메뉴 건너뛰기




Volumn 32, Issue 3-4, 2000, Pages 267-281

What makes P450s work? Searches for answers with known and new P450s

Author keywords

Cytochrome P450; Heterocyclic amines; Indigo; Indole; Phenacetin; Random mutagensis

Indexed keywords

CYTOCHROME P450; PHENACETIN;

EID: 0034538812     PISSN: 03602532     EISSN: None     Source Type: Journal    
DOI: 10.1081/DMR-100102334     Document Type: Conference Paper
Times cited : (18)

References (42)
  • 1
    • 0026564816 scopus 로고
    • Cytochrome P450: Progress and predictions
    • M. J. Coon, X. Ding, S. J. Pernecky, and A. D. N. Vaz, Cytochrome P450: Progress and predictions, FASEB J., 6, 669-673 (1992).
    • (1992) FASEB J. , vol.6 , pp. 669-673
    • Coon, M.J.1    Ding, X.2    Pernecky, S.J.3    Vaz, A.D.N.4
  • 3
    • 0002888510 scopus 로고
    • Human cytochrome P450 enzymes
    • (P. R. Ortiz de Montellano, ed.), Plenum Press, New York
    • F. P. Guengerich, Human cytochrome P450 enzymes, in Cytochrome P450, 2nd ed. (P. R. Ortiz de Montellano, ed.), Plenum Press, New York, 1995, pp. 473-535.
    • (1995) Cytochrome P450, 2nd Ed. , pp. 473-535
    • Guengerich, F.P.1
  • 4
    • 0025895757 scopus 로고
    • Reactions and significance of cytochrome P-450 enzymes
    • F. P. Guengerich, Reactions and significance of cytochrome P-450 enzymes, J. Biol. Chem., 266, 10,019-10,022 (1991).
    • (1991) J. Biol. Chem. , vol.266
    • Guengerich, F.P.1
  • 8
    • 0025922972 scopus 로고
    • BM-3 and other inducible bacterial P450 cytochromes: Biochemistry and regulation
    • BM-3 and other inducible bacterial P450 cytochromes: Biochemistry and regulation, Annu. Rev. Pharmacol. Toxicol., 31, 177-203 (1991).
    • (1991) Annu. Rev. Pharmacol. Toxicol. , vol.31 , pp. 177-203
    • Fulco, A.J.1
  • 9
    • 0033563820 scopus 로고    scopus 로고
    • Unique properties of purified, Escherichia coli-expressed constitutive cytochrome P4504A5
    • G. Hosny, L. J. Roman, M. H. Mostafa, and B. S. S. Masters, Unique properties of purified, Escherichia coli-expressed constitutive cytochrome P4504A5, Arch. Biochem. Biophys., 366, 199-206 (1999).
    • (1999) Arch. Biochem. Biophys. , vol.366 , pp. 199-206
    • Hosny, G.1    Roman, L.J.2    Mostafa, M.H.3    Masters, B.S.S.4
  • 10
    • 0030701529 scopus 로고    scopus 로고
    • Oxidation kinetics of ethanol by human cytochrome P450 2E1. Rate-limiting product release accounts for effects of isotopic hydrogen substitution and cytochrome b5 on steady-state kinetics
    • L. C. Bell and F. P. Guengerich, Oxidation kinetics of ethanol by human cytochrome P450 2E1. Rate-limiting product release accounts for effects of isotopic hydrogen substitution and cytochrome b5 on steady-state kinetics, J. Biol. Chem., 272, 29,643-29,651 (1997).
    • (1997) J. Biol. Chem. , vol.272
    • Bell, L.C.1    Guengerich, F.P.2
  • 11
    • 0033588164 scopus 로고    scopus 로고
    • Kinetics of cytochrome P450 2E1-catalyzed oxidation of ethanol to acetic acid via acetaldehyde
    • L. C. Bell-Parikh and F. P. Guengerich, Kinetics of cytochrome P450 2E1-catalyzed oxidation of ethanol to acetic acid via acetaldehyde, J. Biol. Chem., 274, 23,833-23,840 (1999).
    • (1999) J. Biol. Chem. , vol.274
    • Bell-Parikh, L.C.1    Guengerich, F.P.2
  • 13
    • 33847606787 scopus 로고    scopus 로고
    • A unified mechanism of oxygen activation as determined by cryocrystallography
    • Abstracts, Int. Soc. Study Xenobiotics/Amer. Chem. Soc. - Div. Chem. Toxicol., Nashville, October
    • S. G. Sligar and S. Maves, A unified mechanism of oxygen activation as determined by cryocrystallography, Abstracts, 9th North American Meeting. Int. Soc. Study Xenobiotics/Amer. Chem. Soc. - Div. Chem. Toxicol., Nashville, October 1999, p. 15.
    • (1999) 9th North American Meeting , pp. 15
    • Sligar, S.G.1    Maves, S.2
  • 14
    • 0025186676 scopus 로고
    • Searching sequence space by definably random mutagenesis: Improving the catalytic potency of an enzyme
    • J. D. Hermes, S. C. Blacklow, and J. R. Knowles, Searching sequence space by definably random mutagenesis: Improving the catalytic potency of an enzyme, Proc. Natl. Acad. Sci. USA, 87, 696-700 (1990).
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 696-700
    • Hermes, J.D.1    Blacklow, S.C.2    Knowles, J.R.3
  • 15
    • 0026334373 scopus 로고
    • Enzyme engineering for nonaqueous solvents: Random mutagenesis to enhance activity of subtilisin E in polar organic media
    • K. Chen and F. H. Arnold, Enzyme engineering for nonaqueous solvents: Random mutagenesis to enhance activity of subtilisin E in polar organic media, Bio/Technology, 9, 1073-1077 (1991).
    • (1991) Bio/Technology , vol.9 , pp. 1073-1077
    • Chen, K.1    Arnold, F.H.2
  • 16
    • 33750113139 scopus 로고    scopus 로고
    • Directed evolution of the P450cam specificity
    • R. Laine and P. R. Ortiz de Montellano, Directed evolution of the P450cam specificity, FASEB J., 11, A811 (1997).
    • (1997) FASEB J. , vol.11
    • Laine, R.1    Ortiz De Montellano, P.R.2
  • 17
    • 0006794372 scopus 로고    scopus 로고
    • A visual screening method for identification of functional mutants of recombinant P450 1A2
    • Abstracts, Los Angeles, July
    • C. W. Fisher, M. S. Shet, K. M. Faulkner, and R. W. Estabrook, A visual screening method for identification of functional mutants of recombinant P450 1A2, Abstracts, 11th Int. Sympos. Microsomes and Drug Oxidations. Los Angeles, July 1996, p. 222.
    • (1996) 11th Int. Sympos. Microsomes and Drug Oxidations , pp. 222
    • Fisher, C.W.1    Shet, M.S.2    Faulkner, K.M.3    Estabrook, R.W.4
  • 18
    • 0031041652 scopus 로고    scopus 로고
    • Alanine-scanning mutagenesis of a putative substrate recognition site in human cytochrome P450 3A4: Role of residues 210 and 211 in flavonoid activation and substrate specificity
    • G. R. Harlow and J. R. Halpert, Alanine-scanning mutagenesis of a putative substrate recognition site in human cytochrome P450 3A4: Role of residues 210 and 211 in flavonoid activation and substrate specificity, J. Biol. Chem., 272, 5396-5402 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 5396-5402
    • Harlow, G.R.1    Halpert, J.R.2
  • 19
    • 0029763107 scopus 로고    scopus 로고
    • Identification of retained N-formylmethionine in bacterial recombinant cytochrome P450 proteins with the N-terminal sequence MALLLAVFL . . .: Roles of residues 3-5 in retention and membrane topology
    • M-S. Dong, L. C. Bell, Z. Guo, D. R. Phillips, I. A. Blair, and F. P. Guengerich, Identification of retained N-formylmethionine in bacterial recombinant cytochrome P450 proteins with the N-terminal sequence MALLLAVFL . . .: Roles of residues 3-5 in retention and membrane topology, Biochemistry, 35, 10,031-10,040 (1996).
    • (1996) Biochemistry , vol.35
    • Dong, M.-S.1    Bell, L.C.2    Guo, Z.3    Phillips, D.R.4    Blair, I.A.5    Guengerich, F.P.6
  • 20
    • 33847602115 scopus 로고    scopus 로고
    • Directed evolution of cytochrome P450 thermostability
    • Abstracts, 29 August-2 September, Sendai
    • S. A. Maves and S. G. Sligar, Directed evolution of cytochrome P450 thermostability, Abstracts, 11th Int. Meetg. Cytochrome P450, 29 August-2 September, Sendai, p. 118 (1999).
    • (1999) 11th Int. Meetg. Cytochrome P450 , pp. 118
    • Maves, S.A.1    Sligar, S.G.2
  • 21
    • 0031127850 scopus 로고    scopus 로고
    • Expression, purification, and characterization of a catalytically active human cytochrome P450 1A2:NADPH-cytochrome P450 reductase fusion protein
    • A. Parikh and F. P. Guengerich, Expression, purification, and characterization of a catalytically active human cytochrome P450 1A2:NADPH-cytochrome P450 reductase fusion protein, Protein Express. Purif. 9, 346-354 (1997).
    • (1997) Protein Express. Purif. , vol.9 , pp. 346-354
    • Parikh, A.1    Guengerich, F.P.2
  • 22
    • 0030021995 scopus 로고    scopus 로고
    • 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
    • M-S. Dong, H. Yamazaki, Z. Guo, and F. P. Guengerich, 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., 327, 11-19 (1996).
    • (1996) Arch. Biochem. Biophys. , vol.327 , pp. 11-19
    • Dong, M.-S.1    Yamazaki, H.2    Guo, Z.3    Guengerich, F.P.4
  • 23
    • 0030843652 scopus 로고    scopus 로고
    • Drug metabolism by Escherichia coli expressing human cytochromes P450
    • A. Parikh, E. M. J. Gillam, and F. P. Guengerich, Drug metabolism by Escherichia coli expressing human cytochromes P450, Nature Biotechnol., 15, 784-788 (1997).
    • (1997) Nature Biotechnol. , vol.15 , pp. 784-788
    • Parikh, A.1    Gillam, E.M.J.2    Guengerich, F.P.3
  • 24
    • 0026542989 scopus 로고
    • Substrate recognition sites in cytochrome P450 family 2 (CYP2) proteins inferred from comparative analysis of amino acid and coding nucleotide sequences
    • O. Gotoh, Substrate recognition sites in cytochrome P450 family 2 (CYP2) proteins inferred from comparative analysis of amino acid and coding nucleotide sequences, J. Biol. Chem., 267, 83-90 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 83-90
    • Gotoh, O.1
  • 25
    • 0031896232 scopus 로고    scopus 로고
    • Random mutagenesis via whole plasmid PCR amplification
    • A. Parikh and F. P. Guengerich, Random mutagenesis via whole plasmid PCR amplification, BioTechniques, 24, 428-431 (1998).
    • (1998) BioTechniques , vol.24 , pp. 428-431
    • Parikh, A.1    Guengerich, F.P.2
  • 26
    • 2642703427 scopus 로고    scopus 로고
    • Metabolic activation of aromatic amine mutagens by simultaneous expression of human cytochrome P450 1A2, NADPH-cytochrome P450 reductase, and N-acetyltransferase in Escherichia coli
    • P. D. Josephy, D. H. Evans, A. Parikh, and F. P. Guengerich, Metabolic activation of aromatic amine mutagens by simultaneous expression of human cytochrome P450 1A2, NADPH-cytochrome P450 reductase, and N-acetyltransferase in Escherichia coli, Chem. Res. Toxicol., 11, 70-74 (1998).
    • (1998) Chem. Res. Toxicol. , vol.11 , pp. 70-74
    • Josephy, P.D.1    Evans, D.H.2    Parikh, A.3    Guengerich, F.P.4
  • 27
    • 0033608962 scopus 로고    scopus 로고
    • Selection and characterization of human cytochrome P450 1A2 mutants with altered catalytic properties
    • A. Parikh, P. D. Josephy, and F. P. Guengerich, Selection and characterization of human cytochrome P450 1A2 mutants with altered catalytic properties, Biochemistry, 38, 5283-5289 (1999).
    • (1999) Biochemistry , vol.38 , pp. 5283-5289
    • Parikh, A.1    Josephy, P.D.2    Guengerich, F.P.3
  • 28
    • 0002254766 scopus 로고
    • Analysis and characterization of enzymes
    • (A. W. Hayes, ed.), Raven Press, New York
    • F. P. Guengerich, Analysis and characterization of enzymes, in Principles and Methods of Toxicology (A. W. Hayes, ed.), Raven Press, New York, 1994, pp. 1259-1313.
    • (1994) Principles and Methods of Toxicology , pp. 1259-1313
    • Guengerich, F.P.1
  • 29
    • 0023899032 scopus 로고
    • Cytochrome P-450-catalyzed hydroxylation and carboxylic acid ester cleavage of Hantzsch pyridine esters
    • F. P. Guengerich, L. A. Peterson, and R. H. Böcker, Cytochrome P-450-catalyzed hydroxylation and carboxylic acid ester cleavage of Hantzsch pyridine esters, J. Biol. Chem., 263, 8176-8183 (1988).
    • (1988) J. Biol. Chem. , vol.263 , pp. 8176-8183
    • Guengerich, F.P.1    Peterson, L.A.2    Böcker, R.H.3
  • 30
    • 0028246557 scopus 로고
    • On the mechanism of action of cytochrome P450: Evaluation of hydrogen abstraction in oxygen-dependent alcohol oxidation
    • A. D. N. Vaz and M. J. Coon, On the mechanism of action of cytochrome P450: Evaluation of hydrogen abstraction in oxygen-dependent alcohol oxidation, Biochemistry, 33, 6442-6449 (1994).
    • (1994) Biochemistry , vol.33 , pp. 6442-6449
    • Vaz, A.D.N.1    Coon, M.J.2
  • 31
    • 0033578095 scopus 로고    scopus 로고
    • Laboratory evolution of peroxide-mediated cytochrome P450 hydroxylation
    • H. Joo, Z. L. Lin, and F. H. Arnold, Laboratory evolution of peroxide-mediated cytochrome P450 hydroxylation, Nature, 399, 670-673 (1999).
    • (1999) Nature , vol.399 , pp. 670-673
    • Joo, H.1    Lin, Z.L.2    Arnold, F.H.3
  • 32
    • 0033213940 scopus 로고    scopus 로고
    • A high-throughput digital imaging screen for the discovery and directed evolution of oxygenases
    • H. Joo, A. Arisawa, Z. Lin, and F. H. Arnold, A high-throughput digital imaging screen for the discovery and directed evolution of oxygenases, Chem. Biol., 6, 699-706 (1999).
    • (1999) Chem. Biol. , vol.6 , pp. 699-706
    • Joo, H.1    Arisawa, A.2    Lin, Z.3    Arnold, F.H.4
  • 33
    • 0032967962 scopus 로고    scopus 로고
    • Development of a new genotoxicity test system with Salmonella typhimurium OY1001/1A2 expressing human cytochrome P450 1A2 and NADPH-cytochrome P450 reductase
    • P. Aryal, K. Yoshikawa, T. Terashita, F. P. Guengerich, T. Shimada, and Y. Oda, Development of a new genotoxicity test system with Salmonella typhimurium OY1001/1A2 expressing human cytochrome P450 1A2 and NADPH-cytochrome P450 reductase, Mutat. Res., 442, 113-120 (1999).
    • (1999) Mutat. Res. , vol.442 , pp. 113-120
    • Aryal, P.1    Yoshikawa, K.2    Terashita, T.3    Guengerich, F.P.4    Shimada, T.5    Oda, Y.6
  • 34
    • 0001477412 scopus 로고
    • SOS function tests for studies of chemical carcinogenesis in Salmonella typhimurium TA 1535/ pSK1002, NM2009, and NM3009
    • Gene and Chromosome Analysis (K. W. Adolph, ed.), Academic Press, Orlando, FL
    • T. Shimada, Y. Oda, H. Yamazaki, M. Mimura, and F. P. Guengerich, SOS function tests for studies of chemical carcinogenesis in Salmonella typhimurium TA 1535/ pSK1002, NM2009, and NM3009, Gene and Chromosome Analysis (K. W. Adolph, ed.), Methods in Molecular Genetics Vol. 5, Academic Press, Orlando, FL, 1994, pp. 342-355.
    • (1994) Methods in Molecular Genetics , vol.5 , pp. 342-355
    • Shimada, T.1    Oda, Y.2    Yamazaki, H.3    Mimura, M.4    Guengerich, F.P.5
  • 35
    • 0028981772 scopus 로고
    • Activation of benzylic alcohols to mutagens by rat and human sulfotransferases expressed in Escherichia coli
    • H. Glatt, K. Pauly, A. Czich, J. L. Falany, and C. N. Falany, Activation of benzylic alcohols to mutagens by rat and human sulfotransferases expressed in Escherichia coli, Eur. J. Pharmacol., 293, 173-181 (1995).
    • (1995) Eur. J. Pharmacol. , vol.293 , pp. 173-181
    • Glatt, H.1    Pauly, K.2    Czich, A.3    Falany, J.L.4    Falany, C.N.5
  • 37
    • 0026695811 scopus 로고
    • Salmonella typhimurium strains expressing human arylamine N-acetyltransferases: Metabolism and mutagenic activation of aromatic amines
    • D. M. Grant, P. D. Josephy, H. L. Lord, and L. D. Morrison, Salmonella typhimurium strains expressing human arylamine N-acetyltransferases: Metabolism and mutagenic activation of aromatic amines, Cancer Res., 52, 3961-3964 (1992).
    • (1992) Cancer Res. , vol.52 , pp. 3961-3964
    • Grant, D.M.1    Josephy, P.D.2    Lord, H.L.3    Morrison, L.D.4
  • 39
    • 0031065229 scopus 로고    scopus 로고
    • Biotechnology, bioremediation, and blue genes
    • H. Bialy, Biotechnology, bioremediation, and blue genes, Nature Biotechnol., 15, 110 (1997).
    • (1997) Nature Biotechnol. , vol.15 , pp. 110
    • Bialy, H.1
  • 40
    • 0000941465 scopus 로고
    • Oxidation of carbanions. IV. Oxidation of indoxyl to indigo in basic solution
    • G. A. Russell and G. Kaupp, Oxidation of carbanions. IV. Oxidation of indoxyl to indigo in basic solution, J. Am. Chem. Soc., 91, 3851-3859 (1969).
    • (1969) J. Am. Chem. Soc. , vol.91 , pp. 3851-3859
    • Russell, G.A.1    Kaupp, G.2
  • 42
    • 0015060548 scopus 로고
    • Mammalian indoxyl metabolism and its relation to the formation of urinary indigo pigments
    • J. D. Sapira, S. Somani, A. P. Shapiro, E. T. Scheib, and W. Reihl, Mammalian indoxyl metabolism and its relation to the formation of urinary indigo pigments, Metab. Clin. Exp. 20, 474-486 (1971).
    • (1971) Metab. Clin. Exp. , vol.20 , pp. 474-486
    • Sapira, J.D.1    Somani, S.2    Shapiro, A.P.3    Scheib, E.T.4    Reihl, W.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.