Kinetic and spectroscopic studies of the ATP:corrinoid adenosyltransferase PduO from Lactobacillus reuteri: substrate specificity and insights into the mechanism of Co(II)corrinoid reduction.
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Multiple roles of ATP:cob(I)alamin adenosyltransferases in the conversion of B12 to coenzyme B12Combined spectroscopic/computational studies of vitamin B12 precursors: geometric and electronic structures of cobinamidesResidue 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 † , ‡Structural 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 Trp93Characterization 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?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.Spectral and electronic properties of nitrosylcobalamin.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.Cofactor Editing by the G-protein Metallochaperone Domain Regulates the Radical B12 Enzyme IcmF.Canonical and ECF-type ATP-binding cassette importers in prokaryotes: diversity in modular organization and cellular functions.Spectroscopic Studies of the EutT Adenosyltransferase from Salmonella enterica: Evidence of a Tetrahedrally Coordinated Divalent Transition Metal Cofactor with Cysteine Ligation.Resonance Raman spectroscopic study of the interaction between Co(II)rrinoids and the ATP:corrinoid adenosyltransferase PduO from Lactobacillus reuteri.Spectroscopic and computational characterization of the base-off forms of cob(II)alamin.
P2860
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P2860
Kinetic and spectroscopic studies of the ATP:corrinoid adenosyltransferase PduO from Lactobacillus reuteri: substrate specificity and insights into the mechanism of Co(II)corrinoid reduction.
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
Kinetic and spectroscopic stud ...... of Co(II)corrinoid reduction.
@en
type
label
Kinetic and spectroscopic stud ...... of Co(II)corrinoid reduction.
@en
prefLabel
Kinetic and spectroscopic stud ...... of Co(II)corrinoid reduction.
@en
P2093
P2860
P356
P1433
P1476
Kinetic and spectroscopic stud ...... of Co(II)corrinoid reduction.
@en
P2093
Jorge C Escalante-Semerena
Kiyoung Park
Paola E Mera
P2860
P304
P356
10.1021/BI800419E
P407
P577
2008-08-02T00:00:00Z