메뉴 건너뛰기




Volumn 46, Issue 49, 2007, Pages 14010-14017

Interactions of substrates at the surface of P450s can greatly enhance substrate potency

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME SOLVENT INTERFACE; HEME CONTAINING ENZYMES; NICOTINAMIDE;

EID: 37049036628     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi701667m     Document Type: Article
Times cited : (30)

References (42)
  • 1
    • 0022878676 scopus 로고
    • Characterization of a catalytically self-sufficient 119 000 Da cytochrome P450 monooxygenase induced by barbiturates in Bacillus megaterium
    • Narhi, L. O., and Fulco, A. J. (1986) Characterization of a catalytically self-sufficient 119 000 Da cytochrome P450 monooxygenase induced by barbiturates in Bacillus megaterium, J. Biol. Chem. 261, 7160-7169.
    • (1986) J. Biol. Chem , vol.261 , pp. 7160-7169
    • Narhi, L.O.1    Fulco, A.J.2
  • 2
    • 0021018983 scopus 로고
    • Partial characterization of a barbiturate-induced cytochrome P450-dependent fatty acid monooxygenase from Bacillus megaterium
    • Narhi, L. O., Kim, B. H., Stevenson, P. M., and Fulco, A. J. (1983) Partial characterization of a barbiturate-induced cytochrome P450-dependent fatty acid monooxygenase from Bacillus megaterium, Biochem. Biophys. Res. Commun. 116, 851-858.
    • (1983) Biochem. Biophys. Res. Commun , vol.116 , pp. 851-858
    • Narhi, L.O.1    Kim, B.H.2    Stevenson, P.M.3    Fulco, A.J.4
  • 3
    • 0023654743 scopus 로고
    • Cloning of the gene encoding a catalytically self-sufficient cytochrome P450 fatty acid monooxygenase induced by barbiturates in Bacillus megaterium and its functional expression and regulation in heterologous (Escherichia coli) and homologous (Bacillus megaterium) hosts
    • Wen, L. P., and Fulco, A. J. (1987) Cloning of the gene encoding a catalytically self-sufficient cytochrome P450 fatty acid monooxygenase induced by barbiturates in Bacillus megaterium and its functional expression and regulation in heterologous (Escherichia coli) and homologous (Bacillus megaterium) hosts, J. Biol. Chem. 262, 6676-6682.
    • (1987) J. Biol. Chem , vol.262 , pp. 6676-6682
    • Wen, L.P.1    Fulco, A.J.2
  • 4
    • 0023654954 scopus 로고
    • Identification and characterization of two functional domains in cytochrome P450BM-3, a catalytically self-sufficient monooxygenase induced by barbiturates in Bacillus megaterium
    • Narhi, L. O., and Fulco, A. J. (1987) Identification and characterization of two functional domains in cytochrome P450BM-3, a catalytically self-sufficient monooxygenase induced by barbiturates in Bacillus megaterium, J. Biol. Chem. 262, 6683-6690.
    • (1987) J. Biol. Chem , vol.262 , pp. 6683-6690
    • Narhi, L.O.1    Fulco, A.J.2
  • 5
    • 0016738181 scopus 로고
    • Omega-1, Omega-2, and Omega-3 hydroxylation of long-chain fatty acids, amides, and alcohols by a soluble enzyme system from Bacillus megaterium
    • Miura, Y., and Fulco, A. J. (1975) Omega-1, Omega-2, and Omega-3 hydroxylation of long-chain fatty acids, amides, and alcohols by a soluble enzyme system from Bacillus megaterium, Biochim. Biophys Acta 388, 305-317.
    • (1975) Biochim. Biophys Acta , vol.388 , pp. 305-317
    • Miura, Y.1    Fulco, A.J.2
  • 6
    • 0019949651 scopus 로고
    • Phenobarbital induction of a soluble cytochrome P450-dependent fatty acid monooxygenase in Bacillus megaterium
    • Narhi, L. O., and Fulco, A. J. (1982) Phenobarbital induction of a soluble cytochrome P450-dependent fatty acid monooxygenase in Bacillus megaterium, J. Biol. Chem. 257, 2147-2150.
    • (1982) J. Biol. Chem , vol.257 , pp. 2147-2150
    • Narhi, L.O.1    Fulco, A.J.2
  • 7
    • 0021190076 scopus 로고
    • Acylureas: A new class of barbiturate-like bacterial cytochrome P450 inducers
    • Ruettinger, R. T., Kim, B. H., and Fulco, A. J. (1984) Acylureas: A new class of barbiturate-like bacterial cytochrome P450 inducers, Biochim. Biophys. Acta 801, 372-380.
    • (1984) Biochim. Biophys. Acta , vol.801 , pp. 372-380
    • Ruettinger, R.T.1    Kim, B.H.2    Fulco, A.J.3
  • 8
    • 0029941132 scopus 로고    scopus 로고
    • Induction of cytochrome P450BM-3 (CYP 102) by non-steroidal anti-inflammatory drugs in Bacillus megaterium
    • English, N., Hughes, V., and Wolf, C. R. (1996) Induction of cytochrome P450BM-3 (CYP 102) by non-steroidal anti-inflammatory drugs in Bacillus megaterium, Biochem. J. 316, 279-283.
    • (1996) Biochem. J , vol.316 , pp. 279-283
    • English, N.1    Hughes, V.2    Wolf, C.R.3
  • 9
    • 0030696965 scopus 로고    scopus 로고
    • Fatty acid signals in Bacillus megaterium are attenuated by cytochrome P450-mediated hydroxylation
    • English, N., Palmer, C. N., Alworth, W. L., Rang, L., Hughes, V., and Wolf, C. R. (1997) Fatty acid signals in Bacillus megaterium are attenuated by cytochrome P450-mediated hydroxylation, Biochem. J. 327, 363-368.
    • (1997) Biochem. J , vol.327 , pp. 363-368
    • English, N.1    Palmer, C.N.2    Alworth, W.L.3    Rang, L.4    Hughes, V.5    Wolf, C.R.6
  • 10
    • 0032540922 scopus 로고    scopus 로고
    • The repressor protein, Bm3R1, mediates an adaptive response to toxic fatty acids in Bacillus megaterium
    • Palmer, C. N., Axen, E., Hughes, V., and Wolf, C. R. (1998) The repressor protein, Bm3R1, mediates an adaptive response to toxic fatty acids in Bacillus megaterium, J. Biol. Chem. 273, 18109-18116.
    • (1998) J. Biol. Chem , vol.273 , pp. 18109-18116
    • Palmer, C.N.1    Axen, E.2    Hughes, V.3    Wolf, C.R.4
  • 12
    • 0033563872 scopus 로고    scopus 로고
    • P450BM-3: Absolute configuration of the primary metabolites of palmitic acid
    • Truan, G., Komandla, M. R., Falck, J. R., and Peterson, J. A. (1999) P450BM-3: Absolute configuration of the primary metabolites of palmitic acid, Arch. Biochem. Biophys. 366, 192-198.
    • (1999) Arch. Biochem. Biophys , vol.366 , pp. 192-198
    • Truan, G.1    Komandla, M.R.2    Falck, J.R.3    Peterson, J.A.4
  • 13
    • 0036028698 scopus 로고    scopus 로고
    • Sequence alignments, variabilities, and vagaries
    • Graham, S. E., and Peterson, J. A. (2002) Sequence alignments, variabilities, and vagaries, Methods Enzymol. 357, 15-28.
    • (2002) Methods Enzymol , vol.357 , pp. 15-28
    • Graham, S.E.1    Peterson, J.A.2
  • 14
    • 0026684704 scopus 로고
    • Crystallization and preliminary X-ray diffraction analysis of P450terp and the hemoprotein domain of P450BM-3, enzymes belonging to two distinct classes of the cytochrome P450 superfamily
    • Boddupalli, S. S., Hasemann, C. A., Ravichandran, K. G., Lu, J. Y., Goldsmith, E. J., Deisenhofer, J., and Peterson, J. A. (1992) Crystallization and preliminary X-ray diffraction analysis of P450terp and the hemoprotein domain of P450BM-3, enzymes belonging to two distinct classes of the cytochrome P450 superfamily, Proc. Natl. Acad. Sci. U.S.A. 89, 5567-5571.
    • (1992) Proc. Natl. Acad. Sci. U.S.A , vol.89 , pp. 5567-5571
    • Boddupalli, S.S.1    Hasemann, C.A.2    Ravichandran, K.G.3    Lu, J.Y.4    Goldsmith, E.J.5    Deisenhofer, J.6    Peterson, J.A.7
  • 15
    • 0030014679 scopus 로고    scopus 로고
    • The flavoprotein domain of P450BM-3: Expression, purification, and properties of the flavin adenine dinucleotide- and flavin mononucleotide-binding subdomains
    • Sevrioukova, I., Truan, G., and Peterson, J. A. (1996) The flavoprotein domain of P450BM-3: Expression, purification, and properties of the flavin adenine dinucleotide- and flavin mononucleotide-binding subdomains, Biochemistry 35, 7528-7535.
    • (1996) Biochemistry , vol.35 , pp. 7528-7535
    • Sevrioukova, I.1    Truan, G.2    Peterson, J.A.3
  • 16
    • 0025718934 scopus 로고
    • Expression, purification, and properties of the flavoprotein domain of cytochrome P450BM-3. Evidence for the importance of the amino-terminal region for FMN binding
    • Oster, T., Boddupalli, S. S., and Peterson, J. A. (1991) Expression, purification, and properties of the flavoprotein domain of cytochrome P450BM-3. Evidence for the importance of the amino-terminal region for FMN binding, J. Biol. Chem. 266, 22718-22725.
    • (1991) J. Biol. Chem , vol.266 , pp. 22718-22725
    • Oster, T.1    Boddupalli, S.S.2    Peterson, J.A.3
  • 18
    • 0031569880 scopus 로고    scopus 로고
    • Reconstitution of the fatty acid hydroxylase activity of cytochrome P450BM-3 utilizing its functional domains
    • Sevrioukova, I., Truan, G., and Peterson, J. A. (1997) Reconstitution of the fatty acid hydroxylase activity of cytochrome P450BM-3 utilizing its functional domains, Arch. Biochem. Biophys. 340, 231-238.
    • (1997) Arch. Biochem. Biophys , vol.340 , pp. 231-238
    • Sevrioukova, I.1    Truan, G.2    Peterson, J.A.3
  • 20
    • 0031013972 scopus 로고    scopus 로고
    • The structure of the cytochrome p450BM-3 haem domain complexed with the fatty acid substrate, palmitoleic acid
    • Li, H., and Poulos, T. L. (1997) The structure of the cytochrome p450BM-3 haem domain complexed with the fatty acid substrate, palmitoleic acid, Nat. Struct. Biol. 4, 140-146.
    • (1997) Nat. Struct. Biol , vol.4 , pp. 140-146
    • Li, H.1    Poulos, T.L.2
  • 21
  • 22
    • 78651165715 scopus 로고
    • The carbon monoxide-binding pigment of liver microsomes: I. Evidence for its hemoprotein nature
    • Omura, T., and Sato, R. (1964) The carbon monoxide-binding pigment of liver microsomes: I. Evidence for its hemoprotein nature, J. Biol. Chem. 239, 2370-2378.
    • (1964) J. Biol. Chem , vol.239 , pp. 2370-2378
    • Omura, T.1    Sato, R.2
  • 23
    • 0001205667 scopus 로고
    • Use of esters of N-hydroxysuccinimide in the synthesis of N-acylamino acids
    • Lapidot, Y., Rappoport, S., and Wolman, Y. (1967) Use of esters of N-hydroxysuccinimide in the synthesis of N-acylamino acids, J. Lipid Res. 8, 142-145.
    • (1967) J. Lipid Res , vol.8 , pp. 142-145
    • Lapidot, Y.1    Rappoport, S.2    Wolman, Y.3
  • 24
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode, Methods Enzymol. 276, 307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 27
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T. A., Zou, J. Y., Cowan, S. W., and Kjeldgaard. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models, Acta Crystallogr., Sect. A: Found. Crystallogr. 47, 110-119.
    • (1991) Acta Crystallogr., Sect. A: Found. Crystallogr , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard4
  • 28
    • 0024961119 scopus 로고
    • Protein structure. Selecting buried residues [news]
    • Creighton, T. E., and Chothia, C. (1989) Protein structure. Selecting buried residues [news], Nature (London, U.K.) 339, 14-15.
    • (1989) Nature (London, U.K.) , vol.339 , pp. 14-15
    • Creighton, T.E.1    Chothia, C.2
  • 29
    • 0020355139 scopus 로고
    • A quantitative structure-activity relationship study of the inhibitory action of a series of enkephalin-like peptides in the guinea pig ileum and mouse vas deferens bioassays
    • Fauchere, J. L. (1982) A quantitative structure-activity relationship study of the inhibitory action of a series of enkephalin-like peptides in the guinea pig ileum and mouse vas deferens bioassays, J. Med. Chem. 25, 1428-1431.
    • (1982) J. Med. Chem , vol.25 , pp. 1428-1431
    • Fauchere, J.L.1
  • 31
    • 0021930267 scopus 로고
    • Selectivity in the binding of hydroxylated benzo[a]pyrene derivatives to purified cytochrome P450c
    • Turner, C. R., Marcus, C. B., and Jefcoate, C. R. (1985) Selectivity in the binding of hydroxylated benzo[a]pyrene derivatives to purified cytochrome P450c, Biochemistry 24, 5124-5130.
    • (1985) Biochemistry , vol.24 , pp. 5124-5130
    • Turner, C.R.1    Marcus, C.B.2    Jefcoate, C.R.3
  • 32
    • 2642518851 scopus 로고    scopus 로고
    • Quantitative binding models for CYP2C9 based on benzbromarone analogues
    • Locuson, C. W., II, Rock, D. A., and Jones, J. P. (2004) Quantitative binding models for CYP2C9 based on benzbromarone analogues, Biochemistry 43, 6948-6958.
    • (2004) Biochemistry , vol.43 , pp. 6948-6958
    • Locuson II, C.W.1    Rock, D.A.2    Jones, J.P.3
  • 34
    • 33750606810 scopus 로고    scopus 로고
    • A role for the strained phenylalanine ring rotation induced by substrate binding to cytochrome CYP102A1
    • Haines, D. C. (2006) A role for the strained phenylalanine ring rotation induced by substrate binding to cytochrome CYP102A1, Protein Peptide Lett. 13, 977-980.
    • (2006) Protein Peptide Lett , vol.13 , pp. 977-980
    • Haines, D.C.1
  • 35
    • 0035264116 scopus 로고    scopus 로고
    • Structural determinants of active site binding affinity and metabolism by cytochrome P450 BM-3
    • Cowart, L. A., Falck, J. R., and Capdevila, J. H. (2001) Structural determinants of active site binding affinity and metabolism by cytochrome P450 BM-3, Arch. Biochem. Biophys 387, 117-124.
    • (2001) Arch. Biochem. Biophys , vol.387 , pp. 117-124
    • Cowart, L.A.1    Falck, J.R.2    Capdevila, J.H.3
  • 37
    • 0035786599 scopus 로고    scopus 로고
    • The influence of intact-plant and excised-leaf bioassay designs on volicitin- and jasmonic acid-induced sesquiterpene volatile release in Zea mays
    • Schmelz, E. A., Alborn, H. T., and Tumlinson, J. H. (2001) The influence of intact-plant and excised-leaf bioassay designs on volicitin- and jasmonic acid-induced sesquiterpene volatile release in Zea mays, Planta 214, 171-179.
    • (2001) Planta , vol.214 , pp. 171-179
    • Schmelz, E.A.1    Alborn, H.T.2    Tumlinson, J.H.3
  • 38
    • 0036654981 scopus 로고    scopus 로고
    • Synthesis of the (17R)- and (17S)-isomers of volicitin, an elicitor of plant volatiles contained in the oral secretion of the beet army worm
    • Itoh, S., Kuwahara, S., Hasegawa, M., and Kodama, O. (2002) Synthesis of the (17R)- and (17S)-isomers of volicitin, an elicitor of plant volatiles contained in the oral secretion of the beet army worm, Biosci. Biotechnol. Biochem. 66, 1591-1596.
    • (2002) Biosci. Biotechnol. Biochem , vol.66 , pp. 1591-1596
    • Itoh, S.1    Kuwahara, S.2    Hasegawa, M.3    Kodama, O.4
  • 39
    • 0038133337 scopus 로고    scopus 로고
    • Rapid biosynthesis of N-linolenoyl-L-glutamine, an elicitor of plant volatiles, by membrane-associated enzyme(s) in Manduca sexta
    • Lait, C. G., Alborn, H. T., Teal, P. E., and Tumlinson, J. H., III. (2003) Rapid biosynthesis of N-linolenoyl-L-glutamine, an elicitor of plant volatiles, by membrane-associated enzyme(s) in Manduca sexta, Proc. Natl. Acad. Sci. U.S.A. 100, 7027-7032.
    • (2003) Proc. Natl. Acad. Sci. U.S.A , vol.100 , pp. 7027-7032
    • Lait, C.G.1    Alborn, H.T.2    Teal, P.E.3    Tumlinson III, J.H.4
  • 40
    • 4444353509 scopus 로고    scopus 로고
    • Specific incorporation of L-glutamine into volicitin in the regurgitant of Spodoptera litura
    • Yoshinaga, N., Sawada, Y., Nishida, R., Kuwahara, Y., and Mori, N. (2003) Specific incorporation of L-glutamine into volicitin in the regurgitant of Spodoptera litura, Biosci. Biotechnol. Biochem. 67, 2655-2657.
    • (2003) Biosci. Biotechnol. Biochem , vol.67 , pp. 2655-2657
    • Yoshinaga, N.1    Sawada, Y.2    Nishida, R.3    Kuwahara, Y.4    Mori, N.5
  • 41
    • 0346690403 scopus 로고    scopus 로고
    • Interspecies communication in bacteria
    • Federle, M. J., and Bassler, B. L. (2003) Interspecies communication in bacteria, J. Clin. Invest. 112, 1291-1299.
    • (2003) J. Clin. Invest , vol.112 , pp. 1291-1299
    • Federle, M.J.1    Bassler, B.L.2
  • 42
    • 15944383000 scopus 로고    scopus 로고
    • Quorum sensing and quorum-quenching enzymes
    • Dong, Y. H., and Zhang, L. H. (2005) Quorum sensing and quorum-quenching enzymes, J. Microbiol. 43, 101-109.
    • (2005) J. Microbiol , vol.43 , pp. 101-109
    • Dong, Y.H.1    Zhang, L.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.