Carbon-carbon coupling in biotransformation

Current Opinion in Biotechnology

Volumn 14, Issue 6, 2003, Pages 570-576

  Breuer, Michael ^a   Hauer, Bernhard ^a  

^a Fine Chemicals and Biocatalysis Research   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ACETALDEHYDE ALDOLASE; CARBON; CLOPIDOGREL; COCARBOXYLASE; DEOXYRIBOSEPHOSPHATE ALDOLASE; DIHYDROXYACETONE PHOSPHATE; ENZYME; EPOTHILONE DERIVATIVE; FRUCTOSE BISPHOSPHATE ALDOLASE; HYDROXYNITRILE LYASE; LYASE; PYRIDOXAL 5 PHOSPHATE; UNCLASSIFIED DRUG;

BIOCATALYST; BIOTRANSFORMATION; CARBOHYDRATE METABOLISM; CATALYSIS; CATALYST; CLAISEN CONDENSATION; DIELS ALDER REACTION; DRUG SYNTHESIS; ENZYME ENGINEERING; ENZYME MECHANISM; ESCHERICHIA COLI; PRIORITY JOURNAL; PROTEIN ENGINEERING; REVIEW; STEREOCHEMISTRY;

BETULACEAE; ESCHERICHIA COLI;

EID: 0344255749     PISSN: 09581669     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.copbio.2003.10.004     Document Type: Review

References (39)

1. Schmid A., Dordick J.S., Hauer B., Kiener A., Wubbolts M.G., Witholt B. Industrial biocatalysis today and tomorrow. Nature. 409:2001;258-268 This paper gives a review on biocatalysis from the industrial point of view.
2. Fessner W.D., Helaine V. Biocatalytic synthesis of hydroxylated natural products using aldolases and related enzymes. Curr. Opin. Biotechnol. 12:2001;574-586.
3. 2Zn/Linked-BINOL complex. J. Am. Chem. Soc. 125:2003;2169-2178.
4. Wagner J., Lerner R.A., Barbas C.F. III Efficient aldolase catalytic antibodies that use the enamine mechanism of natural enzymes. Science. 270:1995;1797-1800.
5. Hertweck C. Aldolase antibody 38C2: a biocatalyst expanding the scope of enzymatic transformations. J. Prakt. Chem. 342:2000;832-835.
6. Branneby C., Carlqvist P., Magnusson A., Hult K., Brinck T., Berglund P. Carbon-carbon bonds by hydrolytic enzymes. J. Am. Chem. Soc. 125:2003;874-875 This work is a good example to show the plasticity of proteins as catalysts. Minor changes in the set-up of the active site modified the catalytic scope significantly. It also shows the power of rational protein engineering with an α/β-hydrolase.
7. Machajewski T.D., Wong C.H. The catalytic asymmetric aldol reaction. Angew. Chem. Int. Ed. Engl. 39:2000;1352-1375.
8. Schoevaart R., van Rantwijk F., Sheldon R.A. A four-step enzymatic cascade for the one-pot synthesis of non-natural carbohydrates from glycerol. J. Org. Chem. 65:2000;6940-6943.
9. Schoevaart R., van Rantwijk F., Sheldon R.A. Facile enzymatic aldol reactions with dihydroxyacetone in the presence of arsenate. J. Org. Chem. 66:2001;4559-4562 Arsenate esters are used as an elegant bypass around the substrate limitations of DHAP-dependent aldolases.
10. Schürmann M., Schürmann M., Sprenger G.A. Fructose 6-phosphate aldolase and 1-deoxy-D-xylulose 5-phosphate synthase from Escherichia coli as tools in enzymatic synthesis of 1-deoxysugars. J. Mol. Catal, B Enzym. 19:2002;247-252.
11. Fong S., Machajewski T.D., Mak C.C., Wong C. Directed evolution of D-2-keto-3-deoxy-6-phosphogluconate aldolase to new variants for the efficient synthesis of D- and L-sugars. Chem. Biol. 7:2000;873-883.
12. Liu J.J., Wong C.H. Aldolase-catalyzed asymmetric synthesis of novel pyranose synthons as a new entry to heterocycles and epothilones. Angew. Chem. Int. Ed. Engl. 41:2002;1404-1407.
13. Murphy C.D., O'Hagan D., Schaffrath C. Identification of a PLP-dependent threonine transaldolase: a novel enzyme involved in 4-fluorothreonine biosynthesis in Streptomyces cattleya. Angew. Chem. Int. Ed. Engl. 40:2001;4479-4481.
14. Pohl M., Lingen B., Müller M. Thiamin-diphosphate-dependent enzymes: new aspects of asymmetric C-C bond formation. Chemistry. 8:2002;5288-5295 A comprehensive review on ketolases. Asymmetric syntheses of chiral building blocks using thiamine diphosphate dependent enzymes are covered.
15. Ward O.P., Singh A. Enzymatic asymmetric synthesis by decarboxylases. Curr. Opin. Biotechnol. 11:2000;520-526.
16. Breuer M, Hauer B, Friedrich T: Novel pyruvate decarboxylase, production and use thereof. 2003, Patent application No.: WO 03/020921 A2.
17. Rosche B., Leksawasdi N., Sandford V., Breuer M., Hauer B., Rogers P.L. Enzymatic (R)-phenylacetylcarbinol production in benzaldehyde emulsions. Appl. Microbiol. Biotechnol. 60:2002;94-100.
18. Hauer B, Breuer M, Rogers PL, Sandford V, Rosche B: Process for production of R-phenylacetylcarbinol by an enzymatic process in a two-phase system. 2003, Patent application No: WO 03/020942.
19. Miyazaki M., Shibue M., Ogino K., Nakamura H., Maeda H. Enzymatic synthesis of pyruvic acid from acetaldehyde and carbon dioxide. Chem. Commun. (Camb.). 21:2001;1800-1801 The reverse reaction of pyruvate decarboxylase is a simple but intriguing way to produce pyruvate from cheap starting materials.
20. Miyazaki M, Maeda H, Nakamura H, Yamada N, Shibata M: Carboxylic acids manufacture with decarboxylase from carbon dioxide. 2003, Patent Application No: WO 02/095046 A1.
21. Kricheldorf H.R. Syntheses and application of polylactides. Chemosphere. 43:2001;49-54.
22. Iding H., Dünnwald T., Greiner L., Liese A., Müller M., Siegert P., Grötzinger J., Demir A.S., Pohl M. Benzoylformate decarboxylase from Pseudomonas putida as stable catalyst for the synthesis of chiral 2-hydroxy ketones. Chemistry. 6:2000;1483-1495.
23. Effenberger F., Förster S., Wajant H. Hydroxynitrile lyases in stereoselective catalysis. Curr. Opin. Biotechnol. 11:2000;532-539.
24. Johnson D.V., Zabelinskaja-Mackova A.A., Griengl H. Oxynitrilases for asymmetric C-C bond formation. Curr. Opin. Chem. Biol. 4:2000;103-109.
25. Gruber K. Elucidation of the mode of substrate binding to hydroxynitrile lyase from Hevea brasiliensis. Proteins. 44:2001;26-31.
26. Dreveny I., Kratky C., Gruber K. The active site of hydroxynitrile lyase from Prunus amygdalus: modeling studies provide new insights into the mechanism of cyanogenesis. Protein Sci. 11:2002;292-300.
27. Lauble H., Miehlich B., Förster S., Wajant H., Effenberger F. Crystal structure of hydroxynitrile lyase from Sorghum bicolor in complex with the inhibitor benzoic acid: a novel cyanogenic enzyme. Biochemistry. 41:2002;12043-12050.
28. Lauble H., Miehlich B., Förster S., Wajant H., Effenberger F. Mechanistic aspects of cyanogenesis from active-site mutant Ser80Ala of hydroxynitrile lyase from Manihot esculenta in complex with acetone cyanohydrin. Protein Sci. 10:2001;1015-1022.
29. Yan G., Cheng S., Zhao G., Wu S., Liu Y., Sun W. A single residual replacement improves the folding and stability of recombinant cassava hydroxynitrile lyase in E. coli. Biotechnol. Lett. 25:2003;1041-1047.
30. Bühler H., Effenberger F., Förster S., Roos J., Wajant H. Substrate specificity of mutants of the hydroxynitrile lyase from Manihot esculenta. Chembiochem. 4:2003;211-216.
31. Heath R.J., Rock C.O. The Claisen condensation in biology. Nat. Prod. Rep. 19:2002;581-596 This extensive review summarises all relevant aspects of enzymes that catalyse Claisen-analogous reactions in nature.
32. Katayama K., Kobayashi T., Oikawa H., Honma M., Ichihara A. Enzymatic activity and partial purification of solanapyrone synthase: first enzyme catalyzing Diels-Alder reaction. Biochim. Biophys. Acta. 1384:1998;387-395.
33. Auclair K., Sutherland A., Kennedy J., Witter D.J., van den Heever J.P., Hutchinson C.R., Vederas J.C. Lovastatin nonaketide synthase catalyzes an intramolecular Diels-Alder reaction of a substrate analogue. J. Am. Chem. Soc. 122:2003;11519-11520.
34. Watanabe K., Mie T., Ichihara A., Oikawa H., Honma M. Detailed reaction mechanism of macrophomate synthase. Extraordinary enzyme catalyzing five-step transformation from 2-pyrones to benzoates. J. Biol. Chem. 275:2000;38393-38401.
35. Tarasow T.M., Eaton B.E. The Diels-Alder reaction and biopolymer catalysis. Cell Mol. Life Sci. 55:1999;1463-1472.
36. Jäschke A. RNA-catalyzed carbon-carbon bond formation. Biol. Chem. 382:2001;1321-1325.
37. Tarasow T.M., Tarasow S.L., Eaton B.E. RNA-catalysed carbon-carbon bond formation. Nature. 389:1997;54-57.
38. Seelig B., Jäschke A. A small catalytic RNA motif with Diels-Alderase activity. Chem. Biol. 6:1999;167-176.
39. Ose T., Watanabe K., Mie T., Honma M., Watanabe H., Yao M., Oikawa H., Tanaka I. Insight into a natural Diels-Alder reaction from the structure of macrophomate synthase. Nature. 422:2003;185-189.