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

Biochemistry ◽  
2013 ◽  
Vol 52 (26) ◽  
pp. 4482-4491 ◽  
Author(s):  
Weidong Zhu ◽  
Ashley M. Haile ◽  
Ranjan K. Singh ◽  
John D. Larson ◽  
Danielle Smithen ◽  
...  
Keyword(s):  
Allosteric Regulation ◽  
Membrane Association ◽  
Proline Dehydrogenase ◽  
Proline Utilization ◽  
Proline Utilization A

scholarly journals Structural and functional studies of proline catabolic enzymes and human aldehyde dehydrogenases

2015 ◽  
Author(s):  
◽  
Min Luo
Keyword(s):  
Hot Spot ◽  
Gram Negative Bacteria ◽  
Proline Dehydrogenase ◽  
Aldehyde Dehydrogenases ◽  
Functional Studies ◽  
Gram Positive Bacteria ◽  
Catabolic Enzymes ◽  
Proline Catabolism ◽  
Proline Utilization ◽  
Proline Utilization A

Oxidation of amino acids, like proline catabolism, is a central part of energy metabolism. Proline is oxidized to glutamate by two enzymes: proline dehydrogenase (PRODH) and 1-pyrroline-5-carboxylate dehydrogenase (P5CDH). PRODH catalyzes the first reaction of proline to 1-pyrroline-5-carboxylate (P5C). P5C undergoes a non-enzymatic hydrolysis to glutamate semialdehyde (GSA), which is oxidized to glutamate by a NAD+- dependent enzyme P5CDH. PRODH and P5CDH are mono-functional enzymes in eukaryotes and Gram-positive bacteria; while in Gram-negative bacteria, the two enzymes are fused into one protein as two domains, known as proline utilization A (PutA). This dissertation work involved structural and functional studies of PRODH, P5CDH, PutA, and human aldehyde dehydrogenases (ALDHs). The results illuminated the substrate recognition for mono-functional PRODH and hot spot oligomerization mechanism for mono-functional P5CDH, also, demonstrated that diethylaminobenzaldehyde (DEAB) is a mechanism based inactivator for aldehyde dehydrogenase 7A1. Furthermore, the C-terminal domain found in PutAs, the only domain without any structural and functional information has been structurally and biochemically characterized.

scholarly journals Kinetic and Structural Characterization of Tunnel-Perturbing Mutants in Bradyrhizobium japonicum Proline Utilization A

Biochemistry ◽  
2014 ◽  
Vol 53 (31) ◽  
pp. 5150-5161 ◽  
Author(s):  
Benjamin W. Arentson ◽  
Min Luo ◽  
Travis A. Pemberton ◽  
John J. Tanner ◽  
Donald F. Becker
Keyword(s):  
Structural Characterization ◽  
Bradyrhizobium Japonicum ◽  
Proline Utilization ◽  
Proline Utilization A

scholarly journals Structures of Proline Utilization A (PutA) Reveal the Fold and Functions of the Aldehyde Dehydrogenase Superfamily Domain of Unknown Function

2016 ◽  
Vol 291 (46) ◽  
pp. 24065-24075 ◽  
Author(s):  
Min Luo ◽  
Thameesha T. Gamage ◽  
Benjamin W. Arentson ◽  
Katherine N. Schlasner ◽  
Donald F. Becker ◽  
...  
Keyword(s):  
Aldehyde Dehydrogenase ◽  
Unknown Function ◽  
Aldehyde Dehydrogenase Superfamily ◽  
Proline Utilization ◽  
Domain Of Unknown Function ◽  
Proline Utilization A

scholarly journals Three crystal forms of the bifunctional enzyme proline utilization A (PutA) fromBradyrhizobium japonicum

2008 ◽  
Vol 64 (10) ◽  
pp. 949-953 ◽  
Author(s):  
Jonathan P. Schuermann ◽  
Tommi A. White ◽  
Dhiraj Srivastava ◽  
Dale B. Karr ◽  
John J. Tanner
Keyword(s):  
Bifunctional Enzyme ◽  
Crystal Forms ◽  
Proline Utilization ◽  
Proline Utilization A
Sign in / Sign up

Export Citation Format

Share Document