Isozymes, moonlighting proteins and promiscous enzymes

Current Science

Volumn 100, Issue 8, 2011, Pages 1152-1162

  Gupta, Munishwar Nath ^a   Kapoor, Manali ^a   Majumder, Abir B ^a   Singh, Veena ^a  

^a INDIAN INSTITUTE OF TECHNOLOGY DELHI   (India)

Author keywords

Biological promiscuity; C C bond formation; Enzyme specificity; Isoenzymes; Moonlighting proteins

Indexed keywords

EID: 79955420122     PISSN: 00113891     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review

References (93)

1. Jeffery, C. J., Moonlighting proteins. Trends Biochem. Sci., 1999, 24, 8-11.
2. Jeffery, C. J., Multifunctional proteins: examples of gene sharing. Ann. Med., 2002, 35, 28-35.
3. Wool, I. J., Extraribosomal functions of ribosomal proteins. Trends Biochem. Sci., 1996, 21, 164-165.
4. Fersht, A., Enzyme Structure and Mechanism, Freeman, USA, 1984.
5. Williams, H. D., Stephens, E. and Zhou, M., How can enzymes be so efficient? Chem. Commun., 2003, 1973-1976.
6. Roy, I. and Gupta, M. N., Current trends in affinity-based separation of proteins/enzymes. Curr. Sci., 2000, 78, 587-591.
7. Gupta, M. N. and Roy, I., Affinity-based separation: an overview. In Methods for Affinity-based Separation of Proteins/Enzymes (ed. Gupta, M. N.), Birkhauser Verlag, Basel, 2002, pp. 1-15.
8. Mondal, K., Roy, I. and Gupta, M. N., Affinity based strategies for protein purification. Anal. Chem., 2006, 78, 3499-3504.
9. Vijaylakshmi, M. A. and Pitiot, O., Immobilized histidine ligand affinity chromatography. In Biochromatography: Theory and Practice (ed. Vijaylakshmi, M. A.), Taylor and Francis, London, 2002, pp. 252-271.
10. Labrou, N. E., Design and selection of ligands for affinity chromatography. J. Chromatogr. B, 2003, 790, 67-78.
11. Koshland Jr, D. E., The active site and enzyme action. In Advances in Enzymology (ed. Nord, F. F.), Interscience Publisher, Inc, New York, 1960, vol. 22, pp. 45-97.
12. Markert, C. L., Isoenzymes, Academic Press, New York, 1975, vols 1-4.
13. The Nomenclature of Multiple Forms of Enzymes; Recommendations (1976), based on the report of a subcommittee consisting of Fischer, E. H. et al., The document was published in the following journals: Arch. Biochem. Biophys., 1978, 185, 1-3.
14. Biochem. J., 1978, 171, 37-39.
15. Eur. J. Biochem., 1978, 82, 1-3.
16. J. Biol. Chem., 1977, 252, 5939-5941.
17. In Biochemical Nomenclature and Related Documents, Portland Press, 1992, 2nd edn, pp. 93-95.
18. Palmer, T., Enzymes: Biochemistry, Biotechnology, Clinical Chemistry, Horwood Publishing, Chichester, 2001, pp. 277-384.
19. Kelner, D. N. and Bhalgat, M. K., Analytical strategy for biopharmaceutical development. In Process Scale Bioseperations for the Biopharmaceutical Industry (eds Shukla, A. A., Etzel, M. R. and Gadam, S.), Taylor and Francis Group, CRC Press, London, 2007, pp. 395-418.
20. Voet, D., Voet, J. G. and Pratt, C. W., Introduction to metabolism. In Fundamentals of Biochemistry, John Wiley, 1999, p. 357.
21. Berg, J. M., Tymoczko, J. L. and Stryer, L., Biochemistry, W. H. Freeman and Company, New York, 2002, 5th edn, pp. 373-633.
22. Darnell, J., Lodish, H. and Baltimore, D., The cytoskeleton and cellular movements: actin-myosin. In Molecular Cell Biology, Scientific American Books, Inc, 1986, p. 833.
23. Partyka, R. A. and Szarka, F. T., Enzymatic preparation of (3rcis)-3-(acetoxy)-4-phenyl-2-azetidone: a taxon side-chain synthon. Biotechnol. Appl. Biochem., 1994, 20, 23-33.
24. Patel, R. N., Robinson, R. S. and Szarka, L. J., Stereoselective enzymatic hydrolysis of 2-cyclohexyl and 2 phenyl-1,3-propanediol diacetate in biphasic systems. Appl. Microbiol. Biotechnol., 1990, 34, 10-14.
25. Claon, P. A. and Akoh, C. C., Effect of reaction parameters on SP435 lipase-catalyzed synthesis of citronellyl acetate in organic solvent. Enzyme Microb. Technol., 1994, 16, 835-838.
26. Bradshaw, C. W., Fu, H., Shen, G. H. and Wong, C. H., A pseudomonas sp. alcohol dehydrogenase with broad substrate specificity and unusual stereospecificity for organic synthesis. J. Org. Chem., 1992, 57, 1526-1532.
27. Kula, M. R. and Kragl, U., Dehydrogenases in the synthesis of chiral compounds. In Stereoselective Biocatalysis (ed. Patel, R. N.), Marcel Dekker, Inc., New York, 2000, pp. 839-866.
28. María, P. D., Oerlemans, C. C., Tuin, B., Bargeman, G., van der Meer, A. and Robert van Gemert, Biotechnological applications of Candida antarctica lipase A: state-of-the-art. J. Mol. Catal. B: Enzymol., 2005, 37, 36-46.
29. Paizs, C., Tosa, M., Majdik, C., Tahtinen, P., Irimie, F. D. and Kanerva, L. T., Candida antarctica lipase A in the dynamic resolution of novel furylbenzotiazol-based cyanohydrin acetates. Tetrahedron: Asymm., 2003, 14, 619-627.
30. Piatigorsky, J., Multifunctional lens crystallins and corneal enzymes. More than meets the eye. Ann. New York Acad. Sci., 1998, 842, 7-15.
31. Piatigorsky, J., Lens crystallins: innovation associated with changes in gene regulation. J. Biol. Chem., 1992, 267, 4277-4280.
32. Barker, D. F. and Campbell, A. M., Genetic and biochemical characterization of the birA gene and its product: evidence for a direct role of biotin holoenzyme synthetase in represson of the biotin operon in Escherichia coli. J. Mol. Biol., 1981, 146, 469-492.
33. Jeffery, C. J., Moonlighting proteins: old proteins learning new tricks. Trends Genet., 2003, 19, 415-417.
34. Copley, S. D., Enzymes with extra talents: moonlighting functions and catalytic promiscuity. Curr. Opin. Chem. Biol., 2003, 7, 265-272.
35. Chaput, M. et al., The neurotrophic factor neuroleukin is 90% homologous with phosphohexose isomerase. Nature, 1988, 332, 454-455.
36. Faik, P., Walker, J. I. H., Redmill, A. A. M. and Morgan, M. J., Mouse glucose-6-phosphate isomerase and neuroleukin have identical 3′ sequences. Nature, 1988, 332, 455-456.
37. Siegler, K. M., Mauro, D. J., Seal, G., Wurzer, J., deRiel, J. K. and Sirover, M. A., A human nuclear uracil DNA glycosylase is the 37-kDa subunit of glyceraldehyde-3-phosphate dehydrogenase. Proc. Nat. Acad. Sci. USA, 1991, 88, 8460-8464.
38. Palmiter, R., Hormone action. In Biochemistry (ed. Zubay, G.), Macmillan Publishing Company, New York, 1989, 2nd edn, pp. 1045-1087.
39. Branden, C. and Tooze, J., Introduction to Protein Structure, Garland Publishing, Inc., New York and London, 1991, pp. 217-229.
40. Mowbray, S. L. and Koshland Jr, D. E., Mutations in the aspartate receptor of Escherichia coli which affect aspartate binding. J. Biol. Chem., 1990, 265, 15638-15643.
41. Tizard, I. R., Immunology: An Introduction, Saunders College Publishing, Philadelphia, 1988, 2nd edn.
42. Chu, E., Koeller, D. M., Casey, J. L., Chabner, B. A., Elwood, P. C., Zinn, S. and Allegra, C. J., Autoregulation of human thymidylate synthase messenger RNA translation by thymidylate synthase. Proc. Nat. Acad. Sci. USA, 1991, 88, 8977-8981.
43. Barker, D. F. and Campbell, A. M., Genetic and biochemical characterization of the birA gene and its product: evidence for a direct role of biotin holoenzyme synthetase in repression of the biotin operon in Escherichia coli. J. Mol. Biol., 1981, 146, 469-492.
44. Hult, K. and Berglund, P., Enzyme promiscuity: mechanism and applications. Trends Biotechnol., 2007, 25, 231-238.
45. Bornscheuer, U. T. and Kazlauskas, R. J., Catalytic promiscuity in biocatalysis: using old enzymes to form new bonds and follow new pathways. Angew. Chem. Int. Ed., 2004, 43, 6032-6040.
46. Kazlauskas, R. J., Enhancing catalytic promiscuity for biocatalysis. Curr. Opin. Chem. Biol., 2005, 9, 195-201.
47. Gupta, M. N., Enzyme function in organic solvents. Eur. J. Biochem., 1992, 203, 25-32.
48. Gupta, M. N. and Roy, I., Enzymes in organic media: forms, function and applications. Eur. J. Biochem., 2004, 271, 2575-2583.
49. Hudson, E. P., Eppler, R. K. and Clark, D. S., Biocatalysis in semi-aqueous and nearly anhydrous conditions. Curr. Opin. Biotechnol., 2005, 16, 637-643.
50. Carrea, G. and Riva, S., Properties and synthetic applications of enzymes in organic solvents. Angew. Chem. Int. Ed., 2000, 39, 2226-2254.
51. Gupta, M. N., Methods in Non-Aqueous Enzymology, Birkhauser Verlag, Basel, 2000.
52. Zaks, A. and Klibanov, A. M., Enzymatic catalysis in organic media at 100°C. Science, 1984, 224, 1249-1251.
53. Gupta, M. N., Thermostability of Enzymes, Springer Verlag, Germany, 1993.
54. Capewell, A., Wendel, V., Bornscheuer, U., Meyer, H. H. and Scheper, T., Lipase-catalyzed kinetic resolution of 3-hydroxy esters in organic solvents and supercritical carbon dioxide. Enzyme Microb. Technol., 1996, 19, 181-186.
55. Ulijn, R. V. and Halling, P. J., Solid to solid biocatalysis: thermodynamic feasibility and energy efficiency. Green Chem., 2004, 6, 488-496.
56. Majumder, A. B., Singh, B., Dutta, D., Sadhukhan, S. and Gupta, M. N., Lipase catalyzed synthesis of benzyl acetate in solvent-free medium using vinyl acetate as acyl donor. Bioorg. Med. Chem. Lett., 2006, 16, 4041-4044.
57. Shah, S. and Gupta, M. N., Kinetic resolution of (±)-1-phenylethanol in [Bmim][PF6] using high activity preparations of lipases. Bioorg. Med. Chem. Lett., 2007, 17, 921-924.
58. Berglund, P. and Hult, K., Biocatalytic synthesis of enantiopure compounds using lipases. In Stereoselective Biocatalysis (ed. Patel, R. N.), 2000, pp. 633-658.
59. Bornscheuer, U. T. and Kazlaukas, R. J., Catalytic promiscuity in biocatalysis: using old enzymes to form new bonds and follow new pathways. Angew. Chem. Int. Ed., 2004, 43, 6032-6040.
60. Jackson, R. C. and Handschumacher, R. E., Escherichia coli Lasparaginase. Catalytic activity and subunit nature. Biochemistry, 1970, 9, 3585-3590.
61. Ward, O. P. and Singh, A., Enzymatic asymmetric synthesis by decarboxylases. Curr. Opin. Biotechnol., 2000, 11, 520-526.
62. Li, C., Feng, X.-W., Wang, N., Zhou, Y.-J. and Yu, X.-Q., Biocatalytic promiscuity: the first lipase-catalysed asymmetric aldol reaction. Green Chem., 2008, 10, 616-618.
63. Torre, O., Alfonso, I. and Gotor, V., Lipase catalysed Michael addition of secondary amines to acrylonitrile. Chem. Commun., 2004, 1724-1725.
64. Li, K., He, T., Li, C., Feng, X. W., Wang, N. and Yu, X. O., Lipase-catalysed direct Mannich reaction in water: utilization of biocatalytic promiscuity for C-C bond formation in a 'one-pot' synthesis. Green Chem., 2009, 11, 777-779.
65. Feng, X. W., Li, C., Wang, N., Li, K., Zhang, W. W., Wang, Z. and Yu, X. O., Lipase-catalysed decarboxylative aldol reaction and decarboxylative Knoevenagel reaction. Green Chem., 2009, 11, 1933-1936.
66. Lou, F. W., Liu, B. K., Wu, Q., Lv, D. S. and Lin, X. F., Candida antarctica lipase B (CAL B)-catalyzed carbon sulphur bond addition and controllable selectivity in organic media. Adv. Synth. Catal., 2008, 350, 1959-1962.
67. Majumder, A. B., Ramesh, N. G. and Gupta, M. N., A lipase catalyzed condensation reaction with a tricyclic diketone: yet another example of biocatalytic promiscuity. Tetrahedron Lett., 2009, 50, 5190-5193.
68. Qian, C., Xu, J. M., Wu, Q., Lv, D. S. and Lin, X. F., Promiscuous acylase-catalysed aza-Michael additions of aromatic N-heterocycles in organic solvent. Tetrahedron Lett., 2007, 48, 6100-6104.
69. Reetz, M. T., Mondie're, R. and Daniel, J., Carballeira enzyme promiscuity: first protein-catalyzed Morita-Baylis-Hillman reaction. Tetrahedron Lett., 2007, 48, 1679-1681.
70. Smith, M. J. and Beck, W. S., Peroxidase activity of hemoglobin and its subunits: Effects there upon of haptoglobin. BBA-Protein Struct., 1967, 147, 324-333.
71. Babtie, A., Tokuriki, N. and Hollfelder, F., What makes an enzyme promiscuous? Curr. Opin. Chem. Biol., 2010, 14, 1-8.
72. Khersonsky, O., Roodveldt, C. and Tawfik, D. S., Enzyme promiscuity: evolutionary and mechanistic aspects. Curr. Opin. Chem. Biol., 2006, 10, 498-508.
73. James, L. C. and Tawfik, D. S., Conformational diversity and protein evolution - 60-year-old hypothesis revisited. Trends Biochem. Sci., 2003, 28, 361-368.
74. Janssen, D. B., Dinkla, I. J. T., Poelarends, G. J. and Terpstra, P., Bacterial degradation of xenobiotic compounds: evolution and distribution of novel enzyme activities. Environ. Microbiol., 2005, 7, 1868-1882.
75. Taleb, N. N., The Black Swan: The Impact of the Highly Improbable, Penguin Books Ltd, London, 2007.
76. Watson, J. D., Hopkins, N. H., Roberts, J. W., Steitz, J. A. and Weiner, A. M., The origins of life. In Molecular Biology of the Gene, Benzamin Cummings Publishing Company, Inc, 1987, 4th edn, p. 1103.
77. Richards, F. M. and Wyckoff, H. W., Hydrolysis. In The Enzymes (ed. Paul D. Boyer), 1971, pp. 647-806.
78. Bergmann, M. and Fruton, J. S., The specificity of proteinases. Adv. Enzymol., 1941, 1, 63-98.
79. Stepanov, V. M., Terent'eva, E. Y., Voyushina, T. L. and Gololobov, M. Y., Subtilisin and α-chymotrypsin catalyzed synthesis of peptides containing arginine and lysine p-nitroanilides as Cterminal moieties. Bioorg. Med. Chem. Lett., 1995, 3(5), 479-485.
80. Liu, C. F. and Tam, J. P., Subtilisin-catalyzed synthesis of amino acid and peptide esters. Application in a two-step enzymatic ligation strategy. Org. Lett., 2001, 3(26), 4157-4159.
81. Ferjancic, A., Puigserver, A. and Gaertner, H., Subtilisin catalyzed synthesis and transesterification in organic solvents. Appl. Microbiol. Biotechnol., 1990, 32, 651-657.
82. Clapés, P. and Adlercreutz, P., Substrate specificity of α -chymotrypsin-catalyzed esterification in organic media. BBA-Protein Struct. M., 1991, 1118, 70-76.
83. O'Hagan, D. and Zaldi, N. A., The resolution of tertiary alphaacetylene-acetate esters by the lipase from Candida cylindracea. Tetrahedron: Asymm., 1994, 5, 1111-1118.
84. Weber, H. K., Weber, H. and Kazlauskas, R. J., Watching lipasecatalyzed acylations using 1H NMR: competing hydrolysis of vinyl acetate in dry organic solvents. Tetrahedron: Asymm., 1999, 10, 2635-2638.
85. Bosley, J. A., Casey, J., Macrae, A. R. and MyCock, G. U. S., Process for the esterification of carboxylic acids with tertiary alcohols using a lipase from Candida antarctica. US patent 5658769, 1997, 5, 658-769.
86. Henke, H., Pleiss, J. and Bornscheuer, U. T., Activity of lipases and esterases towards tertiary alcohols: insights into structure function relationships. Angew. Chem. Int. Ed., 2002, 41, 3211-3213.
87. Shin, J. A., Akoh, C. C. and Lee, K. T., Enzymatic interesterification of anhydrous butterfat with flaxseed oil and palm stearin to produce low-trans spreadable fat. Food Chem., 2010, 120, 1-9.
88. 2 activation. Org. Lett., 2009, 11, 4846-4848.
89. Wang, J. L., Li, X., Xie, H. Y., Liu, B. K. and Lin, X. F., Hydrolase-catalyzed fast Henry reaction of nitroalkanes and aldehydes in organic media. J. Biotechnol., 2010, 145, 240-243.
90. Skouridou, V., Stamatis, H. and Kolisis, F. N., A study on the process of lipase-catalyzed synthesis of α -pinene oxide in organic solvents. Biocat. Biotrans., 2003, 21, 285-290.
91. Skouridou, V., Stamatis, H. and Kolisis, F. N., Lipase-mediated epoxidation of alpha-pinene. J. Mol. Catal. B: Enzymol., 2003, 21, 67-69.
92. Lemoult, S. C., Richardson, P. F. and Roberts, S. M., Lipase catalyzed Bayer-Villiger reactions. J. Chem. Soc. Perkin. Trans., 1995, 1, 89-91.
93. Högberg, H.-E. et al., Formation of hemiacetal esters in lipasecatalysed reactions of vinyl esters with hindered secondary alcohols. Tetrahedron Lett., 2000, 41, 3193-3196.