scholarly journals Faculty Opinions recommendation of Crystal structure of the bifunctional proline utilization A flavoenzyme from Bradyrhizobium japonicum.

2010 ◽  
Author(s):  
Andrea Mattevi
Keyword(s):  
Crystal Structure ◽  
Bradyrhizobium Japonicum ◽  
Proline Utilization ◽  
Proline Utilization A

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

2010 ◽  
Vol 107 (7) ◽  
pp. 2878-2883 ◽  
Author(s):  
D. Srivastava ◽  
J. P. Schuermann ◽  
T. A. White ◽  
N. Krishnan ◽  
N. Sanyal ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Bradyrhizobium Japonicum ◽  
Proline Utilization ◽  
Proline Utilization A

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

A STUDY ON KINETIC CHARACTERIZATION OF CHANNEL-BLOCKING MUTANTS IN BRADYRHIZOBIUM JAPONICUM UTILIZATION A

2021 ◽  
pp. 49-52
Author(s):  
Anand Shanker Singh ◽  
G. Radhika ◽  
R. Praveen Kumar ◽  
Debarshi Jana
Keyword(s):  
Active Site ◽  
Bradyrhizobium Japonicum ◽  
Kinetic Data ◽  
Active Sites ◽  
Substrate Channeling ◽  
Site Analysis ◽  
Proline Utilization ◽  
Channel Blocking ◽  
Proline Utilization A

Proline utilization A (PutA) from Bradyrhizobium japonicum (BjPutA) is a bifunctional avoenzyme that catalyzes the oxidation of proline to glutamate using fused proline dehydrogenase (PRODH) and ∆1-pyrroline-5-carboxylate dehydrogenase (P5CDH) domains. Recent crystal structures and kinetic data suggest an intramolecular channel connects the two active sites, promoting substrate channeling of the intermediate P5C from the PRODH domain to the P5CDH domain. In this work several mutations were made along the channel in an effort to block passage of P5C to the second active site. Analysis of several site-specic mutants in the substrate channel of BjPutA revealed an important role for D779 in the channeling path. BjPutA mutants D779Y and D779W signicantly decreased the overall PRODH-P5CDH channeling reaction indicating that bulky mutations at residue D779 impede travel of P5C through the channel. Interestingly, D779Y and D779W also exhibited lower P5CDH activity, suggesting that exogenous P5C must enter the channel upstream of D779. Replacing D779 with a smaller residue (D779A) had no effect on the catalytic and channeling properties of BjPutA showing that the carboxylate group of D779 is not essential for channeling. An identical mutation at D778 (D778Y) did not impact BjPutA channeling activity. Thus, D779 is optimally orientated so that replacement with the larger side chains of Tyr/Trp blocks P5C movment through the channel. The kinetic data reveal not only that bulky mutations at residue D779 hinder passage of P5C to the second active site, but also P5C must use the channel to efciently access the P5CDH domain. Moreover, these mutants may be used to learn more about the hydrolysis event that is thought to take place within the channel

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

scholarly journals Structure, function, and mechanism of proline utilization A (PutA)

2017 ◽  
Vol 632 ◽  
pp. 142-157 ◽  
Author(s):  
Li-Kai Liu ◽  
Donald F. Becker ◽  
John J. Tanner
Keyword(s):  
Structure Function ◽  
Proline Utilization ◽  
Proline Utilization A

scholarly journals Discovery of the Membrane Binding Domain in Trifunctional Proline Utilization A

Biochemistry ◽  
2017 ◽  
Vol 56 (47) ◽  
pp. 6292-6303 ◽  
Author(s):  
Shelbi L. Christgen ◽  
Weidong Zhu ◽  
Nikhilesh Sanyal ◽  
Bushra Bibi ◽  
John J. Tanner ◽  
...  
Keyword(s):  
Membrane Binding ◽  
Binding Domain ◽  
Proline Utilization ◽  
Proline Utilization A

scholarly journals Engineering a trifunctional proline utilization A chimaera by fusing a DNA-binding domain to a bifunctional PutA

2016 ◽  
Vol 36 (6) ◽  
Author(s):  
Benjamin W. Arentson ◽  
Erin L. Hayes ◽  
Weidong Zhu ◽  
Harkewal Singh ◽  
John J. Tanner ◽  
...  
Keyword(s):  
Dna Binding ◽  
Modular Design ◽  
Quaternary Structure ◽  
Lipid Binding ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
Oligomeric State ◽  
Proline Utilization ◽  
Functional Switching ◽  
Proline Utilization A

Proline utilization A (PutA) is a bifunctional flavoenzyme with proline dehydrogenase (PRODH) and Δ1-pyrroline-5-carboxylate (P5C) dehydrogenase (P5CDH) domains that catalyses the two-step oxidation of proline to glutamate. Trifunctional PutAs also have an N-terminal ribbon–helix–helix (RHH) DNA-binding domain and moonlight as autogenous transcriptional repressors of the put regulon. A unique property of trifunctional PutA is the ability to switch functions from DNA-bound repressor to membrane-associated enzyme in response to cellular nutritional needs and proline availability. In the present study, we attempt to construct a trifunctional PutA by fusing the RHH domain of Escherichia coli PutA (EcRHH) to the bifunctional Rhodobacter capsulatus PutA (RcPutA) in order to explore the modular design of functional switching in trifunctional PutAs. The EcRHH–RcPutA chimaera retains the catalytic properties of RcPutA while acquiring the oligomeric state, quaternary structure and DNA-binding properties of EcPutA. Furthermore, the EcRHH–RcPutA chimaera exhibits proline-induced lipid association, which is a fundamental characteristic of functional switching. Unexpectedly, RcPutA lipid binding is also activated by proline, which shows for the first time that bifunctional PutAs exhibit a limited form of functional switching. Altogether, these results suggest that the C-terminal domain (CTD), which is conserved by trifunctional PutAs and certain bifunctional PutAs, is essential for functional switching in trifunctional PutAs.

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