Enzymes from extreme environments and their industrial applications

Frontiers in Bioengineering and Biotechnology

Volumn 3, Issue OCT, 2015, Pages

  Littlechild, Jennifer A ^a  

^a UNIVERSITY OF EXETER   (United Kingdom)

Author keywords

Carbonic anhydrase; Dehalogenase; Epoxide hydrolase; Esterase; L aminoacylase; Transaminase; lactamase

Indexed keywords

CARBONIC ANHYDRASE; CELL IMMOBILIZATION; ESTERS; HYDROLASES; TOXIC MATERIALS; WASTE DISPOSAL;

AMINOACYLASE; DEHALOGENASE; EPOXIDE HYDROLASES; ESTERASE; LACTAMASES; TRANSAMINASE;

BIOCHEMICAL ENGINEERING;

EID: 84969122301     PISSN: None     EISSN: 22964185     Source Type: Journal    
DOI: 10.3389/fbioe.2015.00161     Document Type: Review

References (55)

1. Andreeva, A., Howorth, D., Chothia, C., Kulesha, E., and Murzin, A. G. (2014). SCOP2 prototype: a new approach to protein structure mining. Nucleic Acids Res. 42, D310-D314. doi:10.1093/nar/gkt1242
2. Arai, R., Kukimoto-Niino, M., Kuroishi, C., Bessho, Y., Shirouzu, M., and Yokoyama, S. (2006). Crystal structure of the probable haloacid dehalogenase PH0459 from Pyrococcus horikoshii OT3. Protein Sci. 15, 373-377. doi:10.1110/ps.051922406
3. Arand, M., Hallberg, B. M., Zou, J., Bergfors, T., Oesch, F., van der Werf, M. J., et al. (2003). Structure of Rhodococcus erythropolis limonene-1,2-epoxide hydrolase reveals a novel active site. EMBO J. 22, 2583-2592. doi:10.1093/emboj/cdg275
4. Bains, J., Kaufman, L., Farnell, B., and Boulanger, M. J. (2011). A product analog bound form of 3-oxoadipate-enol-lactonase (PcaD) reveals a multifunctional role for the divergent cap domain. J. Mol. Biol. 406, 649-658. doi:10.1016/j.jmb.2011.01.007
5. Baxter, S., Royer, S., Grogan, G., Brown, F., Holt-Tiffin, K., Taylor, I., et al. (2012). An improved racemase/acylase biotransformation for the amino acids. J. Am. Chem. Soc. 134, 19310-19313. doi:10.1021/ja305438y
6. Bommarius, A. S., Schwarm, M., and Drauz, K. (1998). Biocatalysis to aminoacid-based chiral pharmaceuticals: examples and perspectives. J. Mol. Catal. B Enzym. 5, 1-11. doi:10.1016/S1381-1177(98)00009-5
7. Breezee, J., Cady, N., and Staley, J. T. (2004). Subfreezing growth of the sea ice bacterium Psychromonas ingrahamii. Microb. Ecol. 47, 300-304. doi:10.1007/s00248-003-1040-9
8. Cheeseman, J. D., Tocilj, A., Park, S., Schrag, J. D., and Kazlauskas, R. J. (2004). Structure of an aryl esterase from Pseudomonas fluorescens. Acta Crystallogr. D60, 1237-1243. doi:10.1107/S0907444904010522
9. Chen, B. H., Sayar, A., Kaulmann, U., Dalby, P. A., Ward, J. M., and Woodley, J. M. (2006). Reaction modelling and simulation to assess the integrated use of transketolase and ω-transaminase for the synthesis of an aminotriol. Biocatal. Biotransformation 24, 449-457. doi:10.1080/10242420601068668
10. Daniel, R. M., and Danson, M. J. (2010). A new understanding of how temperature affects the catalytic activity of enzymes. Trends Biochem. Sci. 35, 584-591. doi:10.1016/j.tibs.2010.05.001
11. Di Fiore, A., Capasso, C., De Luca, V., Monti, S. M., Carginale, V., Supuran, C. T., et al. (2013). X-ray structure of the first 'extremo-a-carbonic anhydrase', a dimeric enzyme from the thermophilic bacterium Sulfurihydrogenibium yellowstonense YO3AOP1. Acta Crystallogr. D69, 1150-1159. doi:10.1107/S0907444913007208
12. Drauz, K. (1997). Chiral amino acids: a versatile tool in the synthesis of pharmaceuticals and fine chemicals. Int J Chem Chimia 51, 310-314.
13. Feller, G. (2003). Molecular adaptations to cold in psychrophilic enzymes. Cell. Mol. Life Sci. 60, 648-662. doi:10.1007/s00018-003-2155-3
14. Feller, G., and Gerday, C. (2003). Psychrophilic enzymes: hot topics in cold adaption. Nat. Rev. Microbiol. 1, 200-208. doi:10.1038/nrmicro773
15. Ferrandi, E. E., Sayer, C., Isupov, M. N., Annovazzi, C., Marchesi, C., Iacobone, G., et al. (2015a). Discovery and characterization of thermophilic limonene-1,2-epoxide hydrolases from hot spring metagenomics libraries. FEBS J. 282, 2879-2894. doi:10.1111/febs.13328
16. Ferrandi, E., Marchesi, C., Annovazzi, C., Riva, S., Monti, D., and Wohlgemuth, R. (2015b). Efficient epoxide hydrolase-catalyzed resolutions of (+)-and (-)-cis/trans-limonene oxides. ChemCatChem doi:10.1002/cctc.201500608
17. Georlette, D., Blaise, V., Collins, T., D'Amico, S., Gratia, E., Hoyoux, A., et al. (2004). Some like it cold: biocatalysis at low temperatures. FEMS Microbiol. Rev. 28, 25-42. doi:10.1016/j.femsre.2003.07.003
18. Georlette, D., Damiens, B., Blaise, V., Depiereux, E., Uversky, V. N., Gerday, C., et al. (2003). Structural and functional adaptations to extreme temperatures in psychrophilic, mesophilic and thermophilic DNA ligases. J. Biol. Chem. 278, 37015-37023. doi:10.1074/jbc.M305142200
19. Gerike, U., Danson, M. J., and Hough, D. W. (2001). Cold-active citrate synthase: mutagenesis of active-site residues. Protein Eng. 14, 655-661. doi:10.1093/protein/14.9.655
20. Gerike, U., Danson, M. J., Russell, N. J., and Hough, D. W. (1997). Sequencing and expression of the gene encoding a cold active citrate synthase from an Antarctic bacterium, strain DS2 3R. Eur. J. Biochem. 248, 49-57. doi:10.1111/j.1432-1033.1997.00049.x
21. Gomes, J., and Steiner, W. (2004). The biocatalytic potential of Extremophiles and Extremozymes. Food Technol. Biotechnol. 42, 223-235.
22. Gonsalvez, I. S., Isupov, M., and Littlechild, J. A. (2001). Crystallization and preliminary X-ray analysis of a gamma-lactamase. Acta Crystallogr. D57, 284-286. doi:10.1107/S0907444900016838
23. Guler, O. O., Capasso, C., and Supuran, C. T. (2015). A magnificent enzyme superfamily: carbonic anhydrases, their purification and characterization. J. Enzyme Inhib. Med. Chem. doi:10.3109/14756366.2015.1059333
24. Hickey, A. M., Ngamsom, B., Wiles, C., Greenway, G. M., Watts, P., and Littlechild, J. A. (2009). A microreactor for the study of biotransformations by a cross-linked gamma-lactamase enzyme. Biotechnol. J. 4, 510-516. doi:10.1002/biot.200800302
25. Holt, K. (2004). Biocatalysis and chemocatalysis-a powerful combination for the preparation of enantiomerically pure a-amino acids. Pharmachem 3, 2-4. doi:10.1002/chin200542274
26. Hopmann, K. H., Hallberg, B. M., and Himo, F. (2005). Catalytic mechanism of limonene epoxide hydrolase, a theoretical study. J. Am. Chem. Soc. 127, 14339-14347. doi:10.1021/ja050940p
27. James, P., Isupov, M. N., Sayer, C., Saneei, V., Berg, S., Lioliou, M., et al. (2014). The structure of a tetrameric a-carbonic anhydrase from Thermovibrio ammonificans reveals a core formed around intermolecular disulfides that contribute to its thermostability. Acta Crystallogr. D70, 2607-2618. doi:10.1107/S1399004714016526
28. Kobayashi, M., Fujiwara, Y., Goda, M., Komeda, H., and Shimizu, S. (1997). Identification of active sites in amidase: evolutionary relationship between amide bond-and peptide bond-cleaving enzymes. Proc. Natl. Acad. Sci. U.S.A. 94, 11986-11991. doi:10.1073/pnas.94.22.11986
29. Kong, X.-D., Ma, Q., Zhou, J., Zeng, B.-B., and Xu, J.-H. (2014). A smart library of epoxide hydrolase variants and the top hits for synthesis of (S)-β-blocker precursors. Angew. Chem. Int. Ed. 53, 6641-6644. doi:10.1002/anie.201402653
30. Kotik, M., Archelas, A., and Wohlgemuth, R. (2012). Epoxide hydrolases and their application in organic synthesis. Curr. Org. Chem. 16, 451-482. doi:10.2174/138527212799499840
31. Lee, C. K., Daniel, R. M., Shepherd, C., Saul, D., Cary, S. C., Danson, M. J., et al. (2007). Eurythermalism and temperature dependence of enzyme activity. FASEB J. 8, 1934-1941. doi:10.1096/fj.06-7265com
32. Line, K., Isupov, M. N., and Littlechild, J. A. (2004). The crystal structure of a (-) γ-lactamase from an Aureobacterium species reveals a tetrahedral intermediate in the active site. J. Mol. Biol. 338, 519-532. doi:10.1016/j.jmb.2004.03.001
33. Littlechild, J., James, P., Novak, H., and Sayer, C. (2013). "Mechanisms of thermal stability adopted by thermophilic proteins and their use in white biotechnology," in Thermophilic Microbes in Environmental and Industrial Biotechnology, Biotechnology of Thermophiles, 2nd Edn, eds Satyanarayana T., Littlechild J., and Kawarabayasi Y. (London: Springer Publishers), 481-507.
34. Nestl, B. M., Hammer, S. C., Nebel, B. A., and Hauer, B. (2014). New generation of biocatalysts for organic synthesis. Angew. Chem. Int. Ed. 53, 3070-3095. doi:10.1002/anie.201302195
35. Ngamsom, B., Hickey, A. M., Greenway, G. M., Littlechild, J. A., Watts, P., and Wiles, C. (2010). Development of a high throughput screening tool for biotransformations utilising a thermophilic l-aminoacylase enzyme. J. Mol. Catal. B Enzym. 63, 81-86. doi:10.1016/j.molcatb.2009.12.013
36. Novak, H., and Littlechild, J. (2013). "Marine enzymes for biocatalysis. Sources, biocatalytic characteristics and bioprocesses of marine enzymes," in Marine Enzymes with Applications for Biosynthesis of Fine Chemicals, ed. Trincone A. (Cambridge: Woodhead Publishing Series in Biomedicine), 89-102.
37. Novak, H. R., Sayer, C., Panning, J., and Littlechild, J. A. (2013a). Characterisation of an l-haloacid dehalogenase from the marine psychrophile Psychromonas ingrahamii with potential industrial application. Mar. Biotechnol. 6, 695-705. doi:10.1007/s10126-013-9522-3
38. Novak, H. R., Sayer, C., Isupov, M. N., Paszkiewicz, K., Gotz, D., Mearns-Spragg, A., et al. (2013b). Marine Rhodobacteraceae l-haloacid dehalogenase contains a novel His/Glu dyad which could activate the catalytic water. FEBS J. 280, 1664-1680. doi:10.1111/febs.12177
39. Riley, M., Staley, J. T., Danchin, A., Wang, T. Z., Brettin, T. S., Hauser, L. J., et al. (2008). Genomics of an extreme psychrophile, Psychromonas ingrahamii. BMC Genomics 9:210. doi:10.1186/1471-2164-9-210
40. Rye, C. A., Isupov, M. N., Lebedev, A. A., and Littlechild, J. A. (2007). An order-disorder twin crystal of l-2-haloacid dehalogenase from Sulfolobus tokodaii. Acta Crystallogr. D63, 926-930. doi:10.1107/S0907444907026315
41. Rye, C. A., Isupov, M. N., Lebedev, A. A., and Littlechild, J. A. (2009). Biochemical and structural studies of a l-haloacid dehalogenase from the thermophilic archaeon Sulfolobus tokodaii. Extremophiles 13, 179-190. doi:10.1007/s00792-008-0208-0
42. Sayer, C., Bommer, M., Ward, J. M., Isupov, M. N., and Littlechild, J. A. (2012). Crystal structure and substrate specificity of the thermophilic serine:pyruvate aminotransferase from Sulfolobus solfataricus. Acta Crystallogr. D68, 763-772. doi:10.1107/S0907444912011274
43. Sayer, C., Isupov, M. N., Bonch-Osmolovskaya, E., and Littlechild, J. A. (2015). Structural studies of a thermophilic esterase from a new Planctomycetes species, Thermogutta terrifontis. FEBS J. 282, 2846-2857. doi:10.1111/febs.13326
44. Silverman, D. N., and Lindskog, S. (1988). The catalytic mechanism of carbonic anhydrase: implications of a rate-limiting protolysis of water. Acc. Chem. Res. 21, 30-36. doi:10.1021/ar00145a005
45. Singleton, M., Isupov, M., and Littlechild, J. (1999). X-ray structure of pyrrolidone carboxyl peptidase from the hyperthermophilic archaeon Thermococcus litoralis. Structure 7, 237-244. doi:10.1016/S0969-2126(99)80034-3
46. Smith, K. S., Jakubzick, C., Whittam, T. S., and Ferry, J. G. (1999). Carbonic anhydrase is an ancient enzyme widespread in prokaryotes. Proc. Natl. Acad. Sci. U.S.A. 96, 15184-15189. doi:10.1073/pnas.96.26.15184
47. Tanimoto, K., Higashi, N., Nishioka, M., Ishikawa, K., and Taya, M. (2008). Characterization of thermostable aminoacylase from hyperthermophilic archaeon Pyrococcus horikoshii. FEBS J. 275, 1140-1149. doi:10.1111/j.1742-4658.2008.06274.x
48. Taylor, S. J. C., McCague, R., Wisdom, R., Lee, C., Dickson, K., Ruecroft, G., et al. (1993). Development of the biocatalytic resolution of 2-azabicyclo [2.2.1] hept-5-en-3-one as an entry to single-enantiomer carbocyclic nucleosides. Tetrahedron 4, 1117-1128. doi:10.1016/S0957-4166(00)80218-9
49. Toogood, H. S., Brown, R. C., Line, K., Keene, P. A., Taylor, S. J. C., McCague, R., et al. (2004). The use of a thermostable signature amidase in the resolution of the bicyclic synthon (rac)-γ-lactam. Tetrahedron 60, 711-716. doi:10.1016/j.tet.2003.11.064
50. Toogood, H. S., Hollingsworth, E. J., Brown, R. C., Taylor, I. N., Taylor, S. J., McCague, R., et al. (2002a). A thermostable l-aminoacylase from Thermococcus litoralis: cloning, overexpression, characterization, and applications in biotransformations. Extremophiles 6, 111-122. doi:10.1007/s007920100230
51. Toogood, H. S., Taylor, I. N., Brown, R. C., Taylor, S. J. C., McCague, R., and Littlechild, J. A. (2002b). Immobilisation of the thermostable l-aminoacylase from Thermococcus litoralis to generate a reusable industrial biocatalyst. Biocatal. Biotransformation 20, 241-249. doi:10.1080/10242420290029472
52. Trincone, A. (2011). Marine biocatalysts: enzymatic features and applications. Mar. Drugs 9, 478-499. doi:10.3390/md9040478
53. Van der Ploeg, J., Van Hall, G., and Janssen, D. B. (1991). Characterization of the haloacid dehalogenase from Xanthobacter autotrophicus GJ10 and sequencing of the dhlB gene. J. Bacteriol. 173, 7925-7933.
54. Widersten, M., Gurell, A., and Lindberg, D. (2010). Structure-function relationships of epoxide hydrolases and their potential use in biocatalysis. Biochim. Biophys. Acta 1800, 316-326. doi:10.1016/j.bbagen.2009.11.014
55. Yin, D. L., Bernhardt, P., Morley, K. L., Jiang, Y., Cheeseman, J. D., Purpero, V., et al. (2010). Switching catalysis from hydrolysis to perhydrolysis in P. fluorescens esterase. Biochemistry 49, 1931-1942. doi:10.1021/bi9021268