New applications of bacterial systems to problems in toxicology

Critical Reviews in Toxicology

Volumn 26, Issue 5, 1996, Pages 551-583

  Guengerich, F Peter ^a   Gillam, Elizabeth M J ^b   Shimada, Tsutomu ^c  

^a VANDERBILT UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF QUEENSLAND   (Australia)

^c OSAKA PREFECTURAL INSTITUTE OF PUBLIC HEALTH   (Japan)

Author keywords

bacteria; cytochrome P450; Escherichia coli; genotoxicity assays; glutathione S transferase; Salmonella typhimurium; SOS response; use in toxicology

Indexed keywords

CYTOCHROME P450; ENZYME; GLUTATHIONE TRANSFERASE;

BACTERIUM; DNA REPAIR; ESCHERICHIA COLI; GENOTOXICITY; METABOLIC ACTIVATION; NONHUMAN; REVIEW; SALMONELLA TYPHIMURIUM; TOXICITY TESTING;

ANIMALIA; BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; MAMMALIA; SALMONELLA TYPHIMURIUM; TYPHIMURIUM;

EID: 0029852566     PISSN: 10408444     EISSN: None     Source Type: Journal    
DOI: 10.3109/10408449609037477     Document Type: Review

References (254)

1. Avery, O. T., Macleod, C. M., and McCarty, M., Studies on the chemical nature of the substance inducing transformation of pneumococcal types. I. Induction of transformation by a desoxyribonucleic acid fraction isolated from pneumonococcus type III, J. Exp. Med., 79, 137, 1944.
2. Hayes, W., The Genetics of Bacteria and Their Viruses, 2nd ed., Wiley, New York, 1968.
3. cam substrate and effector interactions, Ann. N. Y. Acad. Sci., 212, 107, 1973.
4. b-methylguanine residues in DNA, Nature, 280, 76, 1979.
5. Grossman, L., Braun, A., Feldberg, R., and Mahler, I., Enzymatic repair of DNA, Annu. Rev. Biochem., 44, 19, 1975.
6. Friedberg, E. , DNA Repair, W. H. Freeman, San Francisco, 1985.
7. Friedberg, E. C., Walker, G. C., and Siede, W., DNA Repair and Mutagenesis, American Society Microbiology, Washington, D. C., 1995.
8. Sancar, A., Mechanisms of DNA excision repair, Science, 266, 1954, 1994.
9. Hanawalt, P. C., Transcription-coupled repair and human disease, Science, 266, 1957, 1994.
10. Modrich, P., Mismatch repair, genetic stability, and cancer, Science, 266, 1959, 1994.
11. Wolf, U., Theodor Boveri and his book "On the problem of the origin of malignant tumors," in Chromosomes and Cancer, German, J., Ed., Wiley, New York, 1974, 3.
12. Kennaway, E. L. and Hieger, I., Carcinogenic substances and their fluorescence spectra, Br. Med. J., i: 1044, 1930.
13. Haddow, A., Influence of certain polycyclic hydrocarbons on the growth of the Jensen rat sarcoma, Nature, 136, 868, 1935.
14. Muller, H. J., Radiation damage to the genetic material. Induction of gene mutations in somatic cells, in Science in Progress, 7th series, Baitsell, G. A., Ed., Yale University Press, New Haven, CT, 1951, 130.
15. Burdette, W. J., The significance of mutation in relation to the origin of tumors: a review, Cancer Res., 15, 201, 1955.
16. Bauer, K. H., Mutationstheorie der Gesch-wulstenstehung, Springer, Berlin, 1928.
17. Boyland, E., Mutagens, Pharmacol. Rev., 6, 345, 1954.
18. Scherr, G. H., Fishman, M., and Weaver, R., The mutagenicity of some carcinogenic compounds for Escherichia coli, Genetics, 39, 141, 1954.
19. Malling, H. V., Dimethylnitrosamine: formation of mutagenic compounds by interaction with mouse liver microsomes, Mutation Res., 13, 425, 1971.
20. Bertani, G., A method for detection of mutations, using streptomycin dependence in Escherichia coli, Genetics, 33, 598, 1951.
21. Bryson, V., The effects of nitrogen mustard on Escherichia coli, J. Bacteriol., 56, 423, 1948.
22. Demerec, M., Induced mutations and possible mechanisms of the transmission of heredity in Escherichia coli, Proc. Natl. Acad. Sci. U.S. A., 32, 36, 1946.
23. Hemmerly, J. and Demerec, M., Tests of chemicals for mutagenicity, Cancer Res., 3 (Suppl.), 69, 1955.
24. Iyer, V. N. and Szybalski, W., Two simple methods for the detection of chemical mutagens, Appl. Microbiol., 6, 23, 1958.
25. Kaplan, R. W., Mutation by photodynamic action in Bacterium prodigiosum, Nature, 163, 573, 1949.
26. Mueller, G. C. and Miller, J. A., The metabolism of 4-dimethylaminoazobenzene by rat liver homogenates, J. Biol. Chem., 176, 535, 1948.
27. Miller, J. A., Carcinogenesis by chemicals: an overview. G.H.A. Clowes Memorial Lecture, Cancer Res., 30, 559, 1970.
28. Ames, B. N., The detection of chemical mutagens with enteric bacteria, in Chemical Mutagens, Principles and Methods for their Detection, Vol. 1, Hollaender, A., Ed., Plenum Press, New York, 1971, 267.
29. Josephy, P. D., New developments in the Ames assay: high-sensitivity detection of mutagenic arylamines, BioEssays, 11, 108, 1989.
30. Hartman, P. E., Ames, B. N., Roth, J. R., Barnes, W. M., and Levin, D. E., Target sequences for mutageneis in Salmonella histidine-requiring mutants, Environ. Mutagen., 8, 631, 1986.
31. Ames, B. N., Durston, W. E., Yamasaki, E., and Lee, F. D., Carcinogens are mutagens: A simple test system combining liver homogenates for activation and bacteria for detection, Proc. Natl. Acad. Sci. U.S. A., 70, 2281, 1973.
32. Wood, A. W., Levin, W., Lu, A. Y. H., Yagi, H., Hernandez, O., Jerina, D. M., and Conney, A. H., Metabolism of benzo[a] pyrene and benzo[a]pyrene derivatives to mutagenic products by highly purified hepatic microsomal enzymes, J. Biol. Chem., 251, 4882, 1976.
33. McCann, J., Spingarn, N. E., Kobori, J., and Ames, B. N., Detection of carcinogens as mutagens: bacterial tester strains with R factor plasmids, Proc. Natl. Acad. Sci. U.S. A., 72, 979, 1975.
34. Maron, D. M. and Ames, B. N., Revised methods for the Salmonella mutagenicity test, Mutation Res., 113, 173, 1983.
35. McCann, J., Choi, E., Yamasaki, E., and Ames, B. N., Detection of carcinogens as mutagens in the Salmonella/microsome test: assay of 300 chemicals, Proc. Natl. Acad. Sci. U.S. A., 72, 5135, 1975.
36. Bartsch, H. and Malaveille, C., The Ames test, ISI Atlas Sci. Pharmacol., p. 1, 1987.
37. Gee, P., Maron, D. M., and Ames, B. N., Detection and classification of mutagens: a set of base-specific Salmonella tester strains, Proc. Natl. Acad. Sci. U.S. A., 91, 11606, 1994.
38. Levin, D. E., Hollstein, M. F., Christman, E. A., Schwiers, E. A., and Ames, B. N., A new Salmonella tester strain (TA102) with A:T base pairs at the site of mutation detects oxidative mutagens, Proc. Natl. Acad. Sci. U.S. A., 79, 7445, 1982.
39. Marnett, L. J., Hurd, H. K., Hollstein, M. C., Levin, D. E., Esterbauer, H., and Ames, B. N., Naturally occurring carbonyl compounds are mutagens in Salmonella tester strain TA104, Mutation Res., 148, 25, 1985.
40. Jung, R., Engelhart, G., Herbolt, B., Jäckh, R., and Müller, W., Collaborative study of mutagenicity with Salmonella typhimurium TA102, Mutation Res., 278, 265, 1992.
41. Bogen, K. T., Improved prediction of carcinogenic potencies from mutagenic potencies for chemicals positive in rodents and the Ames test, Environ. Mol. Mutagen., 25, 37, 1995.
42. Shelby, M. D., The genetic toxicity of human carcinogens and its implications, Mutation Res., 204, 3, 1988.
43. Tennant, R. W., Margolin, B. H., Shelby, M. D., Zeiger, E., Haseman, J. K., Spalding, J., Caspary, W., Resnick, M., Stasiewicz, S., Anderson, B., and Minor, R., Prediction of chemical carcinogenicity in rodents from in vitro genetic toxicity assays, Science, 236, 933, 1987.
44. Ames, B. N. and Gold, L. S. , Chemical carcinogenesis: too many rodent carcinogens, Proc. Natl. Acad. Sci. U.S. A., 87, 7772, 1990.
45. 2u-globulin nephropathy, Regul. Toxicol. Pharmacol., 13, 1, 1991.
46. Ames, B. N., Gold, L. S., and Willett, W. C., The causes and prevention of cancer, Proc. Natl. Acad. Sci. U.S. A., 92, 5258, 1995.
47. Ashby, J., Determination of the genotoxic status of a chemical, Mutation Res., 248, 221, 1991.
48. Boberg, E. W., Liem, A., Miller, E. C., and Miller, J. A., Inhibition by pentachlorophenol of the initiating and promoting activites of 1′-hydroxysafrole for the formation of enzyme-altered foci and tumors in rat liver, Carcinogenesis, 8, 531, 1987.
49. Sullivan, N., Gatehouse, D., and Tweats, D., Mutation, cancer and transgenic models: relevance to the toxicology industry, Mutagenesis, 8, 167, 1993.
50. Brusick, D., Genetic toxicology, in: Principles and Methods of Toxicology. 3rd ed., Hayes, A. W., Ed., Raven Press, New York, 1994, 545.
51. Tennant, R. W. and Zeiger, E., Genetic toxicology: current status of methods of carcinogen identification, Environ. Health Perspect., 100, 307, 1993.
52. Lewis, D. F. V., Comparison between rodent carcinogenicity test results of 44 chemicals and a number of predictive systems, Regul. Toxicol. Pharmacol., 20, 215, 1994.
53. Murli, S. and Walker, G. C., SOS mutagenesis, Curr. Opin. Genet. Dev., 3, 719, 1993.
54. Shimada, T., Oda, Y., Yamazaki, H., Mimura, M., and Guengerich, F. P., SOS function tests for studies of chemical carcinogenesis in Salmonella typhimurium TA 1535/pSK1002, NM2009, and NM3009, in Methods in Molecular Genetics, Vol. 5, Gene and Chromosome Analysis, Adolph, K. W., Ed., Academic Press, Orlando, FL, 1994, 342.
55. Oda, Y., Nakamura, S., Oki, I., Kato, T., and Shinagawa, H., Evaluation of the new system (umu-test) for the detection of environmental mutagens and carcinogens, Mutation Res., 147, 219, 1985.
56. McDaniels, A. E., Reyes, A. L., Wymer, L. J., Rankin, C. C., and Stelma, G. N., Jr., Comparison of the Salmonella (Ames) test, Umu tests, and the SOS chromotests for detecting genotoxins, Environ. Mol. Mutagen., 16, 204, 1990.
57. Sato, T., Chikazawa, K., Yamamori, H., Ose, Y., Nagase, H., and Kito, H., Evaluation of the SOS chromotest for the detection of antimutagens, Environ. Mol. Mutagen., 17, 258, 1991.
58. Walker, G. C., Mutagenesis and inducible responses to deoxyribonucleic acid damage in Escherichia coli, Microbiol. Rev., 48, 60, 1984.
59. Little, J. W. and Mount, D. W., The SOS regulatory system of Escherichia coli, Cell, 29, 11, 1982.
60. Shinagawa, H., Iwasaki, H., Kato, T., and Nakata, A., RecA protein-dependent cleavage of UmuD protein and SOS mutagenesis, Proc. Natl. Acad. Sci. U.S. A., 85, 1806, 1988.
61. Burckhardt, S. E., Woodgate, R., Scheuermann, R. H., and Echols, H., UmuD mutagenesis protein of Escherichia coli: overproduction, purification, and cleavage by RecA, Proc. Natl. Acad. Sci. U.S. A., 85, 1811, 1988.
62. Nohmi, T., Battista, J. R., Dodson, L. A., and Walker, G. C., RecA-mediated cleavage activates UmuD for mutagenesis: mechanistic relationship between transcriptional derepression and posttranslational activation, Proc. Natl. Acad. Sci. U.S. A., 85, 1816, 1988.
63. Quillardet, P., Huisman, O., D'ari, R., and Hofnung, M., SOS chromotest, a direct assay of induction of an SOS function in Escherichia coli K-12 to measure genotoxicity, Proc. Natl. Acad. Sci. U.S. A., 79, 5971, 1982.
64. Ohta, T., Nakamura, N., Moriya, M., Shirasu, Y., and Kada, T., The SOS-function-inducing activity of chemical mutagens in Escherichia coli, Mutation Res., 131, 101, 1984.
65. De Méo, M., Vanelle, P., Bernadini, E., Laget, M., Maldonado, J., Jentzer, O., Crozet, M. P., and Duménil, G., Evaluation of the mutagenic and genotoxic activities of 48 nitroimidazoles and related imidazole derivates by the Ames test and the SOS chromotest, Environ. Mol. Mutagen., 19, 167, 1992.
66. 7 adducts and inducing different genetic responses, Chem. Res. Toxicol., 2, 114, 1989.
67. 1, Chem. Res. Toxicol., 5, 202, 1992.
68. Shimada, T. and Guengerich, F. P., Activation of amino-α-carboline, 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine, and a copper phthalocyanine cellulose extract of cigarette smoke condensate by cytochrome P-450 enzymes in rat and human liver microsomes, Cancer Res., 51, 5284, 1991.
69. Nakamura, S., Oda, Y., Shimada, T., Oki, I., and Sugimoto, K., SOS-inducing activity of chemical carcinogens and mutagens in Salmonella typhimurium TA1535/pSK1002: examination with 151 chemicals, Mutation Res., 192, 239, 1987.
70. Thier, R., Müller, M., Taylor, J. B., Pemble, S. E., Ketterer, B., and Guengerich, F. P., Enhancement of bacterial mutagenicity of bifunctional alkylating agents by expression of mammalian glutathione S-transferase, Chem. Res. Toxicol., 8, 465, 1995.
71. Humphreys, W. G., Kim, D.-H., Cmarik, J. L., Shimada, T., and Guengerich, F. P., Comparison of the DNA alkylating properties and mutagenic responses caused by a series of S-(2-haloethyl)-substituted cysteine and glutathione derivatives, Biochemistry, 29, 10342, 1990.
72. Shimada, T., Yamazaki, H., Oda, Y., Hiratsuka, A., Watabe, T., and Guengerich, F. P., Activation and inactivation of carcino-genic dihaloalkanes and other compounds by glutathione S-transferase 5-5 in Salmonella typhimurium tester strain NM5004, Chem. Res. Toxicol., 9, 333, 1996.
73. Benamira, M. and Marnett, L. J., The lipid peroxidation product 4-hydroxynonenal is a potent inducer of the SOS response, Mutation Res., 293, 1, 1992.
74. Shimada, T. and Okuda, Y., Metabolic activation of environmental carcinogens and mutagens by human liver microsomes: role of cytochrome P-450 homologous to 3-methylcholanthrene-inducible isozyme in rat liver, Biochem. Pharmacol., 37, 459, 1988.
75. Shimada, T. and Nakamura, S. , Cytochrome P-450-mediated activation of procarcinogens and promutagens to DNA-damaging products by measuring expression of umu gene in Salmonella typhimurium TA1535/pSK1002, Biochem. Pharmacol., 36, 1979, 1987.
76. Reifferscheid, G., Heil, J., Oda, Y., and Zahn, R. K., A microplate version of the SOS/umu-test for rapid detection of genotoxins and genotoxic potentials of environmental samples, Mutation Res., 253, 215, 1991.
77. Nebert, D. W., Heidema, J. K., Strobel, H. W., and Coon, M. J., Genetic expression of aryl hydrocarbon hydroxylase induction: genetic specificity resides in the fraction containing cytochromes P448 and P450, J. Biol. Chem., 248, 7631, 1973.
78. Guengerich, F. P., Separation and purification of multiple forms of microsomal cytochrome P-450. Activities of different forms of cytochrome P-450 towards several compounds of environmental interest, J. Biol. Chem., 252, 3970, 1977.
79. Wiebel, F. J., Selkirk, J. K., Gelboin, H. V., Haugen, D. A., van der Hoeven, T. A., and Coon, M. J., Position-specific oxygenation of benzo[a]pyrene by different forms of purified cytochrome P-450 from rabbit liver, Proc. Natl. Acad. Sci. U.S. A., 12, 3917, 1975.
80. Shimada, T., Iwasaki, M., Martin, M. V., and Guengerich, F. P., Human liver microsomal cytochrome P-450 enzymes involved in the bioactivation of procarcinogens detected by umu gene response in Salmonella typhimurium TA1535/pSK1002, Cancer Res., 49, 3218, 1989.
81. Shimada, T., Martin, M. V., Pruess-Schwartz, D., Marnett, L. J., and Guengerich, F. P., Roles of individual human cytochrome P-450 enzymes in the bioactivation of benzo(a)pyrene, 7,8-dihydroxy-7,8-dihydro-benzo(a)pyrene, and other dihydrodiol derivatives of polycyclic aromatic hydrocarbons. Cancer Res., 49, 6304, 1989.
82. NF, the nifedipine oxidase, being the principal enzyme involved in the bioactivation of aflatoxins in human liver, Proc. Natl. Acad. Sci. U.S. A., 86, 462, 1989.
83. Yamazaki, H., Degawa, M., Funae, Y., Imaoka, S., Inui, Y., Guengerich, F. P., and Shimada, T., Roles of different cytochrome P-450 enzymes in bioactivation of the potent hepatocarcinogen 3-methoxy-4-aminoazobenzene by rat and human liver microsomes, Carcinogenesis. 12, 133, 1991.
84. Yamazaki, H., Oda, Y., Funae, Y., Imaoka, S. , Inui, Y., Guengerich, F. P., and Shimada, T., Participation of rat liver cytochrome P450 2E1 in the activation of N-nitrosodimethylamine and N-diethylnitrosamine to products genotoxic in Salmonella tvphimurium NM2009, Carcinogenesis, 13, 979, 1992.
85. Yamazaki, H., Inui, Y., Yun, C.-H., Mimura, M., Guengerich, F. P., and Shimada, T., Cytochrome P450 2E1 and 2A6 enzymes as major catalysts for metabolic activation of N-nitrosodialkylamines and tobacco-related nitrosamines in human liver microsomes, Carcinogenesis, 13, 1789, 1992.
86. Yamazaki, H., Mimura, M., Oda, Y., Inui, Y., Shiraga, T., Iwasaki, K., Guengerich, F. P., and Shimada, T., Roles of different forms of cytochrome P450 in the activation of the promutagen 6-aminochrysene to genotoxic metabolites in human liver microsomes, Carcinogenesis, 14, 1271, 1993.
87. Yamazaki, H., Mimura, M., Oda, Y., Gonzalez, F. J., El-Bayoumy, K., Guengerich, F. P., and Shimada, T., Activation of trans-1,2-dihydro-1,2-dihydroxy-6-aminochrysene to genotoxic metabolites by rat and human cytochromes P450, Carcinogenesis, 15, 465, 1994.
88. Guengerich, F. P. and Shimada, T., Oxidation of toxic and carcinogenic chemicals by human cytochrome P-450 enzymes. Chem. Res. Toxicol., 4, 391, 1991.
89. Guengerich, F. P., Metabolic activation of carcinogens, Pharmacol. Ther., 54, 17, 1992.
90. Miranda, C. L., Reed, R. L., Guengerich, F. P., and Buhler, D. R., Role of cytochrome P450IIIA4 in the metabolism of the pyrrolizidine alkaloid senecionine in human liver, Carcinogenesis, 12, 515, 1991.
91. Smith, T. J., Guo, Z., Gonzalez, F. J., Guengerich, F. P., Stoner, G. D., and Yang, C. S., Metabolism of 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone (NNK) in human lung and liver microsomes and cytochromes P-450 expressed in hepatoma cells, Cancer Res., 52, 1757, 1992.
92. Yun, C.-H., Shimada, T., and Guengerich, F. P., Contributions of human liver cytochrome P-450 enzymes to the N-oxidation of 4,4′-methylene-bis(2-chloroaniline), Carcinogenesis, 13, 217, 1992.
93. Chae, Y. H., Yun, C.-H., Guengerich, F. P., Kadlubar, F. F., and El-Bayoumy, K., Roles of human hepatic and pulmonary cytochrome P450 enzymes in the metabolism of the environmental carcinogen 6-nitrochrysene, Cancer Res., 53, 2028, 1993.
94. 1 by bacterial recombinant human cytochrome P450 enzymes, Chem. Res. Toxicol., 8, 218, 1995.
95. Shimada, T., Yamazaki, H., Shimura, H., Tanaka, R., and Guengerich, F. P., Metabolic deactivation of furylfuramide by cytochrome P450 in human and rat liver microsomes, Carcinogenesis, 11, 103, 1990.
96. Shimada, T. and Guengerich, F. P., Inactivation of 1,3-, 1,6-, and 1,8-dinitropyrene by human and rat microsomes, Cancer Res., 50, 2036, 1990.
97. Watanabe, M., Nohmi, T., and Ishidate, M., Jr., New tester strains of Salmonella typhimurium highly sensitive to mutagenic nitroarenes, Biochem. Biophys. Res. Commun., 147, 974, 1987.
98. Watanabe, M., Ishidate, M., Jr., and Nohmi, T., Sensitive method for the detection of mutagenic nitroarenes and aromatic amines: new derivatives of Salmonella typhimurium tester strains possessing elevated O-acetyltransferase levels, Mutation Res., 234, 337, 1990.
99. Oda, Y., Yamazaki, H., Watanabe, M., Nohmi, T., and Shimada, T., Highly sensitive umu test system for the detection of mutagenic nitroarenes in Salmonella tvphimurium NM3009 having high O-acetyltransferase and nitroreductase activities, Environ. Mol. Mutagen., 21, 357, 1993.
100. Rosenkranz, H. S. and Mermelstein, R., The genotoxicity, metabolism and carcinogenicity of nitrated polycyclic aromatic hydrocarbons, J. Environ. Sci. Health, C3, 221, 1985.
101. Yamazaki, H., Oda, Y., and Shimada, T., Use of a newly developed tester strain, Salmonella typhimurium NM2009, for the study of metabolic activation of carcinogenic aromatic amines by rat liver microsomal cytochrome P-450 enzymes, Mutation Res., 272, 183, 1992.
102. Oda, Y., Yamazaki, H., Watanabe, M., Nohmi, T., and Shimada, T., Development of high sensitive umu test system: rapid detection of genotoxicity of promutagenic aromatic amines by Salmonella typhimurium strain NM2009 possessing high O-acetyltransferase activity, Mutation Res., 334, 145, 1995.
103. Josephy, P. D., Lord, H. L., and Snieckus, V. A., Dimethylnitrosamine genotoxicity: does N-acetyltransferase activity play a role? Carcinogenesis, 15, 479, 1994.
104. Grant, D. M., Josephy, P. D., Lord, H. L., and Morrison, L. D., Salmonella typhimurium strains expressing human arylamine N-acetyltransferases: metabolism and mutagenic activation of aromatic amines, Cancer Res., 52, 3961, 1992.
105. Gold, L., Expression of heterologous proteins in Escherichia coli, Methods Enzymol., 185, 11, 1991.
106. Henner, D. J., Expression of heterologous genes in Bacillus subtilis, Methods Enzymol., 185, 199, 1991.
107. Mendoza, J. A. and Horowitz, P. M., Sulfhydryl modification of E. coli Cpn60 leads to loss of its ability to support refolding of rhodanese but not to form a binary complex, J. Protein Chem., 11, 589, 1992.
108. Kudlicki, W., Odoni, O. W., Kramer, G., Hardesty, B., Merrill, G. A., and Horowitz, P. M., The importance of the N-terminal segment for DnaJ-mediated folding of rhodanese while bound to ribosomes as peptidyl-tRNA, J. Biol. Chem., 270, 10650, 1995.
109. + oxidoreductase in Escherichia coli requires GroE molecular chaperones, J. Biol. Chem., 267, 15537, 1992.
110. Zuber, M. X., Simpson, E. R., and Waterman, M. R., Expression of bovine 17α-hydroxylase cytochrome P-450 cDNA in nonsteroidogenic (COS 1) cells, Science, 234, 1258, 1986.
111. Gonzalez, F. J., Aoyama, T., and Gelboin, H. V., Expression of mammalian cytochrome P450 using vaccinia virus, Methods Enzymol., 206, 85, 1991.
112. Doehmer, J. and Oesch, F., V79 Chinese hamster cells genetically engineered for stable expression of cytochromes P450, Methods Enzymol., 206, 117, 1991.
113. Crespi, C. L., Langenbach, R., and Penman, B. W., Human cell lines, derived from AHH-1 TK+/- human lymphoblasts, genetically engineered for expression of cytochromes P450, Toxicology, 82, 89, 1993.
114. Guengerich, F. P., Brian, W. R., Sari, M.-A., and Ross, J. T., Expression of mammalian cytochrome P450 enzymes using yeast-based vectors. Methods Enzymol., 206, 130, 1991.
115. Renaud, J. P., Peyronneau, M. A., Urban, P., Truan, G., Cullin, C., Pompon, D., Beaune, P., and Mansuy, D., Recombinant yeast in drug metabolism, Toxicology, 82, 39, 1993.
116. Gonzalez, F. J., Kimura, S., Tamura, S., and Gelboin, H. V., Expression of mammalian cytochrome P450 using baculovirus, Methods Enzymol., 206, 93, 1991.
117. Board, P. G. and Pierce, K., Expression of human glutathione S-transferase 2 in Escherichia coli: immunological comparison with the basic glutathione S-transferases isoenzymes from human liver, Biochem. J., 248, 937, 1987.
118. b3 glutathione S-transferase in Escherichia coli and identification of its natural form in rat brain, J. Biol. Chem., 263, 17627, 1988.
119. a subunit in Escherichia coli, Arch. Biochem. Biophys., 269, 536, 1989.
120. Ma, Q., Cui, K., Wang, R. W., Lu, A. Y. H., and Yang, C. S. , Site-directed mutagenesis of rat liver NAD(P)H: quinone oxidoreductase: roles of lysine 76 and cysteine 179, Arch. Biochem. Biophys., 294, 434, 1992.
121. 68 in the catalytic mechanism of polymorphic human NAT2, J. Biol. Chem., 267, 7381, 1992.
122. Ausubel, F. M., Brent, R., Kingston, R. E., Moore, D. D., Seidman, J. G., Smith, J. A., and Struhl, K., Current Protocols in Molecular Biology, Vol. 2, John Wiley & Sons, New York, 1992.
123. Baker, R. T., Smith, S. A., Marano, R., McKee, J., and Board, P. G., Protein expression using cotranslational fusion and cleavage of ubiquitin, J. Biol. Chem., 269, 25381, 1994.
124. Dupret, J.-M., Goodfellow, G. H., Janezic, S. A., and Grant, D. M., Structure-function studies of human arylamine N-acetyltransferases NAT1 and NAT2, J. Biol. Chem., 269, 26830, 1994.
125. Hein, D. W., Doll, M. A., Rustan, T. D., Gray, K., Feng, Y., Ferguson, R. J., and Grant, D. M., Metabolic activation and deactivation of arylamine carcinogens by recombinant human NAT1 and polymorphic NAT2 acetyltransferases, Carcinogenesis, 14, 1633, 1993.
126. Hein, D. W., Ferguson, R. J., Doll, M. A., Rustan, T. D., and Gray, K., Molecular genetics of human polymorphic N-acetyltransferase - Enzymatic analysis of 15 recombinant wildtype, mutant and chimeric NAT2 allozymes, Hum. Mol. Genet., 3, 729, 1994.
127. Chen, X., Yang, Y.-S., Zheng, Y., Martin, B. M., Duffel, M. W., and Jakoby, W. B., Tyrosine-ester sulfotransferase from rat liver: bacterial expression and identification, Protein Purification Expression, 3, 421, 1992.
128. Ogura, K., Satsukawa, M., Okuda, H., Hiratsuka, A., and Watabe, T., Major hydroxysteroid sulfotransferase STa in rat liver cytosol may consist of two microheterogeneous subunits, Chem.-Biol. Interact., 129, 144, 1994.
129. Guo, W.-X. A., Yang, Y.-S., Chen, X., McPhie, P., and Jakoby, W. B., Changes in substrate specificity of the recombinant form of phenol sulfotransferase IV (tyrosine-ester sulfotransferase), Chem.-Biol. Interact., 92, 25, 1994.
130. Falany, C. N., Wheeler, J., Oh, T. S. , and Falany, J. L., Steroid sulfation by expressed human cytosolic sulfotransferases, J. Steroid Biochem. Mol. Biol., 48, 369, 1994.
131. Falany, C. N., Krasnykh, V., and Falany, J. L., Bacterial expression and characterization of a cDNA for human liver estrogen sulfotransferase, J. Steroid Biochem. Mol. Biol., 54, 529, 1995.
132. Song, W.-C., Moore, R., McLachlan, J. A., and Negishi, M., Molecular characterization of a testis-specific estrogen sulfotransferase and aberrant liver expression in obese and diabetogenic C57BL/KsJ-db/db mice, Endocrinology, 136, 2477, 1995.
133. Zheng, Y., Bergold, A., and Duffel, M. W., Affinity labelling of aryl sulfotransferase IV, J. Biol. Chem., 269, 30313, 1994.
134. Porter, T. D., Wilson, T. E. , and Kasper, C. B., Expression of a functional 78,000 dalton mammalian flavoprotein, NADPH-cytochrome P-450 oxidoreductase, in Escherichia coli, Arch. Biochem. Biophys., 254, 353, 1987.
135. Ghrayeb, J., Kimura, H., Takahara, M., Hsiung, H., Masui, Y., and Inouye, M., Secretion cloning vectors in Escherichia coli, EMBO J., 3, 2437, 1984.
136. Shen, A. L., Porter, T. D., Wilson, T. E. , and Kasper, C. B., Structural analysis of the FMN binding domain of NADPH-cytochrome P-450 oxidoreductase by site-directed mutagenesis, J. Biol. Chem., 264, 7584, 1989.
137. Djordjevic, S., Roberts, D. L., Wang, M., Shea, T., Camitta, M. G. W., Masters, B. S. S. , and Kim, J. J. P., Crystallization and preliminary X-ray studies of NADPH-cytochrome P450 reductase, Proc. Natl. Acad. Sci. U.S. A., 92, 3214, 1995.
138. Smith, G. C. W., Tew, D. G., and Wolf, C. R., Dissection of NADPH-cytochrome P450 oxidoreductase into distinct functional domains, Proc. Natl. Acad. Sci. U.S. A., 91, 8710, 1994.
139. 5 and studies on their mechanism of function, Arch. Biochem. Biophys., 312, 554, 1994.
140. 5 with a single tryptophan in the membrane-binding domain, Biochemistry, 30, 10200, 1991.
141. 5, Proc. Natl. Acad. Sci. U.S. A., 83, 9443, 1986.
142. Bell, P. A. and Kasper, C. B., Expression of rat microsomal epoxide hydrolase in Escherichia coli: identification of a histidyl residue essential for catalysis, J. Biol. Chem., 268, 14011, 1993.
143. Knehr, M., Thomas, H., Arand, M., Gebel, T., Zeller, H. D., and Oesch, F., Isolation and characterization of a cDNA encoding rat liver cytosolic epoxide hydrolase and its functional expression in Escherichia coli, J. Biol. Chem., 268, 17623, 1993.
144. Lawton, M. P. and Philpot, R. M., Functional characterization of flavin-containing monooxygenase 1B1 expressed in Saccharomyces cerevisiae and Escherichia coli and analysis of proposed FAD- and membrane-binding domains, J. Biol. Chem., 268, 5728, 1993.
145. Lomri, N., Thomas, J., and Cashman, J. R., Expression in Escherichia coli of the cloned flavin-containing monooxygenase from pig liver, J. Biol. Chem., 268, 5048, 1993.
146. Burnett, V. L., Lawton, M. P., and Philpot, R. M., Cloning and sequencing of flavin-containing monooxygenases FMO3 and FMO4 from rabbit and characterization of FMO3, J. Biol. Chem., 269, 14314, 1994.
147. Rettie, A. E., Lawton, M. P., Sadeque, A. J. M., Meier, G. P., and Philpot, R. M., Prochiral sulfoxidation as a probe for multiple forms of the microsomal flavin-containing monooxygenase: studies with rabbit FMO1, FMO2, FMO3, and FMO5 expressed in Escherichia coli, Arch. Biochem. Biophys., 311, 369, 1994.
148. Overby, L. H., Buckpitt, A. R., Lawton, M. P., Atta-Asafo-Adjei, E., Schulze, J., and Philpot, R. M., Characterization of flavin-containing monooxygenase 5 (FMO5) cloned from human and guinea pig: evidence that the unique catalytic properties of FMO5 are not confined to the rabbit ortholog, Arch. Biochem. Biophys., 317, 275, 1995.
149. Pillot, T., Ouzzine, M., Fournel-Gigleux, S. , Lafaurie, C., Radominska, A., Lester, R., Drake, R., Treat, S. , Siest, G., and Magdalou, J., Characterization of a catalytically active human liver UDP-glucuronosyltransferase expressed as a fusion protein in E. coli, Biochem. Biophys. Res. Commun., 196, 473, 1993.
150. Ouzzine, M., Fournel-Gigleux, S., Pillot, T., Burchell, B., Siest, G., and Magdalou, J., Expression and role of the human UDP-glucuronosyltransferase UGT1*6 in Escherichia coli, EEBS Lett., 339, 195, 1994.
151. Barnes, H. J., Arlotto, M. P., and Waterman, M. R., Expression and enzymatic activity of recombinant cytochrome P450 17α-hydroxylase in Escherichia coli, Proc. Natl. Acad. Sci. U.S. A., 88, 5597, 1991.
152. 2-terminal segment retains catalytic activity and is membrane-bound when expressed in Escherichia coli, J. Biol. Chem., 1991; 266: 7321-7324.
153. Li, Y. C. and Chiang, J. Y. L., The expression of a catalytically active cholesterol 7α-hydroxylase cytochrome P-450 in Escherichia coli, J. Biol. Chem., 266, 19186, 1991.
154. Winters, D. K. and Cederbaum, A. I., Expression of a catalytically active human cytochrome P-4502E1 in Escherichia coli, Biochim. Biophys. Acta, 1156, 43, 1992.
155. Peng, H. M., Ding, X., and Coon, M. J., Isolation and heterologous expression of cloned cDNAs for two rabbit nasal microsomal proteins, CYP2A10 and CYP2A11, that are related to nasal microsomal cytochrome P450 form a, J. Biol. Chem., 268, 17253, 1993.
156. Stormo, G. D., Schneider, T. D., and Gold, L. M., Characterization of translational initiation sites in E. coli, Nucl. Acids Res., 10, 2971, 1982.
157. Jaeger, J. A., Turner, D. H., and Zuker, M., Improved predictions of secondary structures for RNA, Proc. Natl. Acad. Sci. U.S. A., 86, 7706, 1989.
158. Jaeger, J. A., Turner, D. H., and Zuker, M., Predicting optimal and suboptimal secondary structure for RNA, Methods Enzymol., 183, 281, 1989.
159. Richardson, T. H., Hsu, M. H., Kronbach, T., Barnes, H. J., Chan, G., Waterman, M. R., Kemper, B., and Johnson, E. F., Purification and characterization of recombinant-expressed cytochrome P450 2C3 from Escherichia coli: 2C3 encodes the 6β-hydroxylase deficient form of P450 3b, Arch. Biochem. Biophys., 300, 510, 1993.
160. Palmer, C. N. A., Richardson, T. H., Griffin, K. J., Hsu, M. H., Muerhoff, A. S., Clark, J. E., and Johnson, E. F., Characterization of a cDNA encoding a human kidney, cytochrome P-450 4A fatty acid ω-hydroxylase and the cognate enzyme expressed in Escherichia coli, Biochim. Biophys. Acta, 1172, 161, 1993.
161. Nishimoto, M., Clark, J. E., and Masters, B. S. S. , Cytochrome P450 4A4: expression in Escherichia coli, purification, and characterization of catalytic properties, Biochemistry, 32, 8863, 1993.
162. Fisher, C. W., Caudle, D. L., Martin-Wixtrom, C., Quattrochi, L. C., Tukey, R. H., Waterman, M. R., and Estabrook, R. W., High-level expression of functional cytochrome P450 1A2 in Escherichia coli, FASEB J., 6, 759, 1992.
163. Fisher, C. W., Shet, M., Caudle, D. L., Martin-Wixtrom, C., and Estabrook, R. W., Expression of human cytochrome P450s in E. coli, in Abstr. 4th Eur. ISSX Mtg., Bologna, Italy, 1992, 106.
164. John, G. H., Hasler, J. A., He, Y., and Halpert, J. R., Escherichia coli expression and characterization of cytochromes P450 2B11, 2B1, and 2B5, Arch. Biochem. Biophys., 314, 367, 1994.
165. Gillam, E. M. J., Baba, T., Kim, B-R., Ohmori, S., and Guengerich, F. P., Expression of modified human cytochrome P450 3A4 in Escherichia coli and purification and reconstitution of the enzyme, Arch. Biochem. Biophys., 305, 123, 1993.
166. Sandhu, P., Baba, T., and Guengerich, F. P., Expression of modified cytochrome P450 2C10 (2C9) in Escherichia coli, purification, and reconstitution of catalytic activity, Arch. Biochem. Biophys., 306, 443, 1993.
167. Sandhu, P., Guo, Z., Baba, T., Martin, M. V., Tukey, R. H., and Guengerich, F. P., Expression of modified human cytochrome P450 1A2 in Escherichia coli: stabilization, purification, spectral characterization, and catalytic activities of the enzyme, Arch. Biochem. Biophys., 309, 168, 1994.
168. Gillam, E. M. J., Guo, Z., and Guengerich, F. P., Expression of modified human cytochrome P450 2E1 in Escherichia coli, purification, and spectral and catalytic properties, Arch. Biochem. Biophys., 312, 59, 1994.
169. Guo, Z., Gillam, E. M. J., Ohmori, S., Tukey, R. H., and Guengerich, F. P., Expression of modified human cytochrome P450 1A1 in Escherichia coli: effects of 5′ substitution, stabilization, purification, spectral characterization, and catalytic properties, Arch. Biochem. Biophys., 312, 436, 1994.
170. Gillam, E. M. J., Guo, Z., Ueng, Y.-F., Yamazaki, H., Cock, I., Reilly, P. E. B., Hooper, W. D., and Guengerich, F. P., Expression of cytochrome P450 3A5 in Escherichia coli: effects of 5′ modifications, purification, spectral characterization, reconstitution conditions, and catalytic activities,
171. Gillam, E. M. J., Guo, Z., Martin, M. V., Jenkins, C. M., and Guengerich, F. P., Expression of cytochrome P450 2D6 in Escherichia coli, purification, and spectral and catalytic characterization, Arch. Biochem. Biophys., 319, 540, 1995.
172. Gillam, E. M. J., Wunsch, R. M., Zorzi, N. A., Ueng, Y.-F., and Guengerich, F. P., Expression of cytochrome P450 3A7 in Escherichia coli: influence of minor N-terminal changes on expression of recombinant human P450 3A enzymes. Toxicologist, in press.
173. Unger, B. P., Gunsalus, I. C., and Sligar, S. G., Nucleotide sequence of the Pseudomonas putida cytochrome P-450cam gene and its expression in Escherichia coli, J. Biol. Chem., 261, 1158, 1986.
174. Narhi, L. O., Wen, L. P., and Fulco, A. J., Characterization of the protein expressed in Escherichia coli by a recombinant plasmid containing the Bacillus megaterium cytochrome P-450BM-3 gene, Mol. Cell. Biochem., 79, 63, 1988.
175. terp at 2.3 Å resolution, J. Mol. Biol., 236, 1169, 1994.
176. TYR expressed at high levels in Escherichia coli, Arch Biochem Biophys, 322, 369, 1995.
177. Sueyoshi, T., Park, L. J., Moore, R., Juvonen, R. O., and Negishi, M., Molecular engineering of microsomal P450 2a-4 to a stable, water-soluble enzyme, Arch. Biochem. Biophys., 322, 265, 1995.
178. Li, Y. C. and Chiang, J. Y. L., Expression of catalytically active cholesterol 7α-hydroxylase in E. coli, FASEB J., 5, A4597, 1991.
179. Chaurasia, C. S., Alterman, M. A., Lu, P., and Hanzlik, R. P., Biochemical characterization of lauric acid ω-hydroxylation by a CYP4A1/NADPH-cytochrome P450 reductase fusion protein, Arch. Biochem. Biophys., 317, 161, 1995.
180. Kempf, A., Nef, P., and Meyer, U. A., Bacterial expression of spectrally active rat cytochrome P-450 2G1 (P-450 olf), in Abstr. 3rd Int. ISSX Meeting Drug Metabolism: Molecules, Models and Man, Amsterdam, 1991.
181. 2-terminal region on localization in cytosol and membranes, Proc. Natl. Acad. Sci. U.S. A., 90, 2651, 1993.
182. 2-terminal region and expressed in Escherichia coli, Arch. Biochem. Biophys., 318, 446, 1995.
183. Richardson, T. H., Jung, F., Griffin, K. J., Wester, M., Raucy, J. L., Kemper, B., Bornheim, L. M., Hassett, C., Omiecinski, C. J., and Johnson, E. F., A universal approach to the expression of human and rabbit cytochrome P450s of the 2C subfamily in Escherichia coli, Arch. Biochem. Biophys., 323, 87, 1995.
184. Wada, A., Mathew, P. A., Barnes, H. J., Sanders, D., Estabrook, R. W., and Waterman, M. R., Expression of functional bovine cholesterol side chain cleavage cytochrome P450 (P450scc) in Escherichia coli, Arch. Biochem. Biophys., 290, 376, 1991.
185. 2+-chelate affinity purification, and characterization of solubility and aggregation, Arch. Biochem. Biophys., 321, 277, 1995.
186. Xia, Z. and Tai, H. H., Bacterial expression of functional membrane-bound thromboxane synthase having intact sequence and truncated N-terminal hydrophobic segment, Arch. Biochem. Biophys., 321, 531, 1995.
187. 5 in the biosynthesis of androgens by human P450c17, Arch. Biochem. Biophys., 317, 343, 1995.
188. Axén, E., Postlind, H., Sjöberg, H., and Wikvall, K., Liver mitochondrial cytochrome P450 CYP27 and recombinant expressed human CYP27 catalyze 1α-hydroxylation of 25-hydroxyvitamin D3, Proc. Natl. Acad. Sci. U.S. A., 91, 10014, 1994.
189. Strömstedt, M., Rozman, D., and Waterman, M. R., The ubiquitously expressed human CYP51 cDNA encodes lanosterol 14α-demethylase cytochrome P450, Arch. Biochem. Biophys., in press.
190. Woodward, S. I. and Dailey, H. A., Regulation of heme biosynthesis in Escherichia coli, Arch. Biochem. Biophys., 316, 110, 1995.
191. Kery, V., Elleder, D., and Kraus, J. P., d-Aminolevulinate increases heme saturation and yield of human cystathionine β-synthase expressed in Escherichia coli, Arch. Biochem. Biophys., 316, 24, 1995.
192. Dong, M.-S., Yamazaki, H., Guo, Z., and Guengerich, F. P., Recombinant human cytochrome P450 1A2 and an N-terminal truncated form: construction, purification, aggregation properties, and interactions with flavodoxin, ferredoxin, and NADPH-cytochrome P450 reductase, Arch. Biochem. Biophys., in press.
193. Jenkins, C. M. and Waterman, M. R., Flavodoxin and NADPH-flavodoxin reductase from Escherichia coli support bovine cytochrome P450c17 hydroxylase activities, J. Biol. Chem., 269, 27401, 1994.
194. Guengerich, F. P., Martin, M. V., Guo, Z., and Chun, Y.-J., Purification of recombinant human cytochrome P450 enzymes expressed in bacteria, Methods Enzymol., in press.
195. Bordier, C., Phase separation of integral membrane proteins in Triton X-114 solution, J. Biol. Chem., 256, 1604, 1981.
196. Hochuli, E., Dobeli, H., and Schacher, A., A new metal chelate adsorbent selective for proteins and peptides containing neighboring histidaine residues, J. Chromatogr., 411, 177, 1995.
197. PA (P-450IA2), the phenacetin O-deethylase, is primarily responsible for the hepatic 3-demethylation of caffeine and N-oxidation of carcinogenic arylamines, Proc. Natl. Acad. Sci. U.S. A., 86, 7696, 1989.
198. Distlerath, L. M., Reilly, P. E. B., Martin, M. V., Davis, G. G., Wilkinson, G. R., and Guengerich, F. P., Purification and characterization of the human liver cytochromes P-450 involved in debrisoquine 4-hydroxylation and phenacetin O-deethylation, two prototypes for genetic polymorphism in oxidative drug metabolism, J. Biol. Chem., 260, 9057, 1985.
199. Knodell, R. G., Hall, S. D., Wilkinson, G. R., and Guengerich, F. P., Hepatic metabolism of tolbutamide: characterization of the form of cytochrome P-450 involved in methyl hydroxylation and relationship to in vivo disposition, J. Pharmacol. Exp. Ther., 241, 1112, 1987.
200. Yamazaki, H., Guo, Z., and Guengerich, F. P., Selectivity of cytochrome P450 2E1 in chlorzoxazone 6-hydroxylation, Drug Metab. Dispos., 23, 438, 1995.
201. Peter, R., Böcker, R. G., Beaune, P. H., Iwasaki, M., Guengerich, F. P., and Yang, C.-S., Hydroxylation of chlorzoxazone as a specific probe for human liver cytochrome P-450 IIE1, Chem. Res. Toxicol., 3, 566, 1990.
202. Guengerich, F. P., Martin, M. V., Beaune, P. H., Kremers, P., Wolff, T., and Waxman, D. J., Characterization of rat and human liver microsomal cytochrome P-450 forms involved in nifedipine oxidation, a prototype for genetic polymorphism in oxidative drug metabolism, J. Biol. Chem., 261, 5051, 1986.
203. Wrighton, S. A., Brian, W. R., Sari, M. A., Iwasaki, M., Guengerich, F. P., Raucy, J. L., Molowa, D. T., and VandenBranden, M., Studies on the expression and metabolic capabilities of human liver cytochrome P450IIIA5 (HLp3), Mol. Pharmacol., 38, 207, 1990.
204. Shimada, T., Gillam, E. M. J., Sandhu, P., Guo, Z., Tukey, R. H., and Guengerich, F. P., Activation of procarcinogens by human cytochrome P450 enzymes expressed in Escherichia coli. Simplified bacterial systems for genotoxicity assays, Carcinogenesis, 15, 2523, 1994.
205. Yamazaki, H., Inui, Y., Wrighton, S. A., Guengerich, F. P., and Shimada, T., Procarcinogen activation by cytochrome P450 3A4 and 3A5 expressed in Escherichia coli and by human liver microsomes, Carcinogenesis, 16, 2167, 1995.
206. Oda, Y., Yamazaki, H., Shimada, T., and Guengerich, F. P., A new Salmonella typhimurium NM5004 strain expressing rat glutathione S-transferase 5-5: use in detection of genotoxicity of dihaloalkanes using an SOS test system, Carcinogenesis, in press.
207. Thier, R., Pemble, S. E., Taylor, J. B., Humphreys, W. G., Persmark, M., Ketterer, B., and Guengerich, F. P., Expression of mammalian glutathione S-transferase 5-5 in Salmonella typhimurium TA1535 leads to base-pair mutations upon exposure to dihalomethanes, Proc. Natl. Acad. Sci. U.S. A., 90, 8576, 1993.
208. Böhme, V. H., Fischer, H., and Frank, R., Darstellung und Eigenschaften der α-halogenierten Thioäther, Ann. Chem., 563, 54, 1949.
209. 7-guanyl)ethyl]glutathione in DNA, J. Am. Chem. Soc., 110, 3284, 1988.
210. Ahmed, A. E. and Anders, M. W., Metabolism of dihalomethanes to formaldehyde and inorganic halide. I. In vitro studies, Drug Metab. Dispos., 4, 357, 1976.
211. Thier, R., Pemble, S., Kramer, H., Taylor, J. B., Guengerich, F. P., and Ketterer, B., Human glutathione S-transferase T1-1 enhances mutagenicity of 1,2-dibromoethane, dibromomethane, and 1,2,3,4-diepoxybutane in Salmonella typhimurium, Carcinogenesis, in press.
212. Pemble, S., Schroeder, K. R., Spencer, S. R., Meyer, D. J., Hallier, E., Bolt, H. M., Ketterer, B., and Taylor, J. B., Human glutathione S-transferase theta (GSTT1): cDNA cloning and the characterization of a genetic polymorphism, Biochem. J., 300, 271, 1994.
213. Meyer, D. J., Coles, B., Pemble, S. E., Gilmore, K. S., Fraser, G. M., and Ketterer, B., Theta, a new class of glutathione transferases purified from rat and man, Biochem. J., 274, 409, 1991.
214. Reitz, R. H., Mendrala, A., and Guengerich, F. P., In vitro metabolism of methylene chloride in human and animal tissues: use in physiologically-based pharmacokinetic models, Toxicol. Appl. Pharmacol., 97, 230, 1989.
215. Andersen, M. E., Clewell, H. J., III, Gargas, M. L., Smith, F. A., and Reitz, R. H., Physiologically based pharmacokinetics and the risk assessment process for methylene chloride, Toxicol. Appl. Pharmacol., 87, 185, 1987.
216. Anderson, M. W. and Maronpot, R. R., Methylene chloride-induced tumorigenesis, Carcinogenesis, 14, 787, 1993.
217. Wiencke, J. K., Christiani, D. C., and Kelsey, K. T., Bimodal distribution of sensitivity to SCE induction by diepoxybutane in human lymphocytes. I. Correlation with chromosomal abberations, Mutation Res., 248, 17, 1991.
218. Kelsey, K. T., Christiani, D. C., and Wiencke, J. K., Bimodal distribution of sensitivity to SCE induction by diepoxybutane in human lymphocytes. II. Relationship to baseline SCE frequency, Mutation Res., 248, 27, 1991.
219. Wiencke, J. K., Wrensch, M. R., Miike, R., and Petrakis, N. L., Individual susceptibility to induced chromosome damage and its implications for detecting genotoxic exposures in human populations, Cancer Res., 51, 5266, 1991.
220. Tucker, J. D., Auletta, A., Cimino, M. C., Dearfield, K. L., Jacobson-Kram, D., Tice, R. R., and Carrano, A. V., Sister-chromatid exchange: second report of the Gene-Tox program, Mutation Res., 297, 101, 1993.
221. 1, Carcinogenesis, 14, 1371, 1993.
222. Simula, T. P., Glancey, M. J., Söderlund, E. J., Dybing, E., and Wolf, C. R., Increased mutagenicity of 1,2-dibromo-3-chloropropane and tris(2,3-dibromopropyl)phosphate in Salmonella TA100 expressing human glutathione S-transferases, Carcinogenesis, 14, 2303, 1993.
223. Dong, M.-S., Yamazaki, H., Guo, Z., and Guengerich, F. P., Insertion of a thrombin site at the end of the first N-terminal hydrophobic domain of human cytochrome P450 1A2, in Abstr. 1994 Midwest Cytochromes P450 Symp., West Lafayette, IN, September 8 to 9, 1994.
224. Yamazaki, H., Ueng, Y-F., Shimada, T., and Guengerich, F. P., Roles of divalent metal ions in oxidations catalyzed by recombinant cytochrome P450 3A4 and replacement of iron-sulfur proteins and oxygen surrogates, Biochemistry, 34, 8380, 1995.
225. Josephy, P. D., DeBruin, L. S., Lord, H. L., Oak, J., Evans, D. H., Guo, Z., Dong, M-S., and Guengerich, F. P., Bioactivation of aromatic amines by recombinant human cytochrome P450 1A2 expressed in bacteria: a substitute for mammalian tissue preparations in mutagenicity testing, Cancer Res., 55, 799, 1995.
226. Dong, M.-S., Guo, Z., Phillips, D., Bell, L. C., Blair, I. A., Gillam, E. M. J., Baba, T., Waterman, M. R., and Guengerich, F. P., Retention of N-formylmethionine in recombinant bacterial cytochrome P450 enzymes containing the N-terminal sequence MALLLAVFL., FASEB J., 9, A1486, 1995.
227. Schoner, B. E. , Belagaje, R. M., and Schoner, R. G., Enhanced translational efficiency with two-cistron expression system, Methods Enzymol., 185, 94, 1990.
228. Ito, W. and Kurosawa, Y., Development of a prokaryotic expression vector that exploits dicistronic gene organization, Gene, 118, 87, 1992.
229. Murakami, H., Yabusaki, Y., Sakaki, T., Shibata, M., and Ohkawa, H., A genetically engineered P450 monooxygenase: construction of the functional fused enzyme between rat cytochrome P450c and NADPH-cytochrome P450 reductase, DNA, 6, 189, 1987.
230. Narhi, L. O. and Fulco, A. J., Characterization of a catalytically self-sufficient 119,000-dalton cytochrome P-450 monooxygenase induced by barbiturates in Bacillus megaterium, J. Biol. Chem., 261, 7160, 1986.
231. White, K. A. and Marletta, M. A., Nitric oxide synthase is a cytochrome P-450 type hemoprotein, Biochemistry, 31, 6627, 1992.
232. McMillan, K., Bredt, D. S., Hirsch, D. J., Snyder, S. H., Clark, J. E., and Masters, B. S. S., Cloned, expressed rat cerebellar nitric oxide synthase contains stoichiometric amounts of heme, which binds carbon monoxide, Proc. Natl. Acad. Sci. U.S. A., 89, 11141, 1992.
233. Stuehr, D. J. and Ikeda-Saito, M., Spectral characterization of brain and macrophage nitric oxide synthases, J. Biol. Chem., 267, 20547, 1992.
234. Gerber, N. C. and Ortiz de Montellano, P. R., Neuronal nitric oxide synthase: expression in Escherichia coli, irreversible inhibition by phenyldiazene, and active site topology, J. Biol. Chem., 270, 17791, 1995.
235. Shet, M. S., Fisher, C. W., Arlotto, M. P., Shackleton, C. H. L., Holmans, P. L., Martin-Wixtrom, C. A., Saeki, Y., and Estabrook, R. W., Purification and enzymatic properties of a recombinant fusion protein expressed in Escherichia coli containing the domains of bovine P450 17A and rat NADPH-P450 reductase, Arch. Biochem. Biophys., 311, 402, 1994.
236. Chun, Y-J., Shimada, T., and Guengerich, F. P., Construction of a human cytochrome P450 1A1:rat NADPH-P450 reductase fusion protein cDNA, expression in Escherichia coli, purification, and catalytic properties of the enzyme in bacterial cells and after purification, Arch. Biochem. Biophys., in press.
237. Shet, M. S., Fisher, C. W., Holmans, P. L., and Estabrook, R. W., Human cytochrome P450 3A4: enzymatic properties of a purified recombinant fusion protein containing NADPH-P450 reductase, Proc. Natl. Acad. Sci. U.S. A., 90, 11748, 1993.
238. Miles, J. S., Munro, A. W., Rospendowski, B. N., Smith, W. E., McKnight, J., and Thomson, A. J., Domains of the catalytically self-sufficient cytochrome P-450 BM-3: genetic construction, overexpression, purification and spectroscopic characterization, Biochem. J., 288, 503, 1992.
239. 5, NADPH-P450 reductase, and lipid on the rate of 6b-hydroxylation of testosterone as catalyzed by a human P450 3A4 fusion protein, Arch. Biochem. Biophys., 318, 314, 1995.
240. Yamazaki, H., Guo, Z., Persmark, M., Mimura, M., Gonzalez, F. J., Sugahara, C., Guengerich, F. P., and Shimada, T., Bufuralol hydroxylation by cytochrome P450 2D6 and 1A2 enzymes in human liver microsomes, Mol. Pharmacol., 46, 568, 1994.
241. Thomas, P. E., Lu, A. Y. H., Ryan, D., West, S. B., Kawalek, J., and Levin, W., Immunochemical evidence for six forms of rat liver cytochrome P450 obtained using antibodies against purified rat liver cytochromes P450 and P448, Mol. Pharmacol., 12, 746, 1976.
242. Kaminsky, L. S. , Fasco, M. J., and Guengerich, F. P., Production and application of antibodies to rat liver cytochrome P-450, Methods Enzymol., 74, 262, 1981.
243. Souček, P., Martin, M. V., Ueng, Y-F., and Guengerich, F. P., Identification of a common epitope near the conserved heme-binding region with polyclonal antibodies raised against cytochrome P450 family 2 proteins, Biochemistry, 34, 16013-16021.
244. Thomas, P. E., Koreniowski, D., Ryan, D., and Levin, W., Preparation of monospecific antibodies against two forms of rat liver cytochrome P-450 and quantitation of these antigens in microsomes, Arch. Biochem. Biophys., 192, 524, 1979.
245. Kadonaga, J. T. and Knowles, J. R., A simple and efficient method for chemical mutagenesis of DNA, Nucleic Acids Res., 1985; 13, 1733, 1985.
246. Dube, D. K. and Loeb, L. A., Mutants generated by the insertion of random oligonucleotides into the active site of the β-lactamase gene, Biochemistry, 28, 5703, 1989.
247. Widersten, M. and Mannervik, B., Glutathione transferases with novel active sites isolated by phage display from a library of random mutants, J. Mol. Biol., 250, 115, 1995.
248. Gulick, A. M. and Fahl, W. E., Forced evolution of glutathione S-transferase to create a more efficient drug detoxication enzyme, Proc. Natl. Acad. Sci. U.S. A., 92, 8140, 1995.
249. Guengerich, F. P., Kim, D-H., and Iwasaki, M., Role of human cytochrome P-450 IIE1 in the oxidation of many low molecular weight cancer suspects, Chem. Res. Toxicol., 4, 168, 1991.
250. Guengerich, F. P., Cytochrome P450 proteins and potential utilization in biodegradation, Environ. Health Perspect., 103 (Suppl. 5), 25, 1995.
251. Shimada, T., Hayes, C. L., Sutter, T., Amin, S. , Hecht, S. S. , Yamazaki, H., and Guengerich, F. P., submitted.
252. Gillam, E. M. J., Zorzi, N. A., Baba, T., and Guengerich, F. P., submitted.
253. Chun, Y.-C. and Guengerich, F. P., unpublished results.
254. Skinner, C. and Waterman, M. R., personal communication.