Dihydroflavin-driven adenosylation of 4-coordinate Co(II) corrinoids: are cobalamin reductases enzymes or electron transfer proteins?
about
Multiple roles of ATP:cob(I)alamin adenosyltransferases in the conversion of B12 to coenzyme B12Navigating the B(12) road: assimilation, delivery, and disorders of cobalaminThe human flavoproteomeSmall but powerful, the primary endosymbiont of moss bugs, Candidatus Evansia muelleri, holds a reduced genome with large biosynthetic capabilitiesGenetic disorders of vitamin B12 metabolism: eight complementation groups – eight genesThe 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 microcompartmentCharacterisation of PduS, the pdu metabolosome corrin reductase, and evidence of substructural organisation within the bacterial microcompartment.Loss of allostery and coenzyme B12 delivery by a pathogenic mutation in adenosyltransferase.Unprecedented Mechanism Employed by the Salmonella enterica EutT ATP:Co(I)rrinoid Adenosyltransferase Precludes Adenosylation of Incomplete Co(II)rrinoids.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.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.Resonance Raman spectroscopic study of the interaction between Co(II)rrinoids and the ATP:corrinoid adenosyltransferase PduO from Lactobacillus reuteri.FAD binding, cobinamide binding and active site communication in the corrin reductase (CobR)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
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P2860
Dihydroflavin-driven adenosylation of 4-coordinate Co(II) corrinoids: are cobalamin reductases enzymes or electron transfer proteins?
description
2009 nî lūn-bûn
@nan
2009 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
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
Dihydroflavin-driven adenosyla ...... or electron transfer proteins?
@ast
Dihydroflavin-driven adenosyla ...... or electron transfer proteins?
@en
type
label
Dihydroflavin-driven adenosyla ...... or electron transfer proteins?
@ast
Dihydroflavin-driven adenosyla ...... or electron transfer proteins?
@en
prefLabel
Dihydroflavin-driven adenosyla ...... or electron transfer proteins?
@ast
Dihydroflavin-driven adenosyla ...... or electron transfer proteins?
@en
P2860
P356
P1476
Dihydroflavin-driven adenosyla ...... or electron transfer proteins?
@en
P2093
Jorge C Escalante-Semerena
Paola E Mera
P2860
P304
P356
10.1074/JBC.M109.059485
P407
P577
2009-11-21T00:00:00Z