Probing a hydrogen bond pair and the FAD redox properties in the proline dehydrogenase domain of Escherichia coli PutA.
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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 † , ‡Involvement of the β3-α3 Loop of the Proline Dehydrogenase Domain in Allosteric Regulation of Membrane Association of Proline Utilization AStructures of the Escherichia coli PutA proline dehydrogenase domain in complex with competitive inhibitorsSources of superoxide/H2O2 during mitochondrial proline oxidationCloning, purification and crystallization of Thermus thermophilus proline dehydrogenase.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).Structural biology of proline catabolismHydrogen isotopes in individual amino acids reflect differentiated pools of hydrogen from food and water in Escherichia coliThe metabolism of proline as microenvironmental stress substrate.Screening and characterization of proline dehydrogenase flavoenzyme producing Pseudomonas entomophila
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P2860
Probing a hydrogen bond pair and the FAD redox properties in the proline dehydrogenase domain of Escherichia coli PutA.
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name
Probing a hydrogen bond pair a ...... main of Escherichia coli PutA.
@en
Probing a hydrogen bond pair a ...... main of Escherichia coli PutA.
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type
label
Probing a hydrogen bond pair a ...... main of Escherichia coli PutA.
@en
Probing a hydrogen bond pair a ...... main of Escherichia coli PutA.
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prefLabel
Probing a hydrogen bond pair a ...... main of Escherichia coli PutA.
@en
Probing a hydrogen bond pair a ...... main of Escherichia coli PutA.
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P2093
P1476
Probing a hydrogen bond pair a ...... main of Escherichia coli PutA.
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P2093
Berevan A Baban
Donald F Becker
John J Tanner
Madhavan P Vinod
P356
10.1016/J.BBAPAP.2004.06.001
P577
2004-09-01T00:00:00Z