Enzymatic properties of the purified putA protein from Salmonella typhimurium.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference12 articles.
1. Purification of the putA gene product. A bifunctional membrane-bound protein from Salmonella typhimurium responsible for the two-step oxidation of proline to glutamate.
2. Membrane-bound proline dehydrogenase from Escherichia coli. Solubilization, purification, and characterization.
3. Regulation of Proline Degradation in Salmonella typhimurium
4. The Interconversion of Glutamic Acid and Proline
5. Glutamic γ-Semialdehyde and Δ1-Pyrroline-5-carboxylic Acid, Intermediates in the Biosynthesis of Proline1,2
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1. Identification of a Conserved Histidine As Being Critical for the Catalytic Mechanism and Functional Switching of the Multifunctional Proline Utilization A Protein;Biochemistry;2017-06-08
2. Ehrlichia chaffeensis Proliferation Begins with NtrY/NtrX and PutA/GlnA Upregulation and CtrA Degradation Induced by Proline and Glutamine Uptake;mBio;2014-12-31
3. Involvement of the β3-α3 Loop of the Proline Dehydrogenase Domain in Allosteric Regulation of Membrane Association of Proline Utilization A;Biochemistry;2013-06-19
4. Proline dehydrogenase from Pseudomonas fluorescens: Gene cloning, purification, characterization and homology modeling;Applied Biochemistry and Microbiology;2012-02-29
5. Rapid Reaction Kinetics of Proline Dehydrogenase in the Multifunctional Proline Utilization A Protein;Biochemistry;2011-12-15
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