Structure of the proline dehydrogenase domain of the multifunctional PutA flavoprotein
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Functional consequences of PRODH missense mutationsSingle-gene disorders: what role could moonlighting enzymes play?Redox-Induced Changes in Flavin Structure and Roles of Flavin N(5) and the Ribityl 2‘-OH Group in Regulating PutA−Membrane Binding † , ‡Structure and Kinetics of Monofunctional Proline Dehydrogenase from Thermus thermophilusStructure of glycerol-3-phosphate dehydrogenase, an essential monotopic membrane enzyme involved in respiration and metabolism.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 PutAA Conserved Active Site Tyrosine Residue of Proline Dehydrogenase Helps Enforce the Preference for Proline over Hydroxyproline as the Substrate † ‡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 japonicumCrystal Structures and Kinetics of Monofunctional Proline Dehydrogenase Provide Insight into Substrate Recognition and Conformational Changes Associated with Flavin Reduction and Product ReleaseInvolvement of the β3-α3 Loop of the Proline Dehydrogenase Domain in Allosteric Regulation of Membrane Association of Proline Utilization AStructures of the PutA peripheral membrane flavoenzyme reveal a dynamic substrate-channeling tunnel and the quinone-binding siteCharacterization of the proline-utilization pathway in Mycobacterium tuberculosis through structural and functional studiesPurification and characterization of Put1p from Saccharomyces cerevisiae.Structures of the Escherichia coli PutA proline dehydrogenase domain in complex with competitive inhibitorsIdentification of a Conserved Histidine as Critical for the Catalytic Mechanism and Functional Switching of the Multifunctional Proline Utilization A Protein.Comparative analysis of protein structure alignmentsFlavin redox switching of protein functionsMechanistic aspects and redox properties of hyperthermophilic L-proline dehydrogenase from Pyrococcus furiosus related to dimethylglycine dehydrogenase/oxidase.SlgA, encoded by the homolog of the human schizophrenia-associated gene PRODH, acts in clock neurons to regulate Drosophila aggressionCharacterization of a bifunctional PutA homologue from Bradyrhizobium japonicum and identification of an active site residue that modulates proline reduction of the flavin adenine dinucleotide cofactor.Identification and characterization of the DNA-binding domain of the multifunctional PutA flavoenzymeRegulation of PutA-membrane associations by flavin adenine dinucleotide reductionFirst evidence for substrate channeling between proline catabolic enzymes: a validation of domain fusion analysis for predicting protein-protein interactions.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.Cloning, purification and crystallization of Thermus thermophilus proline dehydrogenase.Role of apoptosis-inducing factor, proline dehydrogenase, and NADPH oxidase in apoptosis and oxidative stressCrystal structures of the DNA-binding domain of Escherichia coli proline utilization A flavoprotein and analysis of the role of Lys9 in DNA recognition.Three crystal forms of the bifunctional enzyme proline utilization A (PutA) from Bradyrhizobium japonicum.Expression, Purification and Characterization of the Proline Dehydrogenase Domain of PutA from Pseudomonas putida POS-F84Unique structural features and sequence motifs of proline utilization A (PutA).Proline dehydrogenase regulates redox state and respiratory metabolism in Trypanosoma cruziDetection of L-lactate in polyethylene glycol solutions confirms the identity of the active-site ligand in a proline dehydrogenase structure.Direct linking of metabolism and gene expression in the proline utilization A protein from Escherichia coli.Structural biology of proline catabolism
P2860
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P2860
Structure of the proline dehydrogenase domain of the multifunctional PutA flavoprotein
description
2003 nî lūn-bûn
@nan
2003 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Structure of the proline dehydrogenase domain of the multifunctional PutA flavoprotein
@ast
Structure of the proline dehydrogenase domain of the multifunctional PutA flavoprotein
@en
Structure of the proline dehydrogenase domain of the multifunctional PutA flavoprotein
@nl
type
label
Structure of the proline dehydrogenase domain of the multifunctional PutA flavoprotein
@ast
Structure of the proline dehydrogenase domain of the multifunctional PutA flavoprotein
@en
Structure of the proline dehydrogenase domain of the multifunctional PutA flavoprotein
@nl
prefLabel
Structure of the proline dehydrogenase domain of the multifunctional PutA flavoprotein
@ast
Structure of the proline dehydrogenase domain of the multifunctional PutA flavoprotein
@en
Structure of the proline dehydrogenase domain of the multifunctional PutA flavoprotein
@nl
P2093
P2860
P356
P1476
Structure of the proline dehydrogenase domain of the multifunctional PutA flavoprotein
@en
P2093
Donald F Becker
John J Tanner
Shorena Nadaraia
Yong-Hwan Lee
P2860
P304
P356
10.1038/NSB885
P577
2003-02-01T00:00:00Z