메뉴 건너뛰기




Volumn 14, Issue C, 1996, Pages 57-79

The Molecular Structure of P450S: The Conserved and the Variable Elements

Author keywords

[No Author keywords available]

Indexed keywords


EID: 0006560583     PISSN: 15692558     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1569-2558(08)60340-9     Document Type: Article
Times cited : (3)

References (51)
  • 1
    • 0027283562 scopus 로고
    • The amino-terminal 29 amino acids of cytochrome P450 2C1 are sufficient for retention in the endoplasmic reticulum
    • Ahn K., Szczesna-Skorupa E., and Kemper B. The amino-terminal 29 amino acids of cytochrome P450 2C1 are sufficient for retention in the endoplasmic reticulum. J. Biol. Chem. 268 (1993) 18726-18733
    • (1993) J. Biol. Chem. , vol.268 , pp. 18726-18733
    • Ahn, K.1    Szczesna-Skorupa, E.2    Kemper, B.3
  • 2
    • 23444457486 scopus 로고
    • Functional domains of human aromatase cytochrome P450 characterized by linear alignment and site-directed mutagenesis
    • Amarneh B., Corbin J.C., Peterson J.A., Simpson E.R., and Graham-Lorence S.E. Functional domains of human aromatase cytochrome P450 characterized by linear alignment and site-directed mutagenesis. Mol. Endo. 7 (1993) 1617-1624
    • (1993) Mol. Endo. , vol.7 , pp. 1617-1624
    • Amarneh, B.1    Corbin, J.C.2    Peterson, J.A.3    Simpson, E.R.4    Graham-Lorence, S.E.5
  • 3
    • 0024208742 scopus 로고
    • cam as revealed by site-directed mutagenesis
    • cam as revealed by site-directed mutagenesis. J. Biol. Chem. 263 (1988) 18842-18849
    • (1988) J. Biol. Chem. , vol.263 , pp. 18842-18849
    • Atkins, W.M.1    Sligar, S.G.2
  • 4
    • 0024566973 scopus 로고
    • Molecular recognition in cytochrome P-450: Alteration of regioselective alkane hydroxylation via protein engineering
    • Atkins W.M., and Sligar S.G. Molecular recognition in cytochrome P-450: Alteration of regioselective alkane hydroxylation via protein engineering. J. Am. Chem. Soc. 111 (1989) 2715-2717
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 2715-2717
    • Atkins, W.M.1    Sligar, S.G.2
  • 9
    • 0000747371 scopus 로고
    • The light reversible carbon monoxide inhibition of the steroid c21-hydroxylase system of the adrenal cortex
    • Estabrook R.W., Cooper D.Y., and Rosenthal O. The light reversible carbon monoxide inhibition of the steroid c21-hydroxylase system of the adrenal cortex. Biochemische Zeitschrift 338 (1963) 741-755
    • (1963) Biochemische Zeitschrift , vol.338 , pp. 741-755
    • Estabrook, R.W.1    Cooper, D.Y.2    Rosenthal, O.3
  • 10
    • 0001718982 scopus 로고
    • Studies on pig liver microsomes. I. Enzymic and pigment composition of different microsomal fractions
    • Garfinkel D. Studies on pig liver microsomes. I. Enzymic and pigment composition of different microsomal fractions. Arch. Biochem. Biophys. 77 (1958) 493-509
    • (1958) Arch. Biochem. Biophys. , vol.77 , pp. 493-509
    • Garfinkel, D.1
  • 11
    • 0026542989 scopus 로고
    • Substrate recognition sites in cytochrome P450 family 2 (CYP2) proteins inferred from comparative analyses of amino acid and coding nucleotide sequences
    • Gotoh O. Substrate recognition sites in cytochrome P450 family 2 (CYP2) proteins inferred from comparative analyses of amino acid and coding nucleotide sequences. J. Biol. Chem. 267 (1992) 83-90
    • (1992) J. Biol. Chem. , vol.267 , pp. 83-90
    • Gotoh, O.1
  • 12
    • 0000108223 scopus 로고
    • Evolution, structure, and gene regulation of cytochrome P-450
    • Ruchpaul K. (Ed), Taylor and Francis, London
    • Gotoh O., and Fujii-Kuriyama Y. Evolution, structure, and gene regulation of cytochrome P-450. In: Ruchpaul K. (Ed). Frontiers in Biotransformation (1989), Taylor and Francis, London 195-243
    • (1989) Frontiers in Biotransformation , pp. 195-243
    • Gotoh, O.1    Fujii-Kuriyama, Y.2
  • 14
    • 0015495445 scopus 로고
    • Camphor binding by Pseudomonas putida cytochrome P-450. Kinetics and thermodynamics of the reaction
    • Griffin B.W., and Peterson J.A. Camphor binding by Pseudomonas putida cytochrome P-450. Kinetics and thermodynamics of the reaction. Biochemistry 11 (1972) 4740-4746
    • (1972) Biochemistry , vol.11 , pp. 4740-4746
    • Griffin, B.W.1    Peterson, J.A.2
  • 15
    • 0017831786 scopus 로고
    • cam methylene monooxygenase components: Cytochrome M, putidaredoxin, and pituidaredoxin reductase
    • cam methylene monooxygenase components: Cytochrome M, putidaredoxin, and pituidaredoxin reductase. Methods Enzymol. 52 (1978) 166-188
    • (1978) Methods Enzymol. , vol.52 , pp. 166-188
    • Gunsalus, I.C.1    Wagner, G.C.2
  • 18
    • 0014429758 scopus 로고
    • A soluble cytochrome P450 functional in methylene hydroxylation
    • Katagiri M., Ganguli B.N., and Gunsalus I.C. A soluble cytochrome P450 functional in methylene hydroxylation. J. Biol. Chem. 243 (1968) 3543-3546
    • (1968) J. Biol. Chem. , vol.243 , pp. 3543-3546
    • Katagiri, M.1    Ganguli, B.N.2    Gunsalus, I.C.3
  • 19
    • 0001202995 scopus 로고
    • Pigments of rat liver microsomes
    • Klingenberg M. Pigments of rat liver microsomes. Arch. Biochem. Biophys. 75 (1958) 376-386
    • (1958) Arch. Biochem. Biophys. , vol.75 , pp. 376-386
    • Klingenberg, M.1
  • 20
    • 0025776916 scopus 로고
    • A hypervariable region of P450IIC5 confers progesterone 21-hydroxylase activity to P450IIC1
    • Kronbach T., Kemper B., and Johnson E.F. A hypervariable region of P450IIC5 confers progesterone 21-hydroxylase activity to P450IIC1. Biochemistry 30 (1991) 6097-6102
    • (1991) Biochemistry , vol.30 , pp. 6097-6102
    • Kronbach, T.1    Kemper, B.2    Johnson, E.F.3
  • 21
    • 0025046594 scopus 로고
    • A molecular model for the enzyme cytochrome P450-17α, a major target for the chemotherapy of prostatic cancer
    • Laughton C.A., Neidle S., Zvelebil M.J., and Sternberg J.M.M.J.E. A molecular model for the enzyme cytochrome P450-17α, a major target for the chemotherapy of prostatic cancer. Biochem. Biophys. Res. Commun. 171 (1990) 1160-1167
    • (1990) Biochem. Biophys. Res. Commun. , vol.171 , pp. 1160-1167
    • Laughton, C.A.1    Neidle, S.2    Zvelebil, M.J.3    Sternberg, J.M.M.J.E.4
  • 23
    • 0024976419 scopus 로고
    • Alteration of mouse cytochrome P450coh substrate specificity by mutation of a single amino-acid residue
    • Lindberg R.L.P., and Negishi M. Alteration of mouse cytochrome P450coh substrate specificity by mutation of a single amino-acid residue. Nature 339 (1989) 632-634
    • (1989) Nature , vol.339 , pp. 632-634
    • Lindberg, R.L.P.1    Negishi, M.2
  • 24
    • 77956778400 scopus 로고
    • ω-1, ω-2 or ω-3 hydroxylation of long-chain fatty acids, amides and alcohols by a soluble enzyme system from Bacillus megaterium
    • Miura Y., and Fulco A.J. ω-1, ω-2 or ω-3 hydroxylation of long-chain fatty acids, amides and alcohols by a soluble enzyme system from Bacillus megaterium. Biochim. Biophys. Acta 487 (1975) 487-494
    • (1975) Biochim. Biophys. Acta , vol.487 , pp. 487-494
    • Miura, Y.1    Fulco, A.J.2
  • 25
    • 0022878676 scopus 로고
    • Characterization of a catalytically self-sufficient 119,000-Dalton cytochrome P-450 monooxygenase induced by barbituates in Bacillus megaterium
    • Narhi L.O., and Fulco A.J. Characterization of a catalytically self-sufficient 119,000-Dalton cytochrome P-450 monooxygenase induced by barbituates in Bacillus megaterium. J. Biol. Chem 261 (1986) 7160-7169
    • (1986) J. Biol. Chem , vol.261 , pp. 7160-7169
    • Narhi, L.O.1    Fulco, A.J.2
  • 26
    • 0023654954 scopus 로고
    • BM-3, a catalytically self-sufficient monooygenase induced by barbituates in Bacillus megaterium
    • BM-3, a catalytically self-sufficient monooygenase induced by barbituates in Bacillus megaterium. J. Biol. Chem. 262 (1987) 6683-6690
    • (1987) J. Biol. Chem. , vol.262 , pp. 6683-6690
    • Narhi, L.O.1    Fulco, A.J.2
  • 27
    • 0014757386 scopus 로고
    • A general method applicable to the search for similarities in the amino acid sequence of two proteins
    • Needleman S.B., and Wunsch C.D. A general method applicable to the search for similarities in the amino acid sequence of two proteins. J. Mol. Biol. 48 (1970) 443-453
    • (1970) J. Mol. Biol. , vol.48 , pp. 443-453
    • Needleman, S.B.1    Wunsch, C.D.2
  • 28
  • 29
    • 0023598348 scopus 로고
    • Evolution of cytochrome P-450 proteins
    • Nelson D.R., and Strobel H.W. Evolution of cytochrome P-450 proteins. Mol. Biol. Evol. 4 (1987) 572-593
    • (1987) Mol. Biol. Evol. , vol.4 , pp. 572-593
    • Nelson, D.R.1    Strobel, H.W.2
  • 31
    • 0023918714 scopus 로고
    • On the membrane topology of vertebrate cytochrome P-450 proteins
    • Nelson D.R., and Strobel H.W. On the membrane topology of vertebrate cytochrome P-450 proteins. J. Biol. Chem. 263 (1988) 6038-6050
    • (1988) J. Biol. Chem. , vol.263 , pp. 6038-6050
    • Nelson, D.R.1    Strobel, H.W.2
  • 33
    • 0001045385 scopus 로고
    • A new cytochrome in liver microsomes
    • Omura T., and Sato R. A new cytochrome in liver microsomes. J. Biol. Chem. 237 (1962) 1375-1376
    • (1962) J. Biol. Chem. , vol.237 , pp. 1375-1376
    • Omura, T.1    Sato, R.2
  • 35
    • 0001315041 scopus 로고
    • Camphor binding by Pseudomonas putida cytochrome P-450
    • Peterson J.A. Camphor binding by Pseudomonas putida cytochrome P-450. Arch. Biochem. Biophys. 144 (1971) 678-693
    • (1971) Arch. Biochem. Biophys. , vol.144 , pp. 678-693
    • Peterson, J.A.1
  • 37
    • 0022919721 scopus 로고
    • Crystal structure of substrate-free Pseudomonas putida cytochrome P-450
    • Poulos T.L., Finzell B.C., and Howard A.J. Crystal structure of substrate-free Pseudomonas putida cytochrome P-450. Biochemistry 25 (1986) 5314-5322
    • (1986) Biochemistry , vol.25 , pp. 5314-5322
    • Poulos, T.L.1    Finzell, B.C.2    Howard, A.J.3
  • 40
    • 77956746151 scopus 로고    scopus 로고
    • The flavoprotein domain of P450BM-3: Expression, purification, and properties of the FAD-and FMN-binding sub-domains
    • (in press)
    • Sevrioukova I., Truan G., and Peterson J.A. The flavoprotein domain of P450BM-3: Expression, purification, and properties of the FAD-and FMN-binding sub-domains. Biochemistry (1996) (in press)
    • (1996) Biochemistry
    • Sevrioukova, I.1    Truan, G.2    Peterson, J.A.3
  • 41
    • 0027216444 scopus 로고
    • Role of lysine and arginine residues of cytochrome P450 in the interaction between cytochrome P4502B1 and NADPH-cytochrome P450 reductase
    • Shen S., and Strobel H.W. Role of lysine and arginine residues of cytochrome P450 in the interaction between cytochrome P4502B1 and NADPH-cytochrome P450 reductase. Arch. Biochem. Biophys. 304 (1993) 257-265
    • (1993) Arch. Biochem. Biophys. , vol.304 , pp. 257-265
    • Shen, S.1    Strobel, H.W.2
  • 43
    • 0027323306 scopus 로고
    • Molecular cloning of an allene oxide synthase: A cytochrome P450 specialized for the metabolism of fatty acid hydroperoxides
    • Song W.C., Funk C.D., and Brash A.R. Molecular cloning of an allene oxide synthase: A cytochrome P450 specialized for the metabolism of fatty acid hydroperoxides. Proc. Natl. Acad. Sci. USA 90 (1993) 8519-8523
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 8519-8523
    • Song, W.C.1    Funk, C.D.2    Brash, A.R.3
  • 44
    • 0025195188 scopus 로고
    • cam binding surface as defined by site-directed mutagenesis and electrostatic modeling
    • cam binding surface as defined by site-directed mutagenesis and electrostatic modeling. Biochemistry 29 (1990) 7381-7386
    • (1990) Biochemistry , vol.29 , pp. 7381-7386
    • Stayton, P.S.1    Sligar, S.G.2
  • 45
    • 0027362650 scopus 로고
    • Hydrophobic side chain requirements for lauric acid and progesterone hydroxylation at amino acid 113 in cytochrome P450 2C2, a potential determinant of substrate specificity
    • Straub P., Johnson E.F., and Kemper B. Hydrophobic side chain requirements for lauric acid and progesterone hydroxylation at amino acid 113 in cytochrome P450 2C2, a potential determinant of substrate specificity. Arch. Biochem. Biophys. 306 (1993) 521-527
    • (1993) Arch. Biochem. Biophys. , vol.306 , pp. 521-527
    • Straub, P.1    Johnson, E.F.2    Kemper, B.3
  • 46
    • 0027486820 scopus 로고
    • Cassette mutagenesis of a potential substrate recognition region of cytochrome P450 2C2
    • Straub P., Lloyd M., Johnson E.F., and Kemper B. Cassette mutagenesis of a potential substrate recognition region of cytochrome P450 2C2. J. Biol. Chem. 268 (1993) 21997-22003
    • (1993) J. Biol. Chem. , vol.268 , pp. 21997-22003
    • Straub, P.1    Lloyd, M.2    Johnson, E.F.3    Kemper, B.4
  • 47
    • 0023955730 scopus 로고
    • Positive charges at the NH2 terminus convert the membrane-anchor signal peptide of cytochrome P-450 to a secretory signal peptide
    • Szczesna-Skorupa E., Browne N., Mead D., and Kemper B. Positive charges at the NH2 terminus convert the membrane-anchor signal peptide of cytochrome P-450 to a secretory signal peptide. Proc. Natl. Acad. Sci. USA 85 (1988) 738-742
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 738-742
    • Szczesna-Skorupa, E.1    Browne, N.2    Mead, D.3    Kemper, B.4
  • 48
    • 0024478250 scopus 로고
    • 2-terminal substitutions of basic amino acids induce translocation across the microsomal membrane and glycosylation of rabbit cytochrome P450IIC2
    • 2-terminal substitutions of basic amino acids induce translocation across the microsomal membrane and glycosylation of rabbit cytochrome P450IIC2. J. Cell. Biol. 108 (1989) 1237-1243
    • (1989) J. Cell. Biol. , vol.108 , pp. 1237-1243
    • Szczesna-Skorupa, E.1    Kemper, B.2
  • 50
    • 0024987066 scopus 로고
    • A concept for the mechanism of prostacyclin and thromboxane A2 biosynthesis
    • Samuelsson B., et al. (Ed), Raven Press, Ltd., New York
    • Ullrich V., and Hecker M. A concept for the mechanism of prostacyclin and thromboxane A2 biosynthesis. In: Samuelsson B., et al. (Ed). Advances In Prostaglandin, Thromboxane, and Leukotriene Research 20 (1990), Raven Press, Ltd., New York 95-101
    • (1990) Advances In Prostaglandin, Thromboxane, and Leukotriene Research , vol.20 , pp. 95-101
    • Ullrich, V.1    Hecker, M.2
  • 51
    • 0026488375 scopus 로고
    • Identification by site-directed mutagenesis of two lysine residues in cholesterol side chain cleavage cytochrome P450 that are essential for adrenodoxin binding
    • Wada A., and Waterman M.R. Identification by site-directed mutagenesis of two lysine residues in cholesterol side chain cleavage cytochrome P450 that are essential for adrenodoxin binding. J. Biol. Chem. 267 (1992) 22877-22882
    • (1992) J. Biol. Chem. , vol.267 , pp. 22877-22882
    • Wada, A.1    Waterman, M.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.