Skip to main content
Disciplines
Automotive Business IT + Informatics Construction + Real Estate Electrical Engineering + Electronics Energy + Sustainability Insurance + Risk Finance + Banking Management + Leadership Marketing + Sales Mechanical Engineering + Materials
Events
DE
EN
Books
Journals
Topic Page
Marketing
Start single access now
Access for companies
EXTENDED SEARCH
Log in
Top
Published in:
Cover of the book

2011 | OriginalPaper | Chapter

1. Introduction and Background Information

Author : Prof. Dr. Kurt Faber

Published in: Biotransformations in Organic Chemistry

Publisher: Springer Berlin Heidelberg

Log in

Activate our intelligent search to find suitable subject content or patents.

search-config
loading …

Abstract

>Any exponents of classical organic chemistry might probably hesitate to consider a biochemical solution for one of their synthetic problems. This would be due to the fact, that biological systems would have to be handled. Where the growth and maintenance of whole microorganisms is concerned, such hesitation is probably justified. In order to save endless frustrations, close collaboration with a microbiologist or a biochemist is highly recommended to set up and use fermentation systems [1, 2]. On the other hand, isolated enzymes (which may be obtained increasingly easily from commercial sources either in a crude or partially purified form) can be handled like any other chemical catalyst.

Dont have a licence yet? Then find out more about our products and how to get one now:

Springer Professional "Wirtschaft+Technik"

Online-Abonnement

Mit Springer Professional "Wirtschaft+Technik" erhalten Sie Zugriff auf:

  • über 102.000 Bücher
  • über 537 Zeitschriften

aus folgenden Fachgebieten:

  • Automobil + Motoren
  • Bauwesen + Immobilien
  • Business IT + Informatik
  • Elektrotechnik + Elektronik
  • Energie + Nachhaltigkeit
  • Finance + Banking
  • Management + Führung
  • Marketing + Vertrieb
  • Maschinenbau + Werkstoffe
  • Versicherung + Risiko

Jetzt Wissensvorsprung sichern!

inform now

Springer Professional "Technik"

Online-Abonnement

Mit Springer Professional "Technik" erhalten Sie Zugriff auf:

  • über 67.000 Bücher
  • über 390 Zeitschriften

aus folgenden Fachgebieten:

  • Automobil + Motoren
  • Bauwesen + Immobilien
  • Business IT + Informatik
  • Elektrotechnik + Elektronik
  • Energie + Nachhaltigkeit
  • Maschinenbau + Werkstoffe




 

Jetzt Wissensvorsprung sichern!

inform now
next chapter Biocatalytic Applications
Footnotes
1
The majority of commonly used enzyme preparations are available through chemical suppliers. Nevertheless, for economic reasons, it may be worth contacting an enzyme producer directly, in particular if bulk quantities are required. For a list of enzyme suppliers see the appendix (Chap. 5).
 
2
After all, the exact structure of a Grignard-reagent is still unknown.
 
3
Other sectors of biotechnology have been defined as ‘Red’ (biotechnology in medicine), ‘Green’ (biotechnology for agriculture and plant biotech) and ‘Blue’ (marine biotechnology), http://​www.​EuropaBio.​org, http://​www.​bio.​org
 
4
Only proteases are exceptions to this rule for obvious reasons.
 
5
For exceptional D-chiral proteins see [61].
 
6
According to a BBC-report, the sale of rac-thalidomide to third-world countries has been resumed in mid-1996!
 
7
For a convenient method for controlling the substrate concentration see [85].
 
8
E. coli has ~4,500 genes and Saccharomyces cerevisiae (baker's yeast) ~6,500 genes.
 
9
The amino acid sequence of a protein is generally referred to as its ‘primary structure’, whereas the three-dimensional arrangement of the polyamide chain (the ‘backbone’) in space is called the ‘secondary structure’. The ‘tertiary structure’ includes the arrangement of all atoms, i.e., the amino acid side chains are included, whereas the ‘quarternary structure’ describes the aggregation of several protein molecules to form oligomers.
 
10
Water bound to an enzyme's surface exhibits a (formal) freezing point of about –20°C.
 
11
PDB entry 3icw, courtesy of U. Wagner.
 
12
Also called London forces.
 
13
Also called Coulomb interactions.
 
14
‘To use a picture I want to say that enzyme and glucoside must go together like key and lock in order to exert a chemical effect upon each other’, see [94] p. 2992.
 
15
‘A precise orientation of catalytic groups is required for enzyme action; the substrate may cause an appreciable change in the three-dimensional relationship of the amino acids at the active site, and the changes in protein structure caused by a substrate will bring the catalytic groups into proper orientation for reaction, whereas a non-substrate will not.’ See [96].
 
16
Conformational changes are differentiated into hinge- and shear-type movements [98].
 
17
A ‘record’ of rate acceleration factor of 1014 has been reported. See [100].
 
18
This phenomenon is denoted as ‘electrostatic catalysis’ and was coined as ‘Circe-effect’ by WP Jencks.
 
19
By average, enzymes are 100 times bigger than related chemical catalysts.
 
20
It is important to note that the (modest) pKa of typical amino acid side chains, such as –NH3 + or –CO2– can be substantially altered up to 2–3 pKa-units through neighboring groups within the enzyme environment. As a consequence, the (approximately neutral) imidazole moiety of His can act as strong acid or base, depending on its molecular environment.
 
21
The following rationale was adapted from [111].
 
22
The individual reaction rates v A and v B correspond to v A = (k cat/K M)A · [Enz] · [A] and v B = (k cat/K M)B · [Enz] · [B], respectively, according to Michaelis-Menten kinetics. The ratio of the individual reaction rates of enantiomers is an important parameter for the description of the enantioselectivity of a reaction: v A/v B = E (‘Enantiomeric Ratio’, see Sect. 2.1.1).
 
23
Based on the biotransformation database of Kroutil and Faber (2010) ~14,000 entries.
 
24
For a discussion of the pitfalls associated with TONs and TOFs see [124].
 
25
Assuming that each catalyst molecule has a single active site. For enzymes obeying Michaelis-Menten kinetics the TON is equal to 1/k cat.
 
26
A ‘cofactor’ is tightly bound to an enzyme (e.g., FAD), whereas a ‘coenzyme’ can dissociate into the medium (e.g., NADH). In practice, however, this distinction is not always made in a consequent manner.
 
Literature
1.
Goodhue CT (1982) Microb. Transform. Bioact. Compd. 1: 9
2.
Roberts SM, Turner NJ, Willetts AJ, Turner MK (1995) Introduction to Biocatalysis Using Enzymes and Micro-organisms. Cambridge University Press, Cambridge
3.
Baross JA, Deming JW (1983) Nature 303: 423
4.
Hough DW, Danson MJ (1999) Curr. Opinion Chem. Biol. 3: 39
5.
6.
Feyerabend P (1988) Against Method. Verso, London
7.
Laane C, Boeren S, Vos K, Veeger C (1987) Biotechnol. Bioeng. 30: 81
8.
Carrea G, Ottolina G, Riva S (1995) Trends Biotechnol. 13: 63
9.
Bell G, Halling PJ, Moore BD, Partridge J, Rees DG (1995) Trends Biotechnol. 13: 468
10.
Koskinen AMP, Klibanov AM (eds) (1996) Enzymatic Reactions in Organic Media. Blackie Academic & Professional, London
11.
Gutman AL, Shapira M (1995) Synthetic Applications of Enzymatic Reactions in Organic Solvents. In: Fiechter A (ed) Adv. Biochem. Eng. Biotechnol., vol. 52, pp 87–128, Springer, Berlin Heidelberg New York
12.
Wolfenden R, Snider MJ (2001) Acc. Chem. Res. 34: 938
13.
14.
Zechel DL, Withers SG (2000) Acc. Chem. Res. 33: 11
15.
Garcia-Junceda E (2008) Multi-step Enzyme Catalysis. Wiley-VCH, Weinheim
16.
Sih CJ, Abushanab E, Jones JB (1977) Ann. Rep. Med. Chem. 12: 298
17.
Boland W, Frößl C, Lorenz M (1991) Synthesis 1049
18.
Schmidt-Kastner G, Egerer P (1984) Amino Acids and Peptides. In: Kieslich K (ed) Biotechnology. Verlag Chemie, Weinheim, vol 6a, pp 387–419
19.
Gutman AL, Zuobi K, Guibe-Jampel E (1990) Tetrahedron Lett. 31: 2037
20.
Taylor SJC, Sutherland AG, Lee C, Wisdom R, Thomas S, Roberts SM, Evans C (1990) J. Chem. Soc., Chem. Commun. 1120
21.
Zhang D, Poulter CD (1993) J. Am. Chem. Soc. 115: 1270
22.
Yamamoto Y, Yamamoto K, Nishioka T, Oda J (1988) Agric. Biol. Chem. 52: 3087
23.
Leak DJ, Aikens PJ, Seyed-Mahmoudian M (1992) Trends Biotechnol. 10: 256
24.
Nagasawa T, Yamada H (1989) Trends Biotechnol. 7: 153
25.
Mansuy D, Battoni P (1989) Alkane Functionalization by Cytochromes P450 and by Model Systems Using O2 or H2O2. In: Hill CL (ed) Activation and Functionalization of Alkanes. Wiley, New York
26.
Lemiere GL, Lepoivre JA, Alderweireldt FC (1985) Tetrahedron Lett. 26: 4527
27.
Phillips RS, May SW (1981) Enzyme Microb. Technol. 3: 9
28.
May SW (1979) Enzyme Microb. Technol. 1: 15
29.
Boyd DR, Dorrity MRJ, Hand MV, Malone JF, Sharma ND, Dalton H, Gray DJ, Sheldrake GN (1991) J. Am. Chem. Soc. 113: 667
30.
Walsh CT, Chen YCJ (1988) Angew. Chem., Int. Ed. 27: 333
31.
32.
Koszelewski D, Lavandera I, Clay D, Guebitz G, Rozzell D, Kroutil W (2010) Angew. Chem., Int. Ed. 47: 9337
33.
Findeis MH, Whitesides GM (1987) J. Org. Chem. 52: 2838
34.
Akhtar M, Botting NB, Cohen MA, Gani D (1987) Tetrahedron 43: 5899
35.
Effenberger F, Ziegler T (1987) Angew. Chem., Int. Ed. 26: 458
36.
Neidleman SL, Geigert J (1986) Biohalogenation: Principles, Basic Roles and Applications. Ellis Horwood, Chichester
37.
Stecher H, Twengg M, Ueberbacher BJ, Remler P, Schwab H, Griengl H, Gruber-Khadjawi M (2009) Angew. Chem., Int. Ed. 48: 9546
38.
Buist PH, Dimnik GP (1986) Tetrahedron Lett. 27: 1457
39.
Aresta M, Quaranta E, Liberio R, Dileo C, Tommasi I (1998) Tetrahedron 54: 8841
40.
Ohta H (1999) Adv. Biochem. Eng. Biotechnol. 63: 1
41.
Schwab JM, Henderson BS (1990) Chem. Rev. 90: 1203
42.
Fuganti C, Grasselli P (1988) Baker's Yeast Mediated Synthesis of Natural Products. In: Whitaker JR, Sonnet PE (eds) Biocatalysis in Agricultural Biotechnology, ACS Symposium Series, vol 389, pp 359–370
43.
Toone EJ, Simon ES, Bednarski MD, Whitesides GM (1989) Tetrahedron 45: 5365
44.
Kitazume T, Ikeya T, Murata K (1986) J. Chem. Soc., Chem. Commun. 1331
45.
Pohl M, Lingen B, Müller M (2002) Chem. Eur. J. 8: 5288
46.
Durchschein K, Ferreira-da Silva B, Wallner S, Macheroux P, Kroutil W, Glueck SM, Faber K (2010) Green Chem. 12: 616
47.
Williams RM (2002) Chem. Pharm. Bull. 50: 711
48.
Oikawa H, Katayama K, Suzuki Y, Ichihara A (1995) J. Chem. Soc., Chem. Commun. 1321
49.
50.
Abe I, Rohmer M, Prestwich GD (1993) Chem. Rev. 93: 2189
51.
Ganem B (1996) Angew. Chem., Int. Ed. 35: 936
52.
Bornscheuer UT, Kazlauskas RJ (2004) Angew. Chem., Int. Ed. 43: 6032
53.
Hult K, Berglund P (2007) Trends Biotechnol. 25: 231
54.
55.
Khersonsky O, Roodveldt C, Tawfik DS (2006) Curr. Opinion Chem. Biol. 10: 498
56.
O'Brien PJ, Herschlag D (1999) Chem. Biol. 6: R91
57.
Kazlauskas RJ (2005) Curr. Opinion Chem. Biol. 9: 195
58.
Penning TM, Jez JM (2001) Chem. Rev. 101: 3027
59.
Sweers HM, Wong CH (1986) J. Am. Chem. Soc. 108: 6421
60.
Bashir NB, Phythian SJ, Reason AJ, Roberts SM (1995) J. Chem. Soc., Perkin Trans. 1, 2203
61.
Jung G (1992) Angew. Chem., Int. Ed. 31: 1457
62.
Sih CJ, Wu SH (1989) Topics Stereochem. 19: 63
63.
Fischer E (1898) Zeitschr. physiol. Chem. 26: 60
64.
65.
66.
Ariens EJ (1988) Stereospecificity of Bioactive Agents. In: Ariens EJ, van Rensen JJS, Welling W (eds) Stereoselectivity of Pesticides. Elsevier, Amsterdam, pp 39–108
67.
Crosby J (1997) Introduction. In: Collins AN, Sheldrake GN, Crosby J (eds) Chirality in Industry II, pp 1–10, Wiley, Chichester
68.
Millership JS, Fitzpatrick A (1993) Chirality 5: 573
69.
Borman S (1992) Chem. Eng. News, June 15: 5
70.
71.
US Food & Drug Administration (2004) Pharmaceutical Current Good Manufacturing Practices (cGMPs) for the 21st Century – a Risk-Based Approach: Final Report
72.
Farina V, Reeves JT, Senanayake CH, Song JJ (2006) Chem. Rev. 106: 2734
73.
Agranat H, Caner H, Caldwell J (2002) Nat. Rev. Drug Discov. 1: 753
74.
Sheldon RA (1993) Chirotechnology. Marcel Dekker, New York
75.
Collins AN, Sheldrake GN, Crosby J (eds) (1992, 1997) Chirality in Industry, 2 vols. Wiley, Chichester
76.
Morrison JD (ed) (1985) Chiral catalysis. In: Asymmetric Synthesis, vol 5. Academic Press, London
77.
Hanessian S (1983) Total Synthesis of Natural Products: the ‘Chiron’ Approach. Pergamon Press, Oxford
78.
Scott JW (1984) Readily available chiral carbon fragments and their use in synthesis. In: Morrison JD, Scott JW (eds) Asymmetric Synthesis. Academic Press, New York, vol 4, pp 1-226
79.
Margolin AL (1993) Enzyme Microb. Technol. 15: 266
80.
Mugford P, Wagner U, Jiang Y, Faber K, Kazlauskas R (2008) Angew. Chem. Int. Ed. 47: 8782
81.
Phillips RS (1996) Trends Biotechnol. 14: 13
82.
Schuster M, Aaviksaar A, Jakubke HD (1990) Tetrahedron 46: 8093
83.
84.
85.
D'Arrigo P, Fuganti C, Pedrocchi-Fantoni G, Servi S (1998) Tetrahedron 54: 15017
86.
87.
Cooke R, Kuntz ID (1974) Ann. Rev. Biophys. Bioeng. 3: 95
88.
Ahern TJ, Klibanov AM (1985) Science 228: 1280
89.
Adams MWW, Kelly RM (1998) Trends Biotechnol. 16: 329
90.
Mozhaev VV, Martinek K (1984) Enzyme Microb. Technol. 6: 50
91.
Jencks WP (1969) Catalysis in Chemistry and Enzymology. McGraw-Hill, New York
92.
Fersht A (1985) Enzyme Structure and Mechanism, 2nd edn. Freeman, New York
93.
Walsh C (ed) (1979) Enzymatic Reaction Mechanism. Freeman, San Francisco
94.
Fischer E (1894) Ber. dtsch. chem. Ges. 27: 2985
95.
Lichtenthaler FW (2003) Angew. Chem., Int. Ed. 33: 2364
96.
Koshland DE (1958) Proc. Natl. Acad. Sci. USA 44: 98
97.
Koshland DE, Neet KE (1968) Ann. Rev. Biochem. 37: 359
98.
Gerstein M, Lesk AM, Chotia C (1994) Biochemistry 33: 6739
99.
100.
101.
Warshel A, Aqvist J, Creighton S (1989) Proc. Natl. Acad. Sci. USA 86: 5820
102.
103.
Ottosson J, Rotticci-Mulder JC, Rotticci D, Hult K (2001) Protein Sci. 10: 1769
104.
105.
Ottosson J, Fransson L, Hult K (2002) Protein Sci. 11: 1462
106.
107.
Warshel A, Sharma PK, Kato M, Xiang Y, Liu H, Olsson MHM (2006) Chem. Rev. 106: 3210
108.
Garcia-Viloca M, Gao J, Karplus M, Truhlar DG (2004) Science 303: 186
109.
Masgrau L, Roujeinikova A, Johanissen LO, Hothi P, Basran J, Ranaghan KE, Mulholland AJ, Sutcliffe MJ, Scrutton NS, Leys D (2006) Science 312: 237
110.
111.
Jones JB (1976) Biochemical Systems in Organic Chemistry: Concepts, Principles and Opportunities. In: Jones JB, Sih CJ, Perlman D (eds) Applications of Biochemical Systems in Organic Chemistry, part I. Wiley, New York, pp 1–46
112.
Cipiciani A, Fringuelli F, Mancini V, Piermatti O, Scappini AM, Ruzziconi R (1997) Tetrahedron 53: 11853
113.
Kielbasinski P, Goralczyk P, Mikolajczyk M, Wieczorek MW, Majzner WR (1998) Tetrahedron: Asymmetry 9: 2641
114.
115.
116.
117.
Wolfenden R (1999) Bioorg. Med. Chem. 7: 647
118.
International Union of Biochemistry and Molecular Biology (1992) Enzyme Nomenclature. Academic Press, New York
119.
Schomburg D (ed) (2002) Enzyme Handbook. Springer, Heidelberg
120.
Appel RD, Bairoch A, Hochstrasser DF (1994) Trends Biochem. Sci. 19: 258
121.
122.
123.
Crout DHG, Christen M (1989) Biotransformations in Organic Synthesis. In: Scheffold R (ed) Modern Synthetic Methods, vol 5. pp 1–114
124.
Farina V (2004) Adv. Synth. Catal. 346: 1553
125.
Behr A (2007) Angewandte Homogene Katalyse. Wiley-VCH, Weinheim, p 40
126.
Mahler HR, Cordes HE (1971) Biological Chemistry, 2nd ed. Harper & Row, London
127.
Simon H, Bader J, Günther H, Neumann S, Thanos J (1985) Angew. Chem., Int. Ed. 24: 539
128.
Chaplin MF, Bucke C (1990) Enzyme Technology. Cambridge University Press, New York
129.
White JS, White DC (1997) Source Book of Enzymes. CRC Press, Boca Raton
130.
Spradlin JE (1989) Tailoring Enzymes for Food Processing, in: Whitaker JR, Sonnet PE(eds) ACS Symposium Series, vol 389, p 24, J. Am. Chem. Soc., Washington
Metadata
Title
Introduction and Background Information
Author
Prof. Dr. Kurt Faber
Copyright Year
2011
Publisher
Springer Berlin Heidelberg
Book
Biotransformations in Organic Chemistry

Print ISBN: 978-3-642-17392-9

Electronic ISBN: 978-3-642-17393-6

Copyright Year: 2011

DOI
https://doi.org/10.1007/978-3-642-17393-6_1

Premium Partners

    Image Credits