D90C78E-253A-4C8D-B89F-0309E43983C0Q41698296-D77B0CC3-4E37-4250-8E68-5A8C2DFCE287Q41905339-EC3B5FF1-5F20-437B-9E94-97EB01A06F96Q42128322-CC19DD74-3444-42B4-A7B8-39F21BFFBF7AQ42318672-1E6C09D8-6BAD-41FD-AB11-E1D9D68AEC75Q43021029-2AE5CDE4-999D-4A27-9ADB-3FF4F8F00E52Q43806832-BB68F31E-B974-4FC2-9A9D-43146CF2B719Q46021696-9DD30F65-2F7A-4558-8944-06F7DC496CACQ47230056-99D86DDD-B5E8-4126-A8B6-772E9ECC047DQ47362659-B6470D7E-24B1-456B-901A-48734673F5E3Q48041536-784628CA-7D0B-48AA-92FA-56FEFA3DAF33Q49848669-53BDDB86-62A2-488F-9E61-DC47430B5782Q51771697-36462685-6476-4F5F-B7F4-2AA04EF239EEQ52364046-40A734FE-67D0-4614-944C-7EEE29E08EBE
P2860
What's in a covalent bond? On the role and formation of covalently bound flavin cofactors.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 05 May 2009
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
What's in a covalent bond? On ...... lently bound flavin cofactors.
@en
What's in a covalent bond? On ...... lently bound flavin cofactors.
@nl
type
label
What's in a covalent bond? On ...... lently bound flavin cofactors.
@en
What's in a covalent bond? On ...... lently bound flavin cofactors.
@nl
prefLabel
What's in a covalent bond? On ...... lently bound flavin cofactors.
@en
What's in a covalent bond? On ...... lently bound flavin cofactors.
@nl
P2093
P2860
P1433
P1476
What's in a covalent bond? On ...... lently bound flavin cofactors.
@en
P2093
Dominic P H M Heuts
Marco W Fraaije
Nigel S Scrutton
William S McIntire
P2860
P304
P356
10.1111/J.1742-4658.2009.07053.X
P407
P577
2009-05-05T00:00:00Z