NAD(H)-PEG Swing Arms Improve Both the Activities and Stabilities of Modularly-Assembled Transhydrogenases Designed with Predictable Selectivities.
biocatalysis
enzyme catalysis
protein engineering
protein stability
substrate channeling
Journal
Chembiochem : a European journal of chemical biology
ISSN: 1439-7633
Titre abrégé: Chembiochem
Pays: Germany
ID NLM: 100937360
Informations de publication
Date de publication:
04 02 2022
04 02 2022
Historique:
revised:
04
08
2021
received:
25
05
2021
pubmed:
6
8
2021
medline:
9
3
2022
entrez:
5
8
2021
Statut:
ppublish
Résumé
Protein engineering has been used to enhance the activities, selectivities, and stabilities of enzymes. Frequently tradeoffs are observed, where improvements in some features can come at the expense of others. Nature uses modular assembly of active sites for complex, multi-step reactions, and natural "swing arm" mechanisms have evolved to transfer intermediates between active sites. Biomimetic polyethylene glycol (PEG) swing arms modified with NAD(H) have been explored to introduce synthetic swing arms into fused oxidoreductases. Here we report that increasing NAD(H)-PEG swing arms can improve the activity of synthetic formate:malate oxidoreductases as well as the thermal and operational stabilities of the biocatalysts. The modular assembly approach enables the K
Identifiants
pubmed: 34351671
doi: 10.1002/cbic.202100251
doi:
Substances chimiques
NAD
0U46U6E8UK
Polyethylene Glycols
3WJQ0SDW1A
NADP Transhydrogenases
EC 1.6.1.-
Types de publication
Journal Article
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Pagination
e202100251Subventions
Organisme : US Army Research Office
Organisme : Department of Defense Multidisciplinary University Research Initiative Program
ID : W911NF1410263
Informations de copyright
© 2021 Wiley-VCH GmbH.
Références
B. M. Beadle, B. K. Shoichet, J. Mol. Biol. 2002, 321, 285-296.
P. A. Dalby, Curr. Opin. Struct. Biol. 2011, 21, 473-480.
J. D. Bloom, S. T. Labthavikul, C. R. Otey, F. H. Arnold, PNAS 2006, 103, 5869-5874.
O. K. Tawfik, D. S. Tawfik, Annu. Rev. Biochem. 2010, 79, 471-505.
P. A. Srere, Annu. Rev. Biochem. 1987, 56, 89-124.
T. Robbins, Y.-C. Liu, D. E. Cane, C. Khosla, Curr. Opin. Struct. Biol. 2016, 41, 10-18.
D. E. Cane, J. Biol. Chem. 2010, 285, 27517-27523.
R. N. Perham, Annu. Rev. Biochem. 2000, 69, 961-1004.
I. Wheeldon, S. D. Minteer, S. Banta, S. C. Barton, P. Atanassov, M. Sigman, Nat. Chem. 2016, 8, 299-309.
H. O. Spivey, J. Ovádi, Methods 1999, 19, 306-321.
R. J. Conrado, J. D. Varner, M. P. DeLisa, Curr. Opin. Biotechnol. 2008, 19, 492-499.
D. B. Northrop, J. Biol. Chem. 1969, 244, 5808-5819.
H. F. Ozbakir, K. E. Garcia, S. Banta, Protein Eng. Des. Sel. 2018, 31, 103-108.
B. Zakeri, J. O. Fierer, E. Celik, E. C. Chittock, U. Schwarz-Linek, V. T. Moy, M. Howarth, Proc. Natl. Acad. Sci. USA 2012, 109, E690.
S. R. Piersma, S. de Vries, J. A. Duine, in Enzymology and Molecular Biology of Carbonyl Metabolism 6 (Eds.: H. Weiner, R. Lindahl, D. W. Crabb, T. G. Flynn), Springer US, Boston, MA, 1997, pp. 425-434.
M. Zachariou, R. K. Scopes, J. Bacteriol. 1986, 167, 863-869.
U. T. Bornscheuer, M. Pohl, Curr. Opin. Chem. Biol. 2001, 5, 137-143.
V. B. Damodaran, C. Fee, Eur. Pharmac. Rev. 2010, 15, 18-26.
Y. H. Kim, W. E. Stites, Biochemistry 2008, 47, 8804-8814.
I. M. Kuznetsova, B. Y. Zaslavsky, L. Breydo, K. K. Turoverov, V. N. Uversky, Molecules 2015, 20, 1377-1409.
W. Meng, X. Guo, M. Qin, H. Pan, Y. Cao, W. Wang, Langmuir 2012, 28, 16133-16140.
P. B. Lawrence, Y. Gavrilov, S. S. Matthews, M. I. Langlois, D. Shental-Bechor, H. M. Greenblatt, B. K. Pandey, M. S. Smith, R. Paxman, C. D. Torgerson, J. P. Merrell, C. C. Ritz, M. B. Prigozhin, Y. Levy, J. L. Price, J. Am. Chem. Soc. 2014, 136, 17547-17560.
S. Moreno-Pérez, A. H. Orrego, M. Romero-Fernández, L. Trobo-Maseda, S. Martins-DeOliveira, R. Munilla, G. Fernández-Lorente, J. M. Guisan, Methods Enzymol. 2016, 571, 55-72.
J. Bullock, S. Chowdhury, A. Severdia, J. Sweeney, D. Johnston, L. Pachla, Anal. Biochem. 1997, 254, 254-262.
T. Yu, J. A. Traina, E. Pungor, M. McCaman, Anal. Biochem. 2006, 359, 54-62.
A. S. Bommarius, M. F. Paye, Chem. Soc. Rev. 2013, 42, 6534-6565.
A. S. Bommarius, K. Drauz, H. Klenk, C. Wandrey, Ann. N. Y. Acad. Sci. 1992, 672, 126-136.
N. Pi, Y. Yu, J. D. Mougous, J. A. Leary, Protein Sci. 2004, 13, 903-912.
L. Kirmair, D. L. Seiler, A. Skerra, Appl. Microbiol. Biotechnol. 2015, 99, 10501-10513.
B. A. Shirley, Protein Stability and Folding: Theory and Practice, Humana Press, 1995.
T. A. Rogers, A. S. Bommarius, Chem. Eng. Sci. 2010, 65, 2118-2124.
V. Höllrigl, F. Hollmann, A. C. Kleeb, K. Buehler, A. Schmid, Appl. Microbiol. Biotechnol. 2008, 81, 263-273.
F. Coccia, L. Tonucci, P. Del Boccio, S. Caporali, F. Hollmann, N. D'Alessandro, Nanomaterials 2018, 8, 853.
F. Hollmann, A. Kleeb, K. Otto, A. Schmid, Tetrahedron: Asymmetry 2005, 16, 3512-3519.
V. Höllrigl, K. Otto, A. Schmid, Adv. Synth. Catal. 2007, 349, 1337-1340.
M. Poizat, I. W. C. E. Arends, F. Hollmann, J. Mol. Catal. B 2010, 63, 149-156.
H. Man, S. Gargiulo, A. Frank, F. Hollmann, G. Grogan, J. Mol. Catal. B 2014, 105, 1-6.
E. M. Tarmy, N. O. Kaplan, J. Biol. Chem. 1968, 243, 2587-2596.
P. Kelefiotis-Stratidakis, T. Tyrikos-Ergas, I. V. Pavlidis, Org. Biomol. Chem. 2019, 17, 1634-1642.
R. L. Hanson, B. L. Davis, S. L. Goldberg, R. M. Johnston, W. L. Parker, T. P. Tully, M. A. Montana, R. N. Patel, Org. Process Res. Dev. 2008, 12, 1119-1129.
H. Yu, P. A. Dalby, Proc. Natl. Acad. Sci. USA 2018, 115, E12192-E12200.
A. Cipolla, F. Delbrassine, J.-L. Da Lage, G. Feller, Biochimie 2012, 94, 1943-1950.
A. Yokota, H. Takahashi, T. Takenawa, M. Arai, Biochem. Biophys. Res. Commun. 2010, 391, 1703-1707.
M. Torrado, J. Revuelta, C. Gonzalez, F. Corzana, A. Bastida, J. L. Asensio, J. Biol. Chem. 2009, 284, 23765-23779.
R. S. Fredricksen, C. A. Swenson, Biochemistry 1996, 35, 14012-14026.
G. Feller, C. Gerday, Nat. Rev. Microbiol. 2003, 1, 200-208.