Facilitated substrate channeling in a self-assembled trifunctional enzyme complex

Angewandte Chemie - International Edition

Volumn 51, Issue 35, 2012, Pages 8787-8790

  You, Chun ^a   Myung, Suwan ^a   Zhang, Y H Percival ^a,b,c,d  

^a State University   (United States)

^b VIRGINIA POLYTECHNIC INSTITUTE AND STATE UNIVERSITY   (United States)

^c DOE Bioenergy Science Center   (United States)

^d Gate Fuels Inc   (United States)

Author keywords

biocatalysis; enzyme cascades; enzymes; metabolon; self assembly

Indexed keywords

ALDOLASES; BIOCATALYSIS; COHESINS; ENZYME CASCADES; ENZYME COMPLEXES; ENZYME CONCENTRATIONS; METABOLON; SELF-ASSEMBLED; SYNTHETIC ENZYMES; TRIOSEPHOSPHATE ISOMERASE;

REACTION RATES; SELF ASSEMBLY;

ENZYMES;

FRUCTOSE BISPHOSPHATASE; FRUCTOSE BISPHOSPHATE ALDOLASE; TRIOSEPHOSPHATE ISOMERASE;

ARTICLE; BIOCATALYSIS; CHEMISTRY; ENZYME SPECIFICITY; KINETICS; METABOLISM; PROTEIN TERTIARY STRUCTURE; TEMPERATURE;

BIOCATALYSIS; FRUCTOSE-BISPHOSPHATASE; FRUCTOSE-BISPHOSPHATE ALDOLASE; KINETICS; PROTEIN STRUCTURE, TERTIARY; SUBSTRATE SPECIFICITY; TEMPERATURE; TRIOSE-PHOSPHATE ISOMERASE;

EID: 84865404296     PISSN: 14337851     EISSN: 15213773     Source Type: Journal    
DOI: 10.1002/anie.201202441     Document Type: Article

References (27)

1. P. A. Srere, Annu. Rev. Biochem. 1987, 56, 89-124.
2. B. L. Møller, Science 2010, 330, 1328-1329.
3. Y.-H. P. Zhang, Biotechnol. Adv. 2011, 29, 715-725.
4. L. Iturrate, I. Sanchez-Moreno, E. G. Doyaguez, E. Garcia-Junceda, Chem. Commun. 2009, 1721-1723.
5. H. Pettersson, G. Pettersson, Biochim. Biophys. Acta. Protein Struct. Mol. Enzymol. 2001, 1549, 155-160.
6. Y.-H. P. Zhang, ACS Catal. 2011, 1, 998-1009.
7. X. Ye, Y. Wang, R. C. Hopkins, M. W. W. Adams, B. R. Evans, J. R. Mielenz, Y.-H. P. Zhang, ChemSusChem 2009, 2, 149-152.
8. O. I. Wilner, Y. Weizmann, R. Gill, O. Lioubashevski, R. Freeman, I. Willner, Nat. Nanotechnol. 2009, 4, 249-254.
9. M. J. Moehlenbrock, T. K. Toby, A. Waheed, S. D. Minteer, J. Am. Chem. Soc. 2010, 132, 6288-6289.
10. E. A. Bayer, E. Morag, R. Lamed, Trends Biotechnol. 1994, 12, 379-386.
11. F. Mingardon, A. Chanal, C. Tardif, E. A. Bayer, H.-P. Fierobe, Appl. Environ. Microbiol. 2007, 73, 7138-7149.
12. D. Rakus, M. Pasek, H. Krotkiewski, A. Dzugaj, Biochemistry 2004, 43, 14948-14957
13. S. Beeckmans, E. Van Driessche, L. Kanarek, J. Mol. Recognit. 1993, 6, 195-204.
14. Y. Wang, W. Huang, N. Sathitsuksanoh, Z. Zhu, Y.-H. P. Zhang, Chem. Biol. 2011, 18, 372-380.
15. S. Myung, Y. R. Wang, Y.-H. P. Zhang, Proc. Biochem. 2010, 45, 1882-1887.
16. C. You, X.-Z. Zhang, Y. H. P. Zhang, Biochem. Eng. J. 2012, 63, 57-65.
17. O. Shoseyov, R. H. Doi, Proc. Natl. Acad. Sci. USA 1990, 87, 2192-2195.
18. S.-Y. Ding, M. T. Rincon, R. Lamed, J. C. Martin, S. I. McCrae, V. Aurilia, Y. Shoham, E. A. Bayer, H. J. Flint, J. Bacteriol. 2001, 183, 1945-1953.
19. C. You, X.-Z. Zhang, Y.-H. P. Zhang, Appl. Environ. Microbiol. 2012, 78, 1593-1595.
20. C. You, X. Z. Zhang, N. Sathitsuksanoh, L. R. Lynd, Y.-H. P. Zhang, Appl. Environ. Microbiol. 2012, 78, 1437-1444.
21. S. Moraïs, Y. Barak, Y. Hadar, D. B. Wilson, Y. Shoham, R. Lamed, E. A. Bayer, mBio 2011, 2, e 00233-11.
22. R. L. Veech, L. Raijman, K. Dalziel, H. A. Krebs, Biochem. J. 1969, 115, 837-842.
23. D. Maes, J. P. Zeelen, N. Thanki, N. Beaucamp, M. Alvarez, M. H. Thi, J. Backmann, J. A. Martial, L. Wyns, R. Jaenicke, R. K. Wierenga, Proteins 1999, 37, 441-453.
24. M. Sherawat, D. R. Tolan, K. N. Allen, Acta Crystallogr. D 2008, 64, 543-550.
25. K.-P. Gerbling, M. Steup, E. Latzko, Eur. J. Biochem. 1985, 147, 207-215.
26. L. Bülow, K. Mosbach, Trends Biotechnol. 1991, 9, 226-231.
27. J. E. Dueber, G. C. Wu, G. R. Malmirchegini, T. S. Moon, C. J. Petzold, A. V. Ullal, K. L. J. Prather, J. D. Keasling, Nat. Biotechnol. 2009, 27, 753-759.