Engineering organophosphate hydrolase for enhanced biocatalytic performance: A review

2021 ◽  
Vol 168 ◽  
pp. 107945
Author(s):  
Lijie Wang ◽  
Yan Sun
2010 ◽  
Vol 27 (2) ◽  
pp. 360-367 ◽  
Author(s):  
Jared K. Raynes ◽  
F.Grant Pearce ◽  
Susie J. Meade ◽  
Juliet A. Gerrard

2019 ◽  
Vol 11 (9) ◽  
pp. 2557-2562 ◽  
Author(s):  
Sarwar Azam ◽  
Sunil Parthasarathy ◽  
Chhaya Singh ◽  
Shakti Kumar ◽  
Dayananda Siddavattam

Abstract Sphingobium fuliginis ATCC 27551, previously classified as Flavobacterium sp. ATCC 27551, degrades neurotoxic organophosphate insecticides and nerve agents through the activity of a membrane-associated organophosphate hydrolase. This study was designed to determine the complete genome sequence of S. fuliginis ATCC 27551 to unravel its degradative potential and adaptability to harsh environments. The 5,414,624 bp genome with a GC content of 64.4% is distributed between two chromosomes and four plasmids and encodes 5,557 proteins. Of the four plasmids, designated as pSF1, pSF2, pSF3, and pSF4, only two (pSF1 and pSF2) are self-transmissible and contained the complete genetic repertoire for a T4SS. The other two plasmids (pSF3 and pSF4) are mobilizable and both showed the presence of an oriT and relaxase-encoding sequences. The sequence of plasmid pSF3 coincided with the previously determined sequence of pPDL2 and included an opd gene encoding organophosphate hydrolase as a part of the mobile element. About 15,455 orthologous clusters were identified from among the cumulatively annotated genes of 49 Sphingobium species. Phylogenetic analysis done using the core genome consisting of 802 orthologous clusters revealed a close relationship between S. fuliginis ATCC 27551 and bacteria capable of degradation of polyaromatic hydrocarbon compounds. Genes coding for transposases, efflux pumps conferring resistance to heavy metals, and TonR-type outer membrane receptors are selectively enriched in the genome of S. fuliginis ATCC 27551 and appear to contribute to the adaptive potential of the organism to challenging and harsh environments.


Biochemistry ◽  
2016 ◽  
Vol 55 (9) ◽  
pp. 1408-1417 ◽  
Author(s):  
Peter D. Mabbitt ◽  
Galen J. Correy ◽  
Tamara Meirelles ◽  
Nicholas J. Fraser ◽  
Michelle L. Coote ◽  
...  

1994 ◽  
Vol 41 (3) ◽  
pp. 352-358 ◽  
Author(s):  
Kirti I. Dave ◽  
Crystal Lauriano ◽  
Biwen Xu ◽  
James R. Wild ◽  
Charles M. Kenerley

2001 ◽  
Vol 67 (10) ◽  
pp. 4922-4925 ◽  
Author(s):  
Cui Zhongli ◽  
Li Shunpeng ◽  
Fu Guoping

ABSTRACT A degradative bacterium, M6, was isolated and presumptively identified as Plesiomonas sp. strain M6 was able to hydrolyze methyl parathion to p-nitrophenol. A novel organophosphate hydrolase gene designated mpd was selected from its genomic library prepared by shotgun cloning. The nucleotide sequence of the mpd gene was determined. The gene could be effectively expressed in Esherichia coli.


2006 ◽  
Vol 71 (2) ◽  
pp. 167-172 ◽  
Author(s):  
Yu. A. Votchitseva ◽  
E. N. Efremenko ◽  
T. K. Aliev ◽  
S. D. Varfolomeyev

2018 ◽  
Vol 32 (S1) ◽  
Author(s):  
Cetara Baker ◽  
Jaffet Santiago Garcia ◽  
Richard Sweeney ◽  
Stephen Kirby

2020 ◽  
Author(s):  
Hari Parapatla ◽  
Ramurthy Gudla ◽  
Guruprasad Varma Konduru ◽  
Elsin Raju Devadasu ◽  
Hampapathula Adimurthy Nagarajaram ◽  
...  

Our previous studies have shown the existence of organophosphate hydrolase (OPH) as a part of the inner membrane associated TonB complex (ExbB/ExbD and TonB) of Sphingobium fuliginis. We now show its involvement in iron uptake by establishing direct interactions with ferric-enterobactin. The interactions between OPH and ferric-enterobactin were not affected even when the active site architecture is altered by substituting active site aspartate with either alanine or asparagine. Protein docking studies further substantiated these findings and predicted the existence of ferric-enterobactin binding site that is different from the catalytic site of OPH. A lysine residue (82 K) found at the predicted ferric-enterobactin binding site facilitated interactions between OPH and ferric-enterobactin. Substitution of lysine with alanine did not affect triesterase activity, but it abrogated OPH ability to interact with both ferric-enterobactin and ExbD, strengthening further the fact that the catalytic site is not the site for binding of these ligands. In the absence of interactions between OPHK82A and ExbD, OPHK82A failed to target membrane in E. coli cells. The Sphingobium fuliginis TonB dependent transport (SfTonBDT) system was reconstituted in E. coli GS027 cells generated by deleting the exbD and tonB genes. The E. coli GS030 cells having SfTonBDT system with OPH showed increased iron uptake. Such an increase was not seen in E. coli GS029, cells having SfTonBDT system generated either by omitting OPH or by including its variants, OPHD301A, OPHD301N suggesting a role for OPH in enhanced iron uptake.


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