Redox-Induced Changes in Flavin Structure and Roles of Flavin N(5) and the Ribityl 2‘-OH Group in Regulating PutA−Membrane Binding † , ‡ - Wikidata - awgldk - TriplyDB

Redox-Induced Changes in Flavin Structure and Roles of Flavin N(5) and the Ribityl 2‘-OH Group in Regulating PutA−Membrane Binding † , ‡

Redox-Induced Changes in Flavin Structure and Roles of Flavin N(5) and the Ribityl 2‘-OH Group in Regulating PutA−Membrane Binding † , ‡

http://www.wikidata.org/entity/Q27641075

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Structure and Kinetics of Monofunctional Proline Dehydrogenase from Thermus thermophilus Structural Basis for the Inactivation of Thermus thermophilus Proline Dehydrogenase by N- Propargylglycine † , ‡Structural Basis of the Transcriptional Regulation of the Proline Utilization Regulon by Multifunctional PutA Solution structure of the Pseudomonas putida protein PpPutA45 and its DNA complex The Structure of the Proline Utilization A Proline Dehydrogenase Domain Inactivated by N -Propargylglycine Provides Insight into Conformational Changes Induced by Substrate Binding and Flavin Reduction ,Crystal structure of the bifunctional proline utilization A flavoenzyme from Bradyrhizobium japonicum Crystal Structures and Kinetics of Monofunctional Proline Dehydrogenase Provide Insight into Substrate Recognition and Conformational Changes Associated with Flavin Reduction and Product Release Involvement of the β3-α3 Loop of the Proline Dehydrogenase Domain in Allosteric Regulation of Membrane Association of Proline Utilization A Structures of the PutA peripheral membrane flavoenzyme reveal a dynamic substrate-channeling tunnel and the quinone-binding site Identification of a Conserved Histidine as Critical for the Catalytic Mechanism and Functional Switching of the Multifunctional Proline Utilization A Protein.Flavin redox switching of protein functions Insights into membrane association of Klebsiella pneumoniae NifL under nitrogen-fixing conditions from mutational analysis.Evidence that the C-terminal domain of a type B PutA protein contributes to aldehyde dehydrogenase activity and substrate channeling.Thiol/Disulfide redox switches in the regulation of heme binding to proteins.Steady-state kinetic mechanism of the proline:ubiquinone oxidoreductase activity of proline utilization A (PutA) from Escherichia coli Small-angle X-ray scattering studies of the oligomeric state and quaternary structure of the trifunctional proline utilization A (PutA) flavoprotein from Escherichia coli Rapid reaction kinetics of proline dehydrogenase in the multifunctional proline utilization A protein.Substrate channeling in proline metabolism.Three crystal forms of the bifunctional enzyme proline utilization A (PutA) from Bradyrhizobium japonicum.Unique structural features and sequence motifs of proline utilization A (PutA).Direct linking of metabolism and gene expression in the proline utilization A protein from Escherichia coli.Structural biology of proline catabolism The structural origin of metabolic quantitative diversity.Evidence for hysteretic substrate channeling in the proline dehydrogenase and Δ1-pyrroline-5-carboxylate dehydrogenase coupled reaction of proline utilization A (PutA).Engineering a trifunctional proline utilization A chimaera by fusing a DNA-binding domain to a bifunctional PutA.Multiple functionalities of reduced flavin in the non-redox reaction catalyzed by UDP-galactopyranose mutase.Structure, function, and mechanism of proline utilization A (PutA).Redox-dependent substrate-cofactor interactions in the Michaelis-complex of a flavin-dependent oxidoreductase.Discovery of the Membrane Binding Domain in Trifunctional Proline Utilization A.The Proline Cycle As a Potential Cancer Therapy Target.

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P2860

Redox-Induced Changes in Flavin Structure and Roles of Flavin N(5) and the Ribityl 2‘-OH Group in Regulating PutA−Membrane Binding † , ‡

http://www.wikidata.org/entity/Q27641075

description

2007 nî lūn-bûn

@nan

2007 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2007 թվականի հունվարին հրատարակված գիտական հոդված

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2007年の論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年论文

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name

Redox-Induced Changes in Flavi ...... ng PutA−Membrane Binding † , ‡

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Redox-Induced Changes in Flavi ...... ng PutA−Membrane Binding † , ‡

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Redox-Induced Changes in Flavi ...... ng PutA−Membrane Binding † , ‡

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Redox-Induced Changes in Flavi ...... ng PutA−Membrane Binding † , ‡

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Redox-Induced Changes in Flavi ...... ng PutA−Membrane Binding † , ‡

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Redox-Induced Changes in Flavi ...... ng PutA−Membrane Binding † , ‡

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Redox-induced changes in flavi ...... ulating PutA--membrane binding

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Redox-Induced Changes in Flavi ...... ng PutA−Membrane Binding † , ‡

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Redox-Induced Changes in Flavi ...... ng PutA−Membrane Binding † , ‡

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Redox-Induced Changes in Flavi ...... ng PutA−Membrane Binding † , ‡

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Redox-Induced Changes in Flavi ...... ng PutA−Membrane Binding † , ‡

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P2093

Donald F Becker

http://www.w3.org/2001/XMLSchema#string

Dustin Rewinkel

http://www.w3.org/2001/XMLSchema#string

John J Tanner

http://www.w3.org/2001/XMLSchema#string

Min Zhang

http://www.w3.org/2001/XMLSchema#string

Srimevan Wanduragala

http://www.w3.org/2001/XMLSchema#string

Weidong Zhu

http://www.w3.org/2001/XMLSchema#string

Weimin Zhang

http://www.w3.org/2001/XMLSchema#string

Yuzhen Zhou

http://www.w3.org/2001/XMLSchema#string

P2860

Crystal structures of medium-chain acyl-CoA dehydrogenase from pig liver mitochondria with and without substrate

Three-dimensional structure of human electron transfer flavoprotein to 2.1-A resolution

Improved methods for building protein models in electron density maps and the location of errors in these models

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Crystal structure of reduced thioredoxin reductase from Escherichia coli: Structural flexibility in the isoalloxazine ring of the flavin adenine dinucleotide cofactor

Structure of the proline dehydrogenase domain of the multifunctional PutA flavoprotein

Refined crystal structure of lipoamide dehydrogenase from Azotobacter vinelandii at 2.2 A resolution. A comparison with the structure of glutathione reductase

Substrate binding and catalysis by glutathione reductase as derived from refined enzyme: substrate crystal structures at 2 A resolution

Use of TLS parameters to model anisotropic displacements in macromolecular refinement

Structures of the Escherichia coli PutA proline dehydrogenase domain in complex with competitive inhibitors

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483-91

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scholarly article

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4069939

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10.1021/BI061935G

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2

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46

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2007-01-16T00:00:00Z

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6590919

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17209558

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2527739

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