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Assay, Purification, and Partial Characterization of Choline Monooxygenase from SpinachMICAL-family proteins: Complex regulators of the actin cytoskeletonThe crystal structure of chorismate lyase shows a new fold and a tightly retained productProtein and ligand dynamics in 4-hydroxybenzoate hydroxylaseStructure of the monooxygenase component of a two-component flavoprotein monooxygenaseStructure and Ligand Binding Properties of the Epoxidase Component of Styrene Monooxygenase,Crystallographic trapping in the rebeccamycin biosynthetic enzyme RebCThe FAD Cofactor of RebC Shifts to an IN Conformation upon Flavin Reduction † , ‡Structural basis for a new tetracycline resistance mechanism relying on the TetX monooxygenaseTwo Structures of an N-Hydroxylating Flavoprotein Monooxygenase: ORNITHINE HYDROXYLASE FROM PSEUDOMONAS AERUGINOSAAn Unusual Role for a Mobile Flavin in StaC-like Indolocarbazole Biosynthetic EnzymesThe Substrate-Bound Crystal Structure of a Baeyer–Villiger Monooxygenase Exhibits a Criegee-like ConformationPutative dioxygen-binding sites and recognition of tigecycline and minocycline in the tetracycline-degrading monooxygenase TetXInterdomain binding of NADPH in p-hydroxybenzoate hydroxylase as suggested by kinetic, crystallographic and modeling studies of histidine 162 and arginine 269 variantsCatalytic mechanism of 2-hydroxybiphenyl 3-monooxygenase, a flavoprotein from Pseudomonas azelaica HBP1Structure and activity of the axon guidance protein MICALCrystal 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.Enantioselective substrate binding in a monooxygenase protein model by molecular dynamics and docking.Crystallographic evidence of drastic conformational changes in the active site of a flavin-dependent N-hydroxylase.Comparing protein-ligand interactions in solution and single crystals by Raman spectroscopy.Purification and properties of hydroquinone hydroxylase, a FAD-dependent monooxygenase involved in the catabolism of 4-hydroxybenzoate in Candida parapsilosis CBS604.High-resolution structure of the catalytic region of MICAL (molecule interacting with CasL), a multidomain flavoenzyme-signaling moleculeMolecular and biochemical characterization of the xlnD-encoded 3-hydroxybenzoate 6-hydroxylase involved in the degradation of 2,5-xylenol via the gentisate pathway in Pseudomonas alcaligenes NCIMB 9867Structure of an Aspergillus fumigatus old yellow enzyme (EasA) involved in ergot alkaloid biosynthesis.Accurate simulation and detection of coevolution signals in multiple sequence alignments.Design and properties of human D-amino acid oxidase with covalently attached flavinMultidimensional mutual information methods for the analysis of covariation in multiple sequence alignments.Crystallography gets the jump on the enzymologistsCrystal structure of LAAO from Calloselasma rhodostoma with an L-phenylalanine substrate: insights into structure and mechanismForm follows function: structural and catalytic variation in the class a flavoprotein monooxygenases.Biochemical characterization of a flavin adenine dinucleotide-dependent monooxygenase, ornithine hydroxylase from Pseudomonas aeruginosa, suggests a novel reaction mechanismPurine utilization by Klebsiella oxytoca M5al: genes for ring-oxidizing and -opening enzymes.Spectral and kinetic characterization of intermediates in the aromatization reaction catalyzed by NikD, an unusual amino acid oxidaseBinding of small-molecule ligands to proteins: "what you see" is not always "what you get".Structure, mechanism, and dynamics of UDP-galactopyranose mutase.Seeing the forest for the trees: fluorescence studies of single enzymes in the context of ensemble experiments.Structural and mechanistic basis of differentiated inhibitors of the acute pancreatitis target kynurenine-3-monooxygenaseCrystallization and preliminary X-ray crystallographic analysis of 2-methyl-3-hydroxypyridine-5-carboxylic acid (MHPC) oxygenase from Pseudomonas sp. MA-1.Structures of the Apo and FAD-bound forms of 2-hydroxybiphenyl 3-monooxygenase (HbpA) locate activity hotspots identified by using directed evolution.Crystal structure of p-hydroxybenzoate hydroxylase reconstituted with the modified FAD present in alcohol oxidase from methylotrophic yeasts: evidence for an arabinoflavin.
P2860
Q24672778-7C52D03B-5A04-49A3-9E43-6509B7539790Q26851932-D513B897-43E4-45BB-A816-4B7AB0679951Q27633269-3F23D3CF-7AC3-4700-957F-B2B689487DC0Q27637452-A3BAB82C-39A7-4317-AC3F-097E52D225EDQ27641194-AA3289DC-617C-4181-8123-2B0FC309D21CQ27646752-FD99E71D-F974-436F-A3BC-1424CA2E643DQ27648208-3B0623DA-4723-4BBA-9258-82DAB9F56646Q27652998-561209DE-8CB1-4E3E-BDDB-B2C84D210DF3Q27666972-3E6E86D0-E6F2-4FD2-BDCA-A9C7870ABA03Q27670798-6030DF64-6818-4BB1-B7D6-9BE3A1F85906Q27670926-3E0C3AAA-26D2-4EA6-ACE6-7CEFCCF49E83Q27678560-1B5093D2-C7D1-436A-951E-FF82E3EDCF81Q27685449-03C736D9-929D-4AA1-AD6C-1A2A1FBD82F8Q27764924-94C5CEC2-43F8-43DB-988F-66B46C597800Q28376299-58E4BA2B-B8D9-4444-B377-6FDC1F9AB831Q28507100-DB76C697-B076-4639-8678-0B22E08DB92CQ30152739-F2ABDFA2-CD7C-4FAB-8415-E4C0071ADCDFQ30356250-D01467C9-788E-439E-9597-7DBD52452517Q30588556-D8D77406-4DDE-484B-AAEC-8949EEE565B1Q30983365-5A9D9FAA-4577-4442-9DE0-D005A456039DQ31571906-6C1658C1-82DA-4DB2-9D66-D61D662CC573Q34120510-B10B0F3B-5C4A-4B9C-B3FE-C92DE06A9AEBQ34124298-39B2CC5B-27A2-46DB-B353-BDB826F90B0EQ34299491-D2648F4F-2E43-4309-A12A-5B766B10EEE8Q34455146-92CE667A-464C-48E0-889E-BCB0771AA6C1Q35105532-B9CF8DA9-F935-40C5-B18E-D0A57DB66BA4Q35179164-06BFB3F1-1E8B-4F04-B97F-ED7C44CF4D3EQ36023797-79FCF309-2881-40AF-8543-19913FF49ADCQ36059479-7B2B8FB6-4A16-4875-A4A9-56B0E4CBF3C4Q36538270-71AB06BD-02F7-4136-B3B6-C2354C2E01E9Q37002646-6C399580-81A4-4BF8-A32B-E4B3D090582FQ37075579-58DD3FA7-7376-49D7-AFB4-63CD0F1BA0AFQ37276365-DCFB78D9-79B8-47BD-906A-0AD15F3287D6Q37372747-FD925D17-EFB5-46AB-A88B-C3BC25A2EA30Q37624622-6C1DF466-9C5C-4970-AB0E-A1EDB76AEBB4Q37823829-428A5E4B-02E1-4D91-9ED4-E3348FFC5035Q41089360-8F26FE70-996B-45FE-9581-816A5A3EDF4EQ41769186-27803E22-669B-48DF-9DFB-64EB2138FE4EQ42049761-975504EC-2BF9-4AFA-9C03-C90CEC8BD296Q42844039-D8D46E27-1A37-4788-BDCE-8EC61CCDB143
P2860
description
1994 nî lūn-bûn
@nan
1994 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
name
The mobile flavin of 4-OH benzoate hydroxylase
@ast
The mobile flavin of 4-OH benzoate hydroxylase
@en
The mobile flavin of 4-OH benzoate hydroxylase
@nl
type
label
The mobile flavin of 4-OH benzoate hydroxylase
@ast
The mobile flavin of 4-OH benzoate hydroxylase
@en
The mobile flavin of 4-OH benzoate hydroxylase
@nl
prefLabel
The mobile flavin of 4-OH benzoate hydroxylase
@ast
The mobile flavin of 4-OH benzoate hydroxylase
@en
The mobile flavin of 4-OH benzoate hydroxylase
@nl
P2093
P356
P1433
P1476
The mobile flavin of 4-OH benzoate hydroxylase
@en
P2093
B A Palfey
D P Ballou
M L Ludwig
P356
10.1126/SCIENCE.7939628
P407
P577
1994-10-07T00:00:00Z