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Chapter 4 : Microbial Diversity: Catabolism of Organic Compounds Is Broadly Distributed

Authors: Lawrence P. Wackett1, C. Douglas Hershberger2
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Affiliations: 1: Department of Biochemistry, Molecular Biology & Biophysics and Biological Process Technology Institute, University of Minnesota, St. Paul, Minnesota 55108-1030; 2: Biological Process Technology Institute University of Minnesota, St. Paul, Minnesota 55108-1030
Content Type: Textbook
Publication Year: 2001

Category: Applied and Industrial Microbiology; Environmental Microbiology

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Abstract:

This chapter focuses on microbial diversity and the catabolism of nonintermediary chemical compounds by disparate genera of prokaryotes. It describes the role that prokaryotes and fungi play collectively in biodegradation and how their extensive biocatalytic potential derives from a long evolutionary history. But microbial diversity also implies that individual bacteria and fungi are metabolically unique. In this context, it is useful to think of microbes as metabolic machines, dependent on gathering chemicals from their environment to obtain carbon, other elements, and energy to compete favorably against other microbes. Fungi are prominent in many environmental biodegradation processes and also in industrial biocatalysis. Four of the five major phyla of fungi are commonly used in industry. Of the ascomycota, and are the major fungal genera used in alcoholic-beverage fermentations. Many of the best-studied prokaryotes are aerobic proteobacteria and the high-G + C gram-positive bacteria. These, along with the fungus , are the examples discussed in the chapter. It is important to point out that some of the extensive catabolic activities of this class are based on the broad substrate specificities of a few oxygenases and related enzymes which handle the oxygenated intermediates.

Citation: Wackett L, Hershberger C. 2001. Microbial Diversity: Catabolism of Organic Compounds Is Broadly Distributed, p 39-69. In Biocatalysis and Biodegration. ASM Press, Washington, DC. doi: 10.1128/9781555818036.ch4
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Microbial Diversity: Catabolism of Organic Compounds Is Broadly Distributed
Citation: Wackett L, Hershberger C. 2001. Microbial Diversity: Catabolism of Organic Compounds Is Broadly Distributed, p 39-69. In Biocatalysis and Biodegration. ASM Press, Washington, DC. doi: 10.1128/9781555818036.ch4
/content/10.1128/9781555818036.chap4.fig4-1
Figure 4.1

Divergence in the metabolism of aromatic hydrocarbons by prokaryotes and eukaryotes.

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Figure 4.1

Divergence in the metabolism of aromatic hydrocarbons by prokaryotes and eukaryotes.

Citation: Wackett L, Hershberger C. 2001. Microbial Diversity: Catabolism of Organic Compounds Is Broadly Distributed, p 39-69. In Biocatalysis and Biodegration. ASM Press, Washington, DC. doi: 10.1128/9781555818036.ch4
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Figure 4.2

Taxonomic tree of the bacteria with groups heavily represented in the UM-BBD highlighted in green. (From reference with permission.)

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Image of Figure 4.2
Figure 4.2

Taxonomic tree of the bacteria with groups heavily represented in the UM-BBD highlighted in green. (From reference with permission.)

Citation: Wackett L, Hershberger C. 2001. Microbial Diversity: Catabolism of Organic Compounds Is Broadly Distributed, p 39-69. In Biocatalysis and Biodegration. ASM Press, Washington, DC. doi: 10.1128/9781555818036.ch4
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Figure 4.3

Part of the carbon cycle showing the metabolism of single-carbon compounds and reactions which feed into the cycle.

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Figure 4.3

Part of the carbon cycle showing the metabolism of single-carbon compounds and reactions which feed into the cycle.

Citation: Wackett L, Hershberger C. 2001. Microbial Diversity: Catabolism of Organic Compounds Is Broadly Distributed, p 39-69. In Biocatalysis and Biodegration. ASM Press, Washington, DC. doi: 10.1128/9781555818036.ch4
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Figure 4.4

Continuous acrylamide production by B23 in a fed-batch reactor. (From reference with kind permission from Kluwer Academic Publishers.)

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Image of Figure 4.4
Figure 4.4

Continuous acrylamide production by B23 in a fed-batch reactor. (From reference with kind permission from Kluwer Academic Publishers.)

Citation: Wackett L, Hershberger C. 2001. Microbial Diversity: Catabolism of Organic Compounds Is Broadly Distributed, p 39-69. In Biocatalysis and Biodegration. ASM Press, Washington, DC. doi: 10.1128/9781555818036.ch4
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Figure 4.5

Metabolic pathway for the microbial desulfurization of dibenzothiophene. Substrate and enzyme (green) names are shown in boxes.

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Image of Figure 4.5
Figure 4.5

Metabolic pathway for the microbial desulfurization of dibenzothiophene. Substrate and enzyme (green) names are shown in boxes.

Citation: Wackett L, Hershberger C. 2001. Microbial Diversity: Catabolism of Organic Compounds Is Broadly Distributed, p 39-69. In Biocatalysis and Biodegration. ASM Press, Washington, DC. doi: 10.1128/9781555818036.ch4
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Figure 4.6

Dioxygenase-catalyzed oxidation of indene to yield -(l ,2 )-dihydroxyindan, useful for the production of the anti-HIV drug indinavir.

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Image of Figure 4.6
Figure 4.6

Dioxygenase-catalyzed oxidation of indene to yield -(l ,2 )-dihydroxyindan, useful for the production of the anti-HIV drug indinavir.

Citation: Wackett L, Hershberger C. 2001. Microbial Diversity: Catabolism of Organic Compounds Is Broadly Distributed, p 39-69. In Biocatalysis and Biodegration. ASM Press, Washington, DC. doi: 10.1128/9781555818036.ch4
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Figure 4.7

Consortial metabolism of atrazine, with reactions catalyzed by different bacteria in separate boxes.

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Image of Figure 4.7
Figure 4.7

Consortial metabolism of atrazine, with reactions catalyzed by different bacteria in separate boxes.

Citation: Wackett L, Hershberger C. 2001. Microbial Diversity: Catabolism of Organic Compounds Is Broadly Distributed, p 39-69. In Biocatalysis and Biodegration. ASM Press, Washington, DC. doi: 10.1128/9781555818036.ch4
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Figure 4.8

Output of the UM-BBD “create a pathway” function starting with nitrobenzene.

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Image of Figure 4.8
Figure 4.8

Output of the UM-BBD “create a pathway” function starting with nitrobenzene.

Citation: Wackett L, Hershberger C. 2001. Microbial Diversity: Catabolism of Organic Compounds Is Broadly Distributed, p 39-69. In Biocatalysis and Biodegration. ASM Press, Washington, DC. doi: 10.1128/9781555818036.ch4
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References

/content/book/10.1128/9781555818036.chap4
1. Alcalde, M.,, F. J. Plou,, C. Andersen,, M. T. Martin,, S. Pedersen,, and A. Ballesteros. 1999. Chemical modification of lysine side chains of cyclodextrin glycosyltransferase from Thermoanaerabacter causes a shift from cyclodextrin glycosyltransferase to alpha-amylase specificity. FEBS Lett. 445: 333– 337.
2. Alvey, S.,, and D. E. Crowley. 1996. Survival and activity of an atrazinemineralizing bacterial consortium in rhizosphere soil. Environ. Sci. Technol. 30: 1596– 1603.
3. Barker, H. A. 1940. Studies on the methane fermentation: IV. The isolation and culture of Methanobacterium omelinnskii. Antonie Leeuwenhoek 6: 201– 220.
4. Bertoldo, C ,, F. Duffner,, P. L. Jorgensen,, and G. Antranikian. 1999. Pullulanase type I from Fervidobacterium pennavorans Ven5: cloning, sequencing, and expression of the gene and biochemical characterization of the recombinant enzyme. Appl. Environ. Microbiol. 65: 2084– 2091.
5. Bok, J. D.,, D. A. Yernool,, and D. E. Eveleigh. 1998. Purification, characterization, and molecular analysis of thermostable cellulases CelA and CelB from Thermotoga neapolitana. Appl. Environ. Microbiol. 64: 4774– 4781.
6. Boundy-Mills, K. L.,, M. L. de Souza,, R. T. Mandelbaum,, L. P. Wackett,, and M. J. Sadowsky. 1997. The atzB gene of Pseudomonas sp. strain ADP encodes the second enzyme of a novel atrazine degradation pathway. Appl. Environ. Microbiol. 63: 916– 923.
7. Boyle, A. W.,, C. D. Phelps,, and L. Y. Young. 1999. Isolation from estuarine sediments of a Desulfovibrio strain which can grow on lactate coupled to the reductive dehalogenation of 2,4,6-tribromophenol. Appl. Environ. Microbiol. 65: 1133– 1140.
8. Brauman, A.,, J. A. Muller,, J. L. Garcia,, A. Brune,, and B. Schink. 1998. Fermentative degradation of 3-hydroxybenzoate in pure culture by a novel strictly anaerobic bacterium, Sporotomaculum hydroxybenzoicum gen. nov, sp. nov. Int. J. Syst. Bacteriol. 1: 215– 221.
9. Bryant, M. P.,, E. A. Wolin,, M. J. Wolin,, and R. S. Wolfe. 1967. Methanobacillus omelianskii, a symbiotic association of two species of bacteria. Arch. Mikrobiol. 59: 20– 31.
10. Cerniglia, C. E.,, and D. T. Gibson. 1980. Fungal oxidation of ( + / - ) - 9 , 1 0 - dihydroxy-9,10-dihydrobenzo[a]pyrene: formation of diastereomeric benzo[a]pyrene 9,10-diol 7,8-epoxides. Proc. Natl. Acad. Sci. USA 77: 4554– 4558.
11. Cerniglia, C. E.,, R. L. Hebert,, P. J. Szaniszlo,, and D. T. Gibson. 1978. Fungal transformation of naphthalene. Arch. Microbiol. 117: 135– 143.
12. Cerniglia, C. E.,, and J. J. Perry. 1972. Crude oil degradation by microorganisms isolated from the marine environment. Z. Allg. Mikrobiol. 13: 299– 306.
13. Chen, C. C, and J. Westpheling. 1998. Partial characterization of the Streptomyces lividans xlnB promoter and its use for expression of a thermostable xylanase from Thermotoga maritima. Appl. Environ. Microbiol. 64: 4217– 4225.
14. Chi, Y. I.,, L. A. Martinez-Cruz,, J. Jancarik,, R. V. Swanson,, D. E. Robertson,, and S. H. Kim. 1999. Crystal structure of the beta-glycosidase from the hyperthermophile Thermosphaera aggregans: insights into its activity and thermostability. FEBS Lett. 445: 375– 383.
15. Christiansen, N.,, B. K. Ahring,, G. Wohlfarth,, and G. Diekert. 1998. Purification and characterization of the 3-chloro-4-hydroxy-phenylacetate reductive dehalogenase of Desulfitobacterium hafniense. FEBS Lett. 436: 159– 162.
16. Dagley, S. 1975. A biochemical approach to some problems of environmental pollution, p. 81– 138. Essays in Biochemistry, vol. 11. Academic Press, London, United Kingdom.
17. Daughton, C. G.,, and D. P. Hsieh. 1977. Parathion utilization by bacterial symbionts in a chemostat. Appl. Environ. Microbiol. 34: 175– 184.
18. de Souza, M. L.,, D. Newcombe,, S. Alvey,, D. E. Crowley,, A. Hay,, M. J. Sadowsky,, and L. P. Wackett. 1998. Molecular basis of a bacterial consortium: interspecies catabolism of atrazine. Appl. Environ. Microbiol. 64: 178– 184.
19. de Souza, M. L.,, J. Seffernick,, B. Martinez,, M. J. Sadowsky,, and L. P. Wackett. 1998. The atrazine catabolism genes atzABC are widespread and highly conserved. J. Bacteriol. 180: 1951– 1954.
20. de Souza, M. L.,, M. J. Sadowsky,, and L. P. Wackett. 1996. Atrazine chlorohydrolase from Pseudomonas sp. strain ADP: gene sequence, enzyme purification, and protein characterization. J. Bacteriol. 178: 4894– 4900.
21. de Souza, M. L.,, L. P. Wackett,, and M. J. Sadowsky. 1998. The atzABC genes encoding atrazine catabolism are located on a self-transmissible plasmid in Pseudomonas sp. strain ADP. Appl. Environ. Microbiol. 64: 2323– 2326.
22. Dettori, G.,, R. Grillo,, P. Cattani,, A. Calderaro,, C. Chezzi,, J. Milner,, K. Truelove,, and R. Sellwood. 1995. Comparative study of the enzyme activities of Borrelia burgdorferi and other non-intestinal and intestinal spirochaetes. New Microbiol. 18: 13– 26.
23. Eaton, R. W. 1997. p-Cymene catabolic pathway in Pseudomonas putida Fl: cloning and characterization of DNA encoding conversion of p-cymene to pcumate. J. Bacteriol. 179: 3171– 3180.
24. Fu, W.,, and P. Oriel. 1999. Degradation of 3-phenylpropionic acid by Haloferax sp. D1227. Extremophiles 3: 45– 53.
25. Fu, W.,, and P. Oriel. 1998. Gentisate 1,2-dioxygenase from Haloferax sp. D1227. Extremophiles 2: 439– 446.
26. Gibson, D. T.,, M. Hensley,, H. Yoshioka,, and T. J. Mabry. 1970. Formation of ( + )-ds-2,3-dihydroxy-l-methylcyclohexa-4,6-diene from toluene by Pseudomonas putida. Biochemistry 9: 1626– 1630.
27. Gibson, D. T.,, V. Mahadevan,, D. Jerina,, H. Yagi,, and H. Yeh. 1975. Oxidation of the carcinogens benzo(a)pyrene and benzo(a)anthracene. Science 189: 295– 297.
28. *28. Glazer, A. N.,, and H. Nikaido. 1995. Microbial Biotechnology: Fundamentals of Applied Microbiology. W. H. Freeman and Company, New York, N.Y.
29. Gray, K. A.,, O. S. Pogrebinsky,, G. T. Mrachko,, L. Xi,, D. J. Monticello,, and C. H. Squires. 1996. Molecular mechanisms of biocatalytic desulfurization of fossil fuels. Nat. Biotechnol. 14: 1705– 1709.
30. Harper, D. B. 1994. Biosynthesis of halogenated methanes. Biochem. Soc. Trans. 22: 1007– 1011.
31. Julliand, V.,, A. de Vaux,, L. Millet,, and G. Fonty. 1999. Identification of Ruminococcus flavefaciens as the predominant cellulolytic bacterial species of the equine cecum. Appl. Environ. Microbiol. 65: 3738– 3741.
32. Kieslich, K., 1998. General introduction to biocatalysis and screening, p. 3– 11. In K. Kieslich,, C. P. van der Beek,, J. A. M. de Bont,, and W.J. J. van den Tweel (ed.), New Frontiers in Screening for Microbial Biocatalysis. Elsevier Science, Amsterdam, The Netherlands.
33. Kim, T. J.,, M. J. Kim,, B. C. Kim,, J. C. Kim,, T. K. Cheong,, J. W. Kim,, and K. H. Park. 1999. Modes of action of acarbose hydrolysis and transglycosylation catalyzed by a thermostable maltogenic amylase, the gene for which was cloned from a Thermus strain. Appl. Environ. Microbiol. 65: 1644– 1651.
34. Laskin, A. I.,, and D. C. White. 1999. Preface to special issue on Sphingomonas. J. Ind. Microbiol. Biotechnol. 23: 231.
35. *35. Laskin, A. I.,, and D. C. White (ed.). 1999. Special issue on the genus Sphingomonas. J. Ind. Microbiol. Biotechnol. 23: 231– 445.
36. *36. Lazcano, A.,, and S. L. Miller. 1996. The origin and early evolution of life: prebiotic chemistry, the pre-RNA world, and time. Cell 85: 793– 798.
37. Marr, E. K.,, and R. W. Stone. 1961. Bacterial oxidation of benzene. J. Bacterial. 81: 425– 430.
38. Matheron, C.,, A. M. Delort,, G. Gaudet,, and E. Forano. 1998. In vivo 1 3C NMR study of glucose and cellobiose metabolism by four cellulolytic strains of the genus Fibrobacter. Biodegradation 9: 451– 461.
39. Meckenstock, R. U.,, R. Krieger,, S. Ensign,, P. M. Kroneck,, and B. Schink. 1999. Acetylene hydratase of Pelobacter acetylenicus. Molecular and spectroscopic properties of the tungsten iron-sulfur enzyme. Eur. J. Biochem. 264:176- 182.
40. Meissner, H.,, and W. Liebl. 1998. Thermotoga maritima maltosyltransferase, a novel type of maltodextrin glycosyltransferase acting on starch and maltooligosaccharides. Eur.J. Biochem. 258: 1050– 1058.
41. Morris, D. D.,, M. D. Gibbs,, M. Ford,, J. Thomas,, and P. L. Bergquist. 1999. Family 10 and 11 xylanase genes from Caldicellulosiruptor sp. strain Rt69B.l. Extremophiles 3: 103– 111.
42. Nagasawa, T.,, and H. Yamada. 1990. Bioconversion of nitriles to amides and acids, p. 277– 318. In D. A. Abramowicz (ed.), Biocatalysis. Van Nostrand Reinhold, New York, N.Y.
43. Oren, A.,, P. Gurevich,, and Y. Henis. 1991. Reduction of nitrosubstituted aromatic compounds by the halophilic anaerobic eubacteria Haloanaerobium prevalens and Sporohalobacter marismortui. Appl. Environ. Microbiol. 57: 3367– 3370.
44. Pace, N. R. 1997. A molecular view of microbial diversity and the biosphere. Science 276: 734– 740.
45. Palleroni, N. 1984. Family I. Pseudomonaceae, p. 140– 220. In N. R. Kreig (ed.), Bergey's Manual of Systematic Bacteriology, vol. 1. Williams and Wilkins, Baltimore, Md.
46. Peterson, D. H.,, and H. C. Murray. 1952. Microbiological oxygenation of steroids at carbon 11. J. Am. Chem. Soc. 74: 1871– 1872.
47. Raber, T.,, T. Gorontzy,, M. Kleinschmidt,, K. Steinbach,, and K. H. Blotevogel. 1998. Anaerobic degradation and transformation of p-toluidine by the sulfatereducing bacterium Desulfobacula toluolica. Curr. Microbiol. 37: 172– 176.
48. Reichenbecher, W.,, and B. Schink. 1999. Towards the reaction mechanism of pyrogallol-phloroglucinol transhydroxylase of Pelobacter acidigallici. Biochim. Biophys. Acta 1430: 245– 253.
49. Rocha, E. R.,, and C. J. Smith. 1999. Role of the alkyl hydroperoxide reductase (ahpCF) gene in oxidative stress defense of the obligate anaerobe Bacteroides fragilis. J. Bacteriol. 181: 5701– 5710.
50. Rooney-Varga, J. N.,, R. T. Anderson,, J. L. Fraga,, D. Ringelberg,, and D. R. Lovley. 1999. Microbial communities associated with anaerobic benzene degradation in a petroleum-contaminated aquifer. Appl. Environ. Microbiol. 65: 3056– 3063.
51. Sadowsky, M. J.,, M. L. de Souza,, Z. Tong,, and L. P. Wackett. 1998. AtzC is a member of the amidohydrolase protein superfamily and is homologous to other atrazine-metabolizing enzymes. J. Bacteriol. 180: 152– 158.
52. Schocke, L.,, and B. Schink. 1998. Membrane-bound proton-translocating pyrophosphatase of Syntrophus gentianae, a syntrophically benzoate-degrading fermenting bacterium. Eur. J. Biochem. 256: 589– 594.
53. *53. Senior, E., A. T. Bull, and J. H. Slater. 1976. Enzyme evolution in a microbial community growing on the herbicide Dalapon. Nature (London) 263: 476– 479.
54. Singer, M. E.,, S. M. Tyler,, and W. R. Finnerty. 1985. Growth of Acinetobacter sp. strain HOl-N on K-hexadecanol: physiological and ultrastructural characteristics. J. Bacteriol. 162: 162– 169.
55. Smith, R. V.,, and J. P. Rosazza. 1974. Microbial models of mammalian metabolism. Aromatic hydroxylation. Arch. Biochem. Biophys. 161: 551– 558.
56. Sonea, S.,, and M. Panisset. 1983. A New Bacteriology. Jones and Bartlett Publishers, Inc., Boston, Mass.
57. Thauer, R. K.,, K. Jungermann,, and K. Decker. 1977. Energy conversion in chemotrophic anaerobic bacteria. Microbiol. Rev. 41: 100– 180.
58. Treadway, S. L.,, K. S. Yanagimachi,, E. Lankenau,, P. A. Lessard,, G. Stephanopoulos,, and A. J. Sinskey. 1999. Isolation and characterization of indene bioconversion genes from Rhodococcus strain 124. Appl. Microbiol. Biotechnol. 51: 786– 793.
59. van de Pas, B. A.,, H. Smidt,, W. R. Hagen,, J. van der Oost,, G. Schraa,, A. J . Stains,, and W. de Vos. 1999. Purification and molecular characterization of ortfo-chlorophenol reductive dehalogenase, a key enzyme of halorespiration in Desulfitobacterium dehalogenans. J. Biol. Chem. 274: 20287– 20292.
60.von Wintzingerode, E, B. Selent, W. Hegemann, and U. B. Gobel. 1999. Phylogenetic analysis of an anaerobic, trichlorobenzene-transforming microbial consortium. Appl. Environ. Microbiol. 65: 283– 286.
61. Wackett, L. P.,, and D. T. Gibson. 1982. The metabolism of xenobiotic compounds by enzymes in cell extracts of the fungus Cunninghamella elegans. Biochem. J. 205: 117– 122.
*62. Whitman, W. B.,, D. C. Coleman,, and W. J. Wiebe. 1998. Prokaryotes: the unseen majority. Proc. Natl. Acad. Sci. USA 95: 6578– 6583. Microbial Diversity: Catabolism of Organic Compounds 69
63. Wiegel, J.,, X. Zhang,, and Q. Wu. 1999. Anaerobic dehalogenation of hydroxylated polychlorinated biphenyls by Desulfitobacterium dehalogenans. Appl. Environ. Microbiol. 65: 2217– 2221.
64. Wilson, E. O. 1992. The Diversity of Life. Harvard University Press, Cambridge, Mass.
65. Yamada, H.,, and M. Kobayashi. 1996. Nitrile hydratase and its application to industrial production of acrylamide. Biosci. Biotechnol. Biochem. 60: 1391– 1400.
66. Zengler, K.,, H. H. Richnow,, R. Rossello-Mora,, W. Michaelis,, and F. Widdel. 1999. Methane formation from long-chain alkanes by anaerobic microorganisms. Nature 401: 266– 269.

Tables

Microbial Diversity: Catabolism of Organic Compounds Is Broadly Distributed
Citation: Wackett L, Hershberger C. 2001. Microbial Diversity: Catabolism of Organic Compounds Is Broadly Distributed, p 39-69. In Biocatalysis and Biodegration. ASM Press, Washington, DC. doi: 10.1128/9781555818036.ch4
/content/10.1128/9781555818036.chap4.tab4-1
Table 4.1

Niches and numbers of prokaryotes on Earth

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Table 4.1

Niches and numbers of prokaryotes on Earth

Citation: Wackett L, Hershberger C. 2001. Microbial Diversity: Catabolism of Organic Compounds Is Broadly Distributed, p 39-69. In Biocatalysis and Biodegration. ASM Press, Washington, DC. doi: 10.1128/9781555818036.ch4
/content/10.1128/9781555818036.chap4.tab4-2
Table 4.2

Phyla and classes of fungi active in hydroxylation reactions

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Table 4.2

Phyla and classes of fungi active in hydroxylation reactions

Citation: Wackett L, Hershberger C. 2001. Microbial Diversity: Catabolism of Organic Compounds Is Broadly Distributed, p 39-69. In Biocatalysis and Biodegration. ASM Press, Washington, DC. doi: 10.1128/9781555818036.ch4
/content/10.1128/9781555818036.chap4.tab4-3
Table 4.3

Fungal hydroxylation of steroid substrates

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Table 4.3

Fungal hydroxylation of steroid substrates

Citation: Wackett L, Hershberger C. 2001. Microbial Diversity: Catabolism of Organic Compounds Is Broadly Distributed, p 39-69. In Biocatalysis and Biodegration. ASM Press, Washington, DC. doi: 10.1128/9781555818036.ch4
/content/10.1128/9781555818036.chap4.tab4-4
Table 4.4

Industrially important enzymes produced by fungi

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Table 4.4

Industrially important enzymes produced by fungi

Citation: Wackett L, Hershberger C. 2001. Microbial Diversity: Catabolism of Organic Compounds Is Broadly Distributed, p 39-69. In Biocatalysis and Biodegration. ASM Press, Washington, DC. doi: 10.1128/9781555818036.ch4
/content/10.1128/9781555818036.chap4.tab4-5
Table 4.5

Reclassification of bacterial strains previously classified as species

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Generic image for table
Table 4.5

Reclassification of bacterial strains previously classified as species

Citation: Wackett L, Hershberger C. 2001. Microbial Diversity: Catabolism of Organic Compounds Is Broadly Distributed, p 39-69. In Biocatalysis and Biodegration. ASM Press, Washington, DC. doi: 10.1128/9781555818036.ch4
/content/10.1128/9781555818036.chap4.tab4-6
Table 4.6

Microbial genera known to biodegrade organic compounds, represented in the UM-BBD on 15 August 1999

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Table 4.6

Microbial genera known to biodegrade organic compounds, represented in the UM-BBD on 15 August 1999

Citation: Wackett L, Hershberger C. 2001. Microbial Diversity: Catabolism of Organic Compounds Is Broadly Distributed, p 39-69. In Biocatalysis and Biodegration. ASM Press, Washington, DC. doi: 10.1128/9781555818036.ch4
/content/10.1128/9781555818036.chap4.tab4-7
Table 4.7

Taxonomic distribution of bacteria for which biodegradation reactions were depicted on the UM-BBD as of 15 August 1999

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Table 4.7

Taxonomic distribution of bacteria for which biodegradation reactions were depicted on the UM-BBD as of 15 August 1999

Citation: Wackett L, Hershberger C. 2001. Microbial Diversity: Catabolism of Organic Compounds Is Broadly Distributed, p 39-69. In Biocatalysis and Biodegration. ASM Press, Washington, DC. doi: 10.1128/9781555818036.ch4
/content/10.1128/9781555818036.chap4.tab4-8
Table 4.8

Prokaryotes from taxonomic groups underrepresented in the biodegradation literature, recently reported to catalyze biodegradation reactions

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Table 4.8

Prokaryotes from taxonomic groups underrepresented in the biodegradation literature, recently reported to catalyze biodegradation reactions

Citation: Wackett L, Hershberger C. 2001. Microbial Diversity: Catabolism of Organic Compounds Is Broadly Distributed, p 39-69. In Biocatalysis and Biodegration. ASM Press, Washington, DC. doi: 10.1128/9781555818036.ch4
/content/10.1128/9781555818036.chap4.tab4-9
Table 4.9

Compounds known or proposed to be oxidized by F1

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Table 4.9

Compounds known or proposed to be oxidized by F1

Citation: Wackett L, Hershberger C. 2001. Microbial Diversity: Catabolism of Organic Compounds Is Broadly Distributed, p 39-69. In Biocatalysis and Biodegration. ASM Press, Washington, DC. doi: 10.1128/9781555818036.ch4

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