Residue Phe112 of the Human-Type Corrinoid Adenosyltransferase (PduO) Enzyme of Lactobacillus reuteri Is Critical to the Formation of the Four-Coordinate Co(II) Corrinoid Substrate and to the Activity of the Enzyme † , ‡

Residue Phe112 of the Human-Type Corrinoid Adenosyltransferase (PduO) Enzyme of Lactobacillus reuteri Is Critical to the Formation of the Four-Coordinate Co(II) Corrinoid Substrate and to the Activity of the Enzyme † , ‡

Item
http://www.wikidata.org/entity/Q27653886
Multiple roles of ATP:cob(I)alamin adenosyltransferases in the conversion of B12 to coenzyme B12Structural Insights into the Mechanism of Four-Coordinate Cob(II)alamin Formation in the Active Site of the Salmonella enterica ATP:Co(I)rrinoid Adenosyltransferase Enzyme: Critical Role of Residues Phe91 and Trp93Dissecting cobamide diversity through structural and functional analyses of the base-activating CobT enzyme of Salmonella entericaThe Crystal Structure of the C-Terminal Domain of the Salmonella enterica PduO Protein: An Old Fold with a New Heme-Binding Mode.Characterization of the PduS cobalamin reductase of Salmonella enterica and its role in the Pdu microcompartmentDihydroflavin-driven adenosylation of 4-coordinate Co(II) corrinoids: are cobalamin reductases enzymes or electron transfer proteins?Characterisation of PduS, the pdu metabolosome corrin reductase, and evidence of substructural organisation within the bacterial microcompartment.Diverse bacterial microcompartment organellesSpectroscopic studies of the Salmonella enterica adenosyltransferase enzyme SeCobA: molecular-level insight into the mechanism of substrate Cob(II)alamin activation.Loss of allostery and coenzyme B12 delivery by a pathogenic mutation in adenosyltransferase.Spectroscopic Studies of the EutT Adenosyltransferase from Salmonella enterica: Mechanism of Four-Coordinate Co(II)Cbl Formation.the Eutt enzyme of Salmonella enterica is a unique ATP:Cob(I)alamin adenosyltransferase metalloprotein that requires ferrous ions for maximal activity.The tinker, tailor, soldier in intracellular B12 trafficking.Spectroscopic characterization of active-site variants of the PduO-type ATP:corrinoid adenosyltransferase from Lactobacillus reuteri: insights into the mechanism of four-coordinate Co(II)corrinoid formation.Cofactor Editing by the G-protein Metallochaperone Domain Regulates the Radical B12 Enzyme IcmF.Co+-H interaction inspired alternate coordination geometries of biologically important cob(I)alamin: possible structural and mechanistic consequences for methyltransferases.A New Class of EutT ATP:Co(I)rrinoid Adenosyltransferases Found in Listeria monocytogenes and Other Firmicutes Does Not Require a Metal Ion for Activity
P2860

Residue Phe112 of the Human-Type Corrinoid Adenosyltransferase (PduO) Enzyme of Lactobacillus reuteri Is Critical to the Formation of the Four-Coordinate Co(II) Corrinoid Substrate and to the Activity of the Enzyme † , ‡

Item
http://www.wikidata.org/entity/Q27653886
description
2009 nî lūn-bûn
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2009 թուականի Ապրիլին հրատարակուած գիտական յօդուած
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2009 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2009年の論文
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2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Residue Phe112 of the Human-Ty ...... e Activity of the Enzyme † , ‡
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Residue Phe112 of the Human-Ty ...... e Activity of the Enzyme † , ‡
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Residue Phe112 of the Human-Ty ...... e Activity of the Enzyme † , ‡
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type
label
Residue Phe112 of the Human-Ty ...... e Activity of the Enzyme † , ‡
@ast
Residue Phe112 of the Human-Ty ...... e Activity of the Enzyme † , ‡
@en
Residue Phe112 of the Human-Ty ...... e Activity of the Enzyme † , ‡
@nl
prefLabel
Residue Phe112 of the Human-Ty ...... e Activity of the Enzyme † , ‡
@ast
Residue Phe112 of the Human-Ty ...... e Activity of the Enzyme † , ‡
@en
Residue Phe112 of the Human-Ty ...... e Activity of the Enzyme † , ‡
@nl
P1433
P1476
P2093
P2860
P304
P31
P3181
P356
P407
P433
P478
P50
P577
P5875
P698
P932
P3181
P356
P1433
P1476
Residue Phe112 of the Human-Ty ...... e Activity of the Enzyme † , ‡
@en
P2093
P2860
P304
P31
P3181
P356
P407
P433
P478
P50
P577
P5875
P698
P932