Crystal structure of the bifunctional proline utilization A flavoenzyme from Bradyrhizobium japonicum
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Crystal Structures and Kinetics of Monofunctional Proline Dehydrogenase Provide Insight into Substrate Recognition and Conformational Changes Associated with Flavin Reduction and Product ReleaseStructural basis for hypermodification of the wobble uridine in tRNA by bifunctional enzyme MnmCStructural Determinants of Oligomerization of Δ1-Pyrroline-5-Carboxylate Dehydrogenase: Identification of a Hexamerization Hot SpotStructures of the PutA peripheral membrane flavoenzyme reveal a dynamic substrate-channeling tunnel and the quinone-binding siteKinetic and Structural Characterization of Tunnel-Perturbing Mutants in Bradyrhizobium japonicum Proline Utilization ACharacterization of the proline-utilization pathway in Mycobacterium tuberculosis through structural and functional studiesStructures of Proline Utilization A Reveal the Fold and Functions of the Aldehyde Dehydrogenase Superfamily Domain of Unknown FunctionProline utilization by Bacillus subtilis: uptake and catabolismIdentification and characterization of D-hydroxyproline dehydrogenase and Delta1-pyrroline-4-hydroxy-2-carboxylate deaminase involved in novel L-hydroxyproline metabolism of bacteria: metabolic convergent evolutionProline dehydrogenase 2 (PRODH2) is a hydroxyproline dehydrogenase (HYPDH) and molecular target for treating primary hyperoxaluriaIdentification 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 functionsEvidence that the C-terminal domain of a type B PutA protein contributes to aldehyde dehydrogenase activity and substrate channeling.Proline metabolism increases katG expression and oxidative stress resistance in Escherichia coli.First evidence for substrate channeling between proline catabolic enzymes: a validation of domain fusion analysis for predicting protein-protein interactions.Role of Δ1-pyrroline-5-carboxylate dehydrogenase supports mitochondrial metabolism and host-cell invasion of Trypanosoma cruzi.Steady-state kinetic mechanism of the proline:ubiquinone oxidoreductase activity of proline utilization A (PutA) from Escherichia coliSmall-angle X-ray scattering studies of the oligomeric state and quaternary structure of the trifunctional proline utilization A (PutA) flavoprotein from Escherichia coliProline metabolism and its implications for plant-environment interaction.Rapid reaction kinetics of proline dehydrogenase in the multifunctional proline utilization A protein.Substrate channeling in proline metabolism.Does metabolite channeling accelerate enzyme-catalyzed cascade reactions?Unique structural features and sequence motifs of proline utilization A (PutA).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.L-proline dehydrogenases in hyperthermophilic archaea: distribution, function, structure, and application.Biophysical investigation of type A PutAs reveals a conserved core oligomeric structure.Empirical power laws for the radii of gyration of protein oligomers.Structure, function, and mechanism of proline utilization A (PutA).Molecular cloning and expression analysis of the gene encoding proline dehydrogenase from Jatropha curcas L.Proline dehydrogenase from Thermus thermophilus does not discriminate between FAD and FMN as cofactor.StyA1 and StyA2B from Rhodococcus opacus 1CP: a multifunctional styrene monooxygenase systemStructural Basis for the Substrate Inhibition of Proline Utilization A by Proline.Discovery of the Membrane Binding Domain in Trifunctional Proline Utilization A.Functional Impact of the N-terminal Arm of Proline Dehydrogenase from Thermus thermophilus.Determination of Protein Oligomeric Structure from Small-Angle X-ray Scattering.Tying the knot: occurrence and possible significance of gene fusions in plant metabolism and beyond.Structure and characterization of a class 3B proline utilization A: Ligand-induced dimerization and importance of the C-terminal domain for catalysis.The Proline Cycle As a Potential Cancer Therapy Target.High yields of active Thermus thermophilus proline dehydrogenase are obtained using maltose-binding protein as a solubility tag.
P2860
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P2860
Crystal structure of the bifunctional proline utilization A flavoenzyme from Bradyrhizobium japonicum
description
2010 nî lūn-bûn
@nan
2010 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Crystal structure of the bifun ...... from Bradyrhizobium japonicum
@ast
Crystal structure of the bifun ...... from Bradyrhizobium japonicum
@en
Crystal structure of the bifun ...... from Bradyrhizobium japonicum
@nl
type
label
Crystal structure of the bifun ...... from Bradyrhizobium japonicum
@ast
Crystal structure of the bifun ...... from Bradyrhizobium japonicum
@en
Crystal structure of the bifun ...... from Bradyrhizobium japonicum
@nl
prefLabel
Crystal structure of the bifun ...... from Bradyrhizobium japonicum
@ast
Crystal structure of the bifun ...... from Bradyrhizobium japonicum
@en
Crystal structure of the bifun ...... from Bradyrhizobium japonicum
@nl
P2093
P2860
P356
P1476
Crystal structure of the bifun ...... from Bradyrhizobium japonicum
@en
P2093
Dhiraj Srivastava
Donald F Becker
Greg L Hura
John J Tanner
Jonathan P Schuermann
Michael T Henzl
Navasona Krishnan
Nikhilesh Sanyal
Tommi A White
P2860
P304
P356
10.1073/PNAS.0906101107
P407
P577
2010-02-16T00:00:00Z