Evidence for hysteretic substrate channeling in the proline dehydrogenase and Δ1-pyrroline-5-carboxylate dehydrogenase coupled reaction of proline utilization A (PutA). (Q37563541)

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scientific article published on 18 December 2013

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English	Evidence for hysteretic substrate channeling in the proline dehydrogenase and Δ1-pyrroline-5-carboxylate dehydrogenase coupled reaction of proline utilization A (PutA).	scientific article published on 18 December 2013

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scholarly article

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Europe PubMed Central

PMC publication ID

21 August 2017

Evidence for hysteretic substrate channeling in the proline dehydrogenase and Δ1-pyrroline-5-carboxylate dehydrogenase coupled reaction of proline utilization A (PutA). (English)

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21 August 2017

4

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:24352662%20AND%20SRC:MED&resulttype=core&format=json

11 June 2020

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Michael A Moxley

1

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11 June 2020

Nikhilesh Sanyal

2

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11 June 2020

Navasona Krishnan

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11 June 2020

Donald F Becker

5

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11 June 2020

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18 December 2013

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21 August 2017

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13

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Journal of Biological Chemistry

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11 June 2020

289

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11 June 2020

6

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11 June 2020

3639-3651

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11 June 2020

Involvement of the β3-α3 Loop of the Proline Dehydrogenase Domain in Allosteric Regulation of Membrane Association of Proline Utilization A

1 reference

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Proline mechanisms of stress survival

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Dimerization and bifunctionality confer robustness to the isocitrate dehydrogenase regulatory system in Escherichia coli

1 reference

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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 Release

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1 reference

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Steady-state kinetic mechanism of the proline:ubiquinone oxidoreductase activity of proline utilization A (PutA) from Escherichia coli

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Flavin redox switching of protein functions

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Proline metabolism and microenvironmental stress

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Crystal structure of the bifunctional proline utilization A flavoenzyme from Bradyrhizobium japonicum

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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 ,

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

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Structure of the proline dehydrogenase domain of the multifunctional PutA flavoprotein

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11 June 2020

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