Characterization of 4-hydroxyphenylacetate 3-hydroxylase (HpaB) of Escherichia coli as a reduced flavin adenine dinucleotide-utilizing monooxygenase.
about
The Rut pathway for pyrimidine degradation: novel chemistry and toxicity problemsA flavin-dependent monooxygenase from Mycobacterium tuberculosis involved in cholesterol catabolismCatalysis of a flavoenzyme-mediated amide hydrolysisCharacterization of chlorophenol 4-monooxygenase (TftD) and NADH:flavin adenine dinucleotide oxidoreductase (TftC) of Burkholderia cepacia AC1100Crystal structure of the oxygenase component (HpaB) of the 4-hydroxyphenylacetate 3-monooxygenase from Thermus thermophilus HB8Crystal Structures of NADH:FMN Oxidoreductase (EmoB) at Different Stages of Catalysis4-Hydroxyacetophenone monooxygenase from Pseudomonas fluorescens ACB. A novel flavoprotein catalyzing Baeyer-Villiger oxidation of aromatic compoundsBiodegradation of aromatic compounds by Escherichia coliBiotechnological production of plant-specific hydroxylated phenylpropanoidsMechanism and regulation of the Two-component FMN-dependent monooxygenase ActVA-ActVB from Streptomyces coelicolorCrystal Structures of SgcE6 and SgcC, the Two-Component Monooxygenase That Catalyzes Hydroxylation of a Carrier Protein-Tethered Substrate during the Biosynthesis of the Enediyne Antitumor Antibiotic C-1027 in Streptomyces globisporus.Cloning, sequencing, and characterization of a gene cluster involved in EDTA degradation from the bacterium BNC1.Isolation and purification of Thermus thermophilus HpaB by a crystallization approach.Production of three phenylethanoids, tyrosol, hydroxytyrosol, and salidroside, using plant genes expressing in Escherichia coliIdentification, purification, and characterization of iminodiacetate oxidase from the EDTA-degrading bacterium BNC1phzO, a gene for biosynthesis of 2-hydroxylated phenazine compounds in Pseudomonas aureofaciens 30-84.A single monooxygenase, ese, is involved in the metabolism of the organochlorides endosulfan and endosulfate in an Arthrobacter sp.Paerucumarin, a new metabolite produced by the pvc gene cluster from Pseudomonas aeruginosa.Complementarity of ensemble and single-molecule measures of protein motion: a relaxation dispersion NMR study of an enzyme complexCloning of a gene cluster involved in the catabolism of p-nitrophenol by Arthrobacter sp. strain JS443 and characterization of the p-nitrophenol monooxygenaseFunctions of flavin reductase and quinone reductase in 2,4,6-trichlorophenol degradation by Cupriavidus necator JMP134Structural and biochemical characterization of EDTA monooxygenase and its physical interaction with a partner flavin reductase.Biochemical characterization of StyAB from Pseudomonas sp. strain VLB120 as a two-component flavin-diffusible monooxygenaseGenetic and biochemical characterization of a 2,4,6-trichlorophenol degradation pathway in Ralstonia eutropha JMP134.Crystallization and preliminary X-ray analysis of the oxygenase component (HpaB) of 4-hydroxyphenylacetate 3-monooxygenase from Thermus thermophilus HB8.Identification and characterization of the flavin:NADH reductase (PrnF) involved in a novel two-component arylamine oxygenase.A two-component flavin-dependent monooxygenase involved in actinorhodin biosynthesis in Streptomyces coelicolor.Mechanism of 4-nitrophenol oxidation in Rhodococcus sp. Strain PN1: characterization of the two-component 4-nitrophenol hydroxylase and regulation of its expression.A novel two-protein component flavoprotein hydroxylase.Reduced flavins promote oxidative DNA damage in non-respiring Escherichia coli by delivering electrons to intracellular free iron.FAD is a preferred substrate and an inhibitor of Escherichia coli general NAD(P)H:flavin oxidoreductase.Phenol hydroxylase from Bacillus thermoglucosidasius A7, a two-protein component monooxygenase with a dual role for FAD.A monooxygenase catalyzes sequential dechlorinations of 2,4,6-trichlorophenol by oxidative and hydrolytic reactions.Initial investigations of C4a-(hydro)peroxyflavin intermediate formation by dibenzothiophene monooxygenase.A two-component hydroxylase involved in the assimilation of 3-hydroxyphenyl acetate in Pseudomonas putida.An aromatic hydroxylation reaction catalyzed by a two-component FMN-dependent Monooxygenase. The ActVA-ActVB system from Streptomyces coelicolor.RutA-Catalyzed Oxidative Cleavage of the Uracil Amide Involves Formation of a Flavin-N5-oxide.Elucidation of the trigonelline degradation pathway reveals previously undescribed enzymes and metabolites.Biosynthesis of Tropolones in Streptomyces spp: Interweaving Biosynthesis and Degradation of Phenylacetic Acid and Hydroxylations on Tropone Ring.Two-Component FAD-Dependent Monooxygenases: Current Knowledge and Biotechnological Opportunities
P2860
Q24596433-EAA9DEF3-A4A6-4213-80FC-E0BBD2E23088Q24609899-3DC9265D-1A9B-498F-B03F-A9963B4C7CCCQ24610928-1EDC318F-F514-4DA3-B510-C3AEEBA85D2BQ24676583-A9682B14-72B7-46AC-B7FA-0755CED9D3B1Q27647881-8384D9A9-7C1B-494D-8B25-6A49712784C2Q27651551-A231D0BE-DB91-4558-BBD9-C3350C2170E2Q28185572-85AADE9F-CE13-4F99-A4E7-7D731B7F2110Q28208239-FF385480-CE17-4A87-B332-EC7573EC3CD7Q28238654-B3AB789F-4DA4-4CC8-A6C3-78B4977B171AQ28757790-A5BF0089-1B7A-47C0-855E-5A8AEB1F098FQ30152739-7CFA6C71-359E-4C84-9D9A-64D412DD2011Q30649466-65738EA4-4DBC-4A5C-8CF6-7698A39FDFA8Q33707357-80C2FDC5-B546-4746-9865-4BF8F952240DQ33746925-E0A07CBD-6A19-4033-A53D-F68CA0A9195BQ33988840-71C579A2-1F60-4102-AD4D-805F7A8C42D1Q33995251-17FE49FA-DBE0-4C17-870F-622C8941C81EQ34649694-F43D745B-42F2-4498-9CEE-FD02FE91753DQ34806014-714B45AF-343F-46EE-B031-F18E514C6FF5Q35033085-979B4520-B2D9-4E9B-8DE3-4DC746471C63Q36314849-E57572E3-C49D-465E-B18D-72DDDDF1FE41Q36483252-7415C53F-00AF-45F3-86E5-A7088ACAB2E0Q36984484-0A970B75-6DDB-49C7-AD08-AA245F571DEDQ37007744-615F936D-8DE7-43D4-BBCB-E4F3587B087EQ39679593-4DAF4BA3-008F-45AD-8618-998D1A028459Q41955823-5FD8521B-199C-4086-BBB2-B2CD263560B5Q41983662-114A18C7-661E-4926-9E89-7384FFD4D11EQ42632990-BABAA6F0-6562-4A91-9195-0F8F43EEAF05Q43248279-6CA52D93-78DB-4E15-BD53-01E549F7EE63Q43782483-FD44A313-A990-4E0C-90E6-AC5178C14FD3Q44038769-0B7FAEF1-4E1E-47A6-8D99-2C801AFFD778Q44102186-738D1E60-0315-40F7-A474-66411ECEBEB4Q44580840-81463933-0871-43F3-BE8D-EB8B03F2E857Q44684915-63AAA83C-C629-4EF5-B375-796AE714B551Q46304816-9EB38D17-77C7-4C00-BAD8-94530B487345Q46468787-6035F162-06F0-4324-BBAC-A17C74B3E050Q46788461-D2FE1FC5-258A-4A50-ABAD-B5DE235CC472Q48201609-9A6F1C37-EC01-4763-98C6-DC68DD65ED78Q52568665-1011DEB3-CF0E-4607-8E22-B0743573CA04Q52589142-2AC03A68-99F3-407B-84DB-B1BB8E8E99A7Q58802616-5EF62CFD-B01C-495F-9486-C71970A336E4
P2860
Characterization of 4-hydroxyphenylacetate 3-hydroxylase (HpaB) of Escherichia coli as a reduced flavin adenine dinucleotide-utilizing monooxygenase.
description
2000 nî lūn-bûn
@nan
2000年の論文
@ja
2000年学术文章
@wuu
2000年学术文章
@zh-cn
2000年学术文章
@zh-hans
2000年学术文章
@zh-my
2000年学术文章
@zh-sg
2000年學術文章
@yue
2000年學術文章
@zh
2000年學術文章
@zh-hant
name
Characterization of 4-hydroxyp ...... otide-utilizing monooxygenase.
@en
Characterization of 4-hydroxyphenylacetate 3-hydroxylase
@nl
type
label
Characterization of 4-hydroxyp ...... otide-utilizing monooxygenase.
@en
Characterization of 4-hydroxyphenylacetate 3-hydroxylase
@nl
prefLabel
Characterization of 4-hydroxyp ...... otide-utilizing monooxygenase.
@en
Characterization of 4-hydroxyphenylacetate 3-hydroxylase
@nl
P2860
P1476
Characterization of 4-hydroxyp ...... otide-utilizing monooxygenase.
@en
P2093
P2860
P304
P356
10.1128/AEM.66.2.481-486.2000
P407
P577
2000-02-01T00:00:00Z