9-Mercaptodethiobiotin is formed as a competent catalytic intermediate by Escherichia coli biotin synthase.
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Structures of lipoyl synthase reveal a compact active site for controlling sequential sulfur insertion reactionsStoichiometry of the redox neutral deamination and oxidative dehydrogenation reactions catalyzed by the radical SAM enzyme DesII.A radically different mechanism for S-adenosylmethionine-dependent methyltransferases.Adenosyl radical: reagent and catalyst in enzyme reactions.Biotin and Lipoic Acid: Synthesis, Attachment, and Regulation.The biosynthesis of thiol- and thioether-containing cofactors and secondary metabolites catalyzed by radical S-adenosylmethionine enzymes.S K-edge XAS and DFT calculations on SAM dependent pyruvate formate-lyase activating enzyme: nature of interaction between the Fe4S4 cluster and SAM and its role in reactivity.Radical SAM enzymes in the biosynthesis of sugar-containing natural products.Anaerobic functionalization of unactivated C-H bonds.Characterization and mechanistic studies of DesII: a radical S-adenosyl-L-methionine enzyme involved in the biosynthesis of TDP-D-desosamine.Radical S-adenosylmethionine enzymes.Structural insights into radical generation by the radical SAM superfamily.Radical S-adenosylmethionine enzymes: mechanism, control and function.Involvement of SgvP in carbon-sulfur bond formation during Griseoviridin biosynthesis.Density functional theory calculations on the active site of biotin synthase: mechanism of S transfer from the Fe(2)S(2) cluster and the role of 1st and 2nd sphere residues.Reduction of the [2Fe-2S] cluster accompanies formation of the intermediate 9-mercaptodethiobiotin in Escherichia coli biotin synthase.A complex between biotin synthase and the iron-sulfur cluster assembly chaperone HscA that enhances in vivo cluster assembly.9-Mercaptodethiobiotin is generated as a ligand to the [2Fe-2S]+ cluster during the reaction catalyzed by biotin synthase from Escherichia coli.Catalytic activity of the anaerobic tyrosine lyase required for thiamine biosynthesis in Escherichia coli.A combined computational and experimental investigation of the [2Fe-2S] cluster in biotin synthase.
P2860
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P2860
9-Mercaptodethiobiotin is formed as a competent catalytic intermediate by Escherichia coli biotin synthase.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
@zh-cn
name
9-Mercaptodethiobiotin is form ...... herichia coli biotin synthase.
@en
9-Mercaptodethiobiotin is form ...... herichia coli biotin synthase.
@nl
type
label
9-Mercaptodethiobiotin is form ...... herichia coli biotin synthase.
@en
9-Mercaptodethiobiotin is form ...... herichia coli biotin synthase.
@nl
prefLabel
9-Mercaptodethiobiotin is form ...... herichia coli biotin synthase.
@en
9-Mercaptodethiobiotin is form ...... herichia coli biotin synthase.
@nl
P2093
P2860
P356
P1433
P1476
9-Mercaptodethiobiotin is form ...... herichia coli biotin synthase.
@en
P2093
Andrew M Taylor
Christine E Farrar
Joseph T Jarrett
P2860
P304
P356
10.1021/BI801035B
P407
P577
2008-08-09T00:00:00Z