Stabilization of C4a-hydroperoxyflavin in a two-component flavin-dependent monooxygenase is achieved through interactions at flavin N5 and C4a atoms.
about
Structure of DnmZ, a nitrososynthase in the Streptomyces peucetius anthracycline biosynthetic pathway.The 1.6 Å Crystal Structure of Pyranose Dehydrogenase from Agaricus meleagris Rationalizes Substrate Specificity and Reveals a Flavin IntermediateFlavin-mediated dual oxidation controls an enzymatic Favorskii-type rearrangementRationally engineered flavin-dependent oxidase reveals steric control of dioxygen reductionHow pH Modulates the Reactivity and Selectivity of a Siderophore-Associated Flavin MonooxygenaseCrystallization and preliminary X-ray analysis of the reductase component of p-hydroxyphenylacetate 3-hydroxylase from Acinetobacter baumannii.The reaction kinetics of 3-hydroxybenzoate 6-hydroxylase from Rhodococcus jostii RHA1 provide an understanding of the para-hydroxylation enzyme catalytic cycle.Crystal structures of TdsC, a dibenzothiophene monooxygenase from the thermophile Paenibacillus sp. A11-2, reveal potential for expanding its substrate selectivity.Kinetic Mechanism of the Dechlorinating Flavin-dependent Monooxygenase HadA.Kinetic mechanism of L-α-glycerophosphate oxidase from Mycoplasma pneumoniae.Interactions with the substrate phenolic group are essential for hydroxylation by the oxygenase component of p-hydroxyphenylacetate 3-hydroxylase.Flavin-Dependent Redox Transfers by the Two-Component Diketocamphane Monooxygenases of Camphor-Grown Pseudomonas putida NCIMB 10007.Oxidation mode of pyranose 2-oxidase is controlled by pH.FAD C(4a)-hydroxide stabilized in a naturally fused styrene monooxygenase.The C-terminal domain of 4-hydroxyphenylacetate 3-hydroxylase from Acinetobacter baumannii is an autoinhibitory domain.Initial investigations of C4a-(hydro)peroxyflavin intermediate formation by dibenzothiophene monooxygenase.Inactivation mechanism of N61S mutant of human FMO3 towards trimethylamine.Two-Component FAD-Dependent Monooxygenases: Current Knowledge and Biotechnological Opportunities
P2860
Q27317024-B627B74E-51CB-42E7-BAA2-C105BF528B75Q27675932-B238D1CE-F10D-4577-97D7-AA006D7D9F35Q27680465-8F22FBB7-8A80-4E39-AA43-19FAC7A9CDC2Q27697651-97D7FA97-A61B-4A6F-90A1-7FF2DB26AE48Q28468160-4AEAD52F-391B-4070-99A2-70A091263D0DQ36019261-FE53C8B3-3F7A-4D70-96B8-7FF9B288040AQ37368655-76402FF9-0A1F-414E-AD1C-D03EEAB27524Q38647925-C7327E6B-4E26-468F-B2F3-D7BA1B76A6A4Q38761766-1526D20D-6C93-4E23-B3E3-6B8F3155441DQ39035702-CDAE8C07-E954-4C17-A455-9EF8B4173A7BQ40042462-FB2992AE-C760-46A9-8D32-9C784DC85ED9Q40048504-7CEE2457-EB82-46BC-A8FC-8F1DE1A000CAQ41052298-75630893-85FB-4E71-A5A7-D36D7AC34EE8Q42082251-04A580D4-C2FC-4361-9C65-004486F4568FQ42252645-344A508D-FEEA-4C42-86BB-780D4E384CD8Q46304816-AC98F203-E187-4077-9436-40FA177B4CC6Q47107145-0303F6B6-1063-4508-8555-B616525C8E07Q58802616-46931BF7-C0AF-4E0A-8250-7E9CE0A49847
P2860
Stabilization of C4a-hydroperoxyflavin in a two-component flavin-dependent monooxygenase is achieved through interactions at flavin N5 and C4a atoms.
description
2011 nî lūn-bûn
@nan
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
2011年论文
@zh
2011年论文
@zh-cn
name
Stabilization of C4a-hydropero ...... ns at flavin N5 and C4a atoms.
@en
Stabilization of C4a-hydropero ...... ns at flavin N5 and C4a atoms.
@nl
type
label
Stabilization of C4a-hydropero ...... ns at flavin N5 and C4a atoms.
@en
Stabilization of C4a-hydropero ...... ns at flavin N5 and C4a atoms.
@nl
prefLabel
Stabilization of C4a-hydropero ...... ns at flavin N5 and C4a atoms.
@en
Stabilization of C4a-hydropero ...... ns at flavin N5 and C4a atoms.
@nl
P2093
P2860
P356
P1476
Stabilization of C4a-hydropero ...... ns at flavin N5 and C4a atoms.
@en
P2093
Jeerus Sucharitakul
Kittisak Thotsaporn
Pirom Chenprakhon
P2860
P304
28170-28180
P356
10.1074/JBC.M111.241836
P407
P577
2011-06-16T00:00:00Z