2.3. 2 Addition of Water to C=C Bonds
Book
Editors: Faber, K.; Fessner, W.-D.; Turner, N. J.
Title: Biocatalysis Organic Synthesis 2
Print ISBN: 9783131741615; Online ISBN: 9783131975317; Book DOI: 10.1055/b-003-125813
1st edition © 2015. Thieme. All rights reserved.
Georg Thieme Verlag KG, Stuttgart
Subjects: Organic Chemistry
Science of Synthesis Reference Libraries
Parent publication
Title: Science of Synthesis
DOI: 10.1055/b-00000101
Type: Multivolume Edition
Abstract
![](https://www.thieme-connect.de/media/10.1055-b-003-125813/thumbnails/a_210cch.jpg)
While chemists struggle to find efficient methods to perform the asymmetric addition of water, nature employs countless enzymes (called hydratases or hydro-lyases) to perform this reaction using substrates with both activated and nonactivated double bonds. However, compared to the vast number of hydratases involved in metabolic pathways in nature, only a few are described for their use in organic synthesis. Nevertheless, their potential in asymmetric catalysis has been recognized and some hydratases are used on a large scale in industrial processes. Since hydratases perform the addition of water, water is used as both a solvent and a reagent, opening up a very efficient and green route to both secondary and tertiary alcohols. This chapter focuses on hydratases that catalyze interesting reactions and are tested beyond their biochemical characterization.
Key words
acetylene hydratase - aconitase - carotenoid hydratases - citraconase - fumarase - hydratase - hydratase–tautomerase bifunctionality - hydro-lyase - kievitone hydratase - limonene hydratase - linalool dehydrogenase–isomerase - malease - oleate hydratase - phaseollidin hydratase - urocanase - water addition- 5 Hahn H.-D, Dämbkes G, Rupprich N, Bahl H, Frey GD. Ullmannʼs Encyclopedia of Industrial Chemistry. Wiley-VCH; Weinheim, Germany 2013
- 6 Falbe J, Bahrmann H, Lipps W, Mayer D, Frey GD. Ullmannʼs Encyclopedia of Industrial Chemistry. Wiley-VCH; Weinheim, Germany 2013
- 7 Sheldon RA, Arends IWCE, Hanefeld U. Green Chemistry and Catalysis. Wiley-VCH; Weinheim, Germany 2007
- 10 van der Werf MJ, van den Tweel WJJ, Kamphuis J, Hartmans S, de Bont JAM. Trends Biotechnol. 1994; 12: 95
- 11 van Leeuwen BNM, van der Wulp AM, Duijnstee I, van Maris AJA, Straathof AJJ. Appl. Microbiol. Biotechnol. 2012; 93: 1377
- 13 Mohrig JR, Moerke KA, Cloutier DL, Lane BD, Person EC, Onasch TB. Science (Washington, D. C.) 1995; 269: 527
- 26 Niehaus Jr WG, Kisic A, Torkelson A, Bednarczyk DJ, Schroepfer Jr GJ. J. Biol. Chem. 1970; 245: 3790
- 31 Gocho S, Tabogami N, Inagaki M, Kawabata C, Komai T. Biosci., Biotechnol., Biochem. 1995; 59: 1571
- 37 Song J.-W, Jeon E.-Y, Song D.-H, Jang H.-Y, Bornscheuer UT, Oh D.-K, Park J.-B. Angew. Chem. 2013; 125: 2594 Angew. Chem. Int. Ed. 2013; 52: 2534
- 50 Pearlman PS, Chen C, Botes AL, Conradie AVE. US 2013 0 189 753, 2013 Chem. Abstr.. 2013 158 288625
- 54 Bicas JL, Barros FFC, Wagner R, Godoy HT, Pastore GM. J. Ind. Microbiol. Biotechnol. 2008; 35: 1061
- 57 Rottava I, Toniazzo G, Cortina PF, Martello E, Grando CE, Lerin LA, Treichel H, Mossi AJ, de Oliveira D, Cansian RL, Antunes OAC, Oestreicher EG. LWT–Food Sci. Technol. 2010; 43: 1128
- 62 Savithiry N, Cheong T, Oriel P, Biotechnology for Fuels and Chemicals Davison BH, Wyman CE, Finkelstein M. Humana New York 1997; 63–65. 213
- 64 Pescheck M, Mirata MA, Brauer B, Krings U, Berger RG, Schrader J. J. Ind. Microbiol. Biotechnol. 2009; 36: 827
- 68 Seiffert GB, Ullmann GM, Messerschmidt A, Schink B, Kroneck PMH, Einsle O. Proc. Natl. Acad. Sci. U. S. A. 2007; 104: 3073
- 69 Einsle O, Niessen H, Abt DJ, Seiffert G, Schink B, Huber R, Messerschmidt A, Kroneck PMH. Acta Crystallogr., Sect. F 2005; 61: 299
- 75 Span I, Wang K, Wang W, Zhang Y, Bacher A, Eisenreich W, Li K, Schulz C, Oldfield E, Groll M. Nature Commun. 2012; 3: 1042
- 79 Woods SA, Schwartzbach SD, Guest JR. Biochim. Biophys. Acta, Protein Struct. Mol. Enzymol. 1988; 954: 14
- 84 Weaver T, Lees M, Zaitsev V, Zaitseva I, Duke E, Lindley P, McSweeny S, Svensson A, Keruchenko J, Keruchenko I, Gladilin K, Banaszak L. J. Mol. Biol. 1998; 280: 431
- 85 Yang J, Wang Y, Woolridge EM, Arora V, Petsko GA, Kozarich JW, Ringe D. Biochemistry 2004; 43: 10424
- 106 Rao MRR, Subramanian SS, Rahatekar HI, Paranjape SV. Biochem. Biophys. Res. Commun. 1963; 12: 78
- 110 Williams CH, Stillman TJ, Barynin VV, Sedelnikova SE, Tang Y, Green J, Guest JR, Artymiuk PJ. Nature Struct. Mol. Biol. 2002; 9: 447
- 112 Kennedy MC, Mende-Mueller L, Blondin GA, Beinert H. Proc. Natl. Acad. Sci. U. S. A. 1992; 89: 11730
- 113 Haile DJ, Rouault TA, Harford JB, Kennedy MC, Blondin GA, Beinert H, Klausner RD. Proc. Natl. Acad. Sci. U. S. A. 1992; 89: 11735
- 117 Grueninger D, Treiber N, Ziegler MOP, Koetter JWA, Schulze M.-S, Schulz GE. Science (Washington, D. C.) 2008; 319: 206
- 121 Schubert C, Zhao Y, Shin J.-H, Rétey J. Angew. Chem. 1994; 106: 1331 Angew. Chem. Int. Ed. Engl. 1994; 33: 1279
- 126 Poelarends GJ, Serrano H, Johnson WH, Hoffman DW, Whitman CP. J. Am. Chem. Soc. 2004; 126: 15658
- 127 Almrud JJ, Poelarends GJ, Johnson WH, Serrano H, Hackert ML, Whitman CP. Biochemistry 2005; 44: 14818
- 134 Bhaumik P, Koski MK, Glumoff T, Hiltunen JK, Wierenga RK. Curr. Opin. Struct. Biol. 2005; 15: 621
- 135 Bell AF, Feng Y, Hofstein HA, Parikh S, Wu J, Rudolph MJ, Kisker C, Whitty A, Tonge PJ. Chem. Biol. 2002; 9: 1247
- 142 Hasegawa J, Ogura M, Kanema H, Noda N, Kawaharada H, Watanabe K. J. Ferment. Technol. 1982; 60: 501
- 161 Masai E, Harada K, Peng X, Kitayama H, Katayama Y, Fukuda M. Appl. Environ. Microbiol. 2002; 68: 4416
- 162 Leonard PM, Brzozowski AM, Lebedev A, Marshall CM, Smith DJ, Verma CS, Walton NJ, Grogan G. Acta Crystallogr., Sect. D 2006; 62: 1494
- 163 Leonard PM, Marshall CM, Dodson EJ, Walton NJ, Grogan G. Acta Crystallogr., Sect. D 2004; 60: 2343
- 164 Bennett JP, Bertin L, Moulton B, Fairlamb IJS, Brzozowski AM, Walton NJ, Grogan G. Biochem. J. 2008; 414: 281