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Volumn 82, Issue 3, 2014, Pages 491-504

Conservation analysis of class-specific positions in cytochrome P450 monooxygenases: Functional and structural relevance

Author keywords

Conservation; CYP; Database; Heme interaction; P450; Reductase interaction site; Sequence structure function relationship

Indexed keywords

ARGININE; CYTOCHROME P450; GLYCINE; HEME; OXIDOREDUCTASE; PROLINE; TYROSINE;

EID: 84893744481     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.24415     Document Type: Article
Times cited : (30)

References (59)
  • 1
    • 78649449149 scopus 로고    scopus 로고
    • Progress in tracing the evolutionary paths of cytochrome P450
    • Nelson DR. Progress in tracing the evolutionary paths of cytochrome P450. Biochim Biophys Acta 2011;1814:14-18.
    • (2011) Biochim Biophys Acta , vol.1814 , pp. 14-18
    • Nelson, D.R.1
  • 3
    • 73449127232 scopus 로고    scopus 로고
    • The cytochrome P450 engineering database: Integration of biochemical properties
    • Sirim D, Wagner F, Lisitsa A, Pleiss J. The cytochrome P450 engineering database: Integration of biochemical properties. BMC Biochem. 2009;10:27.
    • (2009) BMC Biochem. , vol.10 , pp. 27
    • Sirim, D.1    Wagner, F.2    Lisitsa, A.3    Pleiss, J.4
  • 5
    • 33745652737 scopus 로고    scopus 로고
    • Cytochrome P450 monooxygenases: perspectives for synthetic application
    • Urlacher VB, Eiben S. Cytochrome P450 monooxygenases: perspectives for synthetic application. Trends Biotechnol 2006;24:324-330.
    • (2006) Trends Biotechnol , vol.24 , pp. 324-330
    • Urlacher, V.B.1    Eiben, S.2
  • 6
    • 0037068964 scopus 로고    scopus 로고
    • Clinical importance of the cytochromes P450
    • Nebert DW, Russell DW. Clinical importance of the cytochromes P450. Lancet. 2002;360:1155-1162.
    • (2002) Lancet. , vol.360 , pp. 1155-1162
    • Nebert, D.W.1    Russell, D.W.2
  • 7
    • 0036890399 scopus 로고    scopus 로고
    • The cytochrome P450 superfamily: biochemistry, evolution and drug metabolism in humans
    • Danielson PB. The cytochrome P450 superfamily: biochemistry, evolution and drug metabolism in humans. Curr Drug Metab 2002;3:561-597.
    • (2002) Curr Drug Metab , vol.3 , pp. 561-597
    • Danielson, P.B.1
  • 8
    • 33846473252 scopus 로고    scopus 로고
    • Cytochrome P450 systems-biological variations of electron transport chains
    • Hannemann F, Bichet A, Ewen KM, Bernhardt R. Cytochrome P450 systems-biological variations of electron transport chains. Biochim Biophys Acta 2007;1770:330-344.
    • (2007) Biochim Biophys Acta , vol.1770 , pp. 330-344
    • Hannemann, F.1    Bichet, A.2    Ewen, K.M.3    Bernhardt, R.4
  • 9
    • 0034733026 scopus 로고    scopus 로고
    • Association of cytochromes P450 with their reductases: opposite sign of the electrostatic interactions in P450BM-3 as compared with the microsomal 2B4 system
    • Davydov DR, Kariakin AA, Petushkova NA, Peterson JA. Association of cytochromes P450 with their reductases: opposite sign of the electrostatic interactions in P450BM-3 as compared with the microsomal 2B4 system. Biochemistry 2000;39:6489-6497.
    • (2000) Biochemistry , vol.39 , pp. 6489-6497
    • Davydov, D.R.1    Kariakin, A.A.2    Petushkova, N.A.3    Peterson, J.A.4
  • 10
    • 75149138842 scopus 로고    scopus 로고
    • Exhaustive computational search of ionic-charge clusters that mediate interactions between mammalian cytochrome P450 (CYP) and P450-oxidoreductase (POR) proteins
    • Zawaira A, Gallotta M, Beeton-Kempen N, Coulson L, Marais P, Kuttel M, Blackburn J. Exhaustive computational search of ionic-charge clusters that mediate interactions between mammalian cytochrome P450 (CYP) and P450-oxidoreductase (POR) proteins. Comput Biol Chem 2010;34:42-52.
    • (2010) Comput Biol Chem , vol.34 , pp. 42-52
    • Zawaira, A.1    Gallotta, M.2    Beeton-Kempen, N.3    Coulson, L.4    Marais, P.5    Kuttel, M.6    Blackburn, J.7
  • 11
    • 0023695280 scopus 로고
    • Electrostatic interactions between cytochrome P-450 LM2 and NADPH-cytochrome P-450 reductase
    • Bernhardt R, Kraft R, Otto A, Ruckpaul K. Electrostatic interactions between cytochrome P-450 LM2 and NADPH-cytochrome P-450 reductase. Biomed Biochim Acta. 1988;47:581-592.
    • (1988) Biomed Biochim Acta. , vol.47 , pp. 581-592
    • Bernhardt, R.1    Kraft, R.2    Otto, A.3    Ruckpaul, K.4
  • 12
    • 0023645035 scopus 로고
    • High-resolution crystal structure of cytochrome P450cam
    • Poulos TL, Finzel BC, Howard AJ. High-resolution crystal structure of cytochrome P450cam. J Mol Biol 1987;195:687-700.
    • (1987) J Mol Biol , vol.195 , pp. 687-700
    • Poulos, T.L.1    Finzel, B.C.2    Howard, A.J.3
  • 14
    • 84869078734 scopus 로고    scopus 로고
    • A standard numbering scheme for thiamine diphosphate-dependent decarboxylases
    • Vogel C, Widmann M, Pohl M, Pleiss J. A standard numbering scheme for thiamine diphosphate-dependent decarboxylases. BMC Biochem 2012;13:24.
    • (2012) BMC Biochem , vol.13 , pp. 24
    • Vogel, C.1    Widmann, M.2    Pohl, M.3    Pleiss, J.4
  • 16
    • 84862514282 scopus 로고    scopus 로고
    • Systematic analysis of metallo-beta-lactamases using an automated database
    • Widmann M, Pleiss J, Oelschlaeger P. Systematic analysis of metallo-beta-lactamases using an automated database. Antimicrob Agents Chemother 2012;56:3481-3491.
    • (2012) Antimicrob Agents Chemother , vol.56 , pp. 3481-3491
    • Widmann, M.1    Pleiss, J.2    Oelschlaeger, P.3
  • 18
    • 0031558798 scopus 로고    scopus 로고
    • Standard conformations for the canonical structures of immunoglobulins
    • Al-Lazikani B, Lesk AM, Chothia C. Standard conformations for the canonical structures of immunoglobulins. J Mol Biol 1997;273:927-948.
    • (1997) J Mol Biol , vol.273 , pp. 927-948
    • Al-Lazikani, B.1    Lesk, A.M.2    Chothia, C.3
  • 19
    • 77957924784 scopus 로고    scopus 로고
    • Prediction and analysis of the modular structure of cytochrome P450 monooxygenases
    • Sirim D, Widmann M, Wagner F, Pleiss J. Prediction and analysis of the modular structure of cytochrome P450 monooxygenases. BMC Struct Biol 2010;10:34.
    • (2010) BMC Struct Biol , vol.10 , pp. 34
    • Sirim, D.1    Widmann, M.2    Wagner, F.3    Pleiss, J.4
  • 20
    • 33745911122 scopus 로고    scopus 로고
    • Class-dependent sequence alignment strategy improves the structural and functional modeling of P450s
    • Baudry J, Rupasinghe S, Schuler MA. Class-dependent sequence alignment strategy improves the structural and functional modeling of P450s. Protein Eng Des Sel 2006;19:345-353.
    • (2006) Protein Eng Des Sel , vol.19 , pp. 345-353
    • Baudry, J.1    Rupasinghe, S.2    Schuler, M.A.3
  • 21
    • 77957244650 scopus 로고    scopus 로고
    • Search and clustering orders of magnitude faster than BLAST
    • Edgar RC. Search and clustering orders of magnitude faster than BLAST. Bioinformatics 2010;26:2460-2461.
    • (2010) Bioinformatics , vol.26 , pp. 2460-2461
    • Edgar, R.C.1
  • 23
    • 0042121237 scopus 로고    scopus 로고
    • Multiple sequence alignment with the Clustal series of programs
    • Chenna R. Multiple sequence alignment with the Clustal series of programs. Nucleic Acids Res 2003;31:3497-3500.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3497-3500
    • Chenna, R.1
  • 24
    • 80055082271 scopus 로고    scopus 로고
    • Accelerated Profile HMM Searches
    • Eddy SR. Accelerated Profile HMM Searches. PLoS Comput Biol 2011;7:e1002195.
    • (2011) PLoS Comput Biol , vol.7
    • Eddy, S.R.1
  • 25
    • 0026743174 scopus 로고
    • Multiple protein sequence alignment from tertiary structure comparison: assignment of global and residue confidence levels
    • Russell RB, Barton GJ. Multiple protein sequence alignment from tertiary structure comparison: assignment of global and residue confidence levels. Proteins 1992;14:309-323.
    • (1992) Proteins , vol.14 , pp. 309-323
    • Russell, R.B.1    Barton, G.J.2
  • 26
    • 0028143135 scopus 로고
    • The role of tryptophan 97 of cytochrome P450 BM3 from Bacillus megaterium in catalytic function. Evidence against the "covalent switching" hypothesis of P-450 electron transfer
    • Munro AW, Malarkey K, McKnight J, Thomson AJ, Kelly SM, Price NC, Lindsay JG, Coggins JR, Miles JS. The role of tryptophan 97 of cytochrome P450 BM3 from Bacillus megaterium in catalytic function. Evidence against the "covalent switching" hypothesis of P-450 electron transfer. Biochem J. 1994;303:423-428.
    • (1994) Biochem J. , vol.303 , pp. 423-428
    • Munro, A.W.1    Malarkey, K.2    McKnight, J.3    Thomson, A.J.4    Kelly, S.M.5    Price, N.C.6    Lindsay, J.G.7    Coggins, J.R.8    Miles, J.S.9
  • 27
    • 0024468304 scopus 로고
    • Putidaredoxin competitively inhibits cytochrome b5-cytochrome P-450cam association: a proposed molecular model for a cytochrome P-450cam electron-transfer complex
    • Stayton PS, Poulos TL, Sligar SG. Putidaredoxin competitively inhibits cytochrome b5-cytochrome P-450cam association: a proposed molecular model for a cytochrome P-450cam electron-transfer complex. Biochemistry 1989;28:8201-8205.
    • (1989) Biochemistry , vol.28 , pp. 8201-8205
    • Stayton, P.S.1    Poulos, T.L.2    Sligar, S.G.3
  • 29
    • 67749089303 scopus 로고    scopus 로고
    • How is the reactivity of cytochrome P450cam affected by Thr252X mutation? A QM/MM study for X=serine, valine, alanine, glycine
    • Altarsha M, Benighaus T, Kumar D, Thiel W. How is the reactivity of cytochrome P450cam affected by Thr252X mutation? A QM/MM study for X=serine, valine, alanine, glycine. J Am Chem Soc 2009;131:4755-63.
    • (2009) J Am Chem Soc , vol.131 , pp. 4755-4763
    • Altarsha, M.1    Benighaus, T.2    Kumar, D.3    Thiel, W.4
  • 31
    • 0031846996 scopus 로고    scopus 로고
    • Thr268 in substrate binding and catalysis in P450BM-3
    • Truan G, Peterson JA. Thr268 in substrate binding and catalysis in P450BM-3. Arch Biochem Biophys 1998;349:53-64.
    • (1998) Arch Biochem Biophys , vol.349 , pp. 53-64
    • Truan, G.1    Peterson, J.A.2
  • 33
    • 24744459452 scopus 로고    scopus 로고
    • Crystallographic study on the dioxygen complex of wild-type and mutant cytochrome P450cam. Implications for the dioxygen activation mechanism
    • Nagano S, Poulos TL. Crystallographic study on the dioxygen complex of wild-type and mutant cytochrome P450cam. Implications for the dioxygen activation mechanism. J Biol Chem. 2005;280:31659-31663.
    • (2005) J Biol Chem. , vol.280 , pp. 31659-31663
    • Nagano, S.1    Poulos, T.L.2
  • 34
    • 0000247412 scopus 로고    scopus 로고
    • Proline isomerization and its catalysis in protein folding
    • Oxford: Oxford University Press.
    • Balbach J, Schmid FX. Proline isomerization and its catalysis in protein folding. In: Mechanisms of protein folding. Oxford: Oxford University Press; 2000. pp 212-249.
    • (2000) Mechanisms of protein folding , pp. 212-249
    • Balbach, J.1    Schmid, F.X.2
  • 35
    • 0019443447 scopus 로고
    • The anatomy and taxonomy of protein structure
    • Richardson JS. The anatomy and taxonomy of protein structure. Adv Protein Chem 1981;34:167-339.
    • (1981) Adv Protein Chem , vol.34 , pp. 167-339
    • Richardson, J.S.1
  • 36
    • 0023123051 scopus 로고
    • Isolation, Complementary DNA sequence, and regulation of rat hepatic lauric acid o-hydroxylase (cytochrome P-450LAo)
    • Hardwick JP, Songs B, Huberman E, Gonzalezq FJ. Isolation, Complementary DNA sequence, and regulation of rat hepatic lauric acid o-hydroxylase (cytochrome P-450LAo). J Biol Chem 1987;262:801-810.
    • (1987) J Biol Chem , vol.262 , pp. 801-810
    • Hardwick, J.P.1    Songs, B.2    Huberman, E.3    Gonzalezq, F.J.4
  • 37
    • 0042845800 scopus 로고    scopus 로고
    • Proline can have opposite effects on fast and slow protein folding phases
    • Osváth S, Gruebele M. Proline can have opposite effects on fast and slow protein folding phases. Biophys J 2003;85:1215-1222.
    • (2003) Biophys J , vol.85 , pp. 1215-1222
    • Osváth, S.1    Gruebele, M.2
  • 40
    • 0028103432 scopus 로고
    • Kinetic Solvent Isotope Effects during Oxygen Activation by Cytochrome P-450cam
    • Aikens J, Sligar SG. Kinetic Solvent Isotope Effects during Oxygen Activation by Cytochrome P-450cam. J Am Chem Soc 1994;116:1143-1144.
    • (1994) J Am Chem Soc , vol.116 , pp. 1143-1144
    • Aikens, J.1    Sligar, S.G.2
  • 41
    • 0035856564 scopus 로고    scopus 로고
    • Phenylalanine 393 exerts thermodynamic control over the heme of flavocytochrome P450 BM3
    • Ost TWB, Miles CS, Munro AW, Murdoch J, Reid GA, Chapman SK. Phenylalanine 393 exerts thermodynamic control over the heme of flavocytochrome P450 BM3. Biochemistry 2001;74:13421-13429.
    • (2001) Biochemistry , vol.74 , pp. 13421-13429
    • Ost, T.W.B.1    Miles, C.S.2    Munro, A.W.3    Murdoch, J.4    Reid, G.A.5    Chapman, S.K.6
  • 43
    • 49249113945 scopus 로고    scopus 로고
    • Theoretical and experimental evaluation of a CYP106A2 low homology model and production of mutants with changed activity and selectivity of hydroxylation
    • Lisurek M, Simgen B, Antes I, Bernhardt R. Theoretical and experimental evaluation of a CYP106A2 low homology model and production of mutants with changed activity and selectivity of hydroxylation. Chembiochem 2008;9:1439-1449.
    • (2008) Chembiochem , vol.9 , pp. 1439-1449
    • Lisurek, M.1    Simgen, B.2    Antes, I.3    Bernhardt, R.4
  • 44
    • 0034088779 scopus 로고    scopus 로고
    • The Catalytic Pathway of Cytochrome P450cam at Atomic Resolution
    • Schlichting I. The Catalytic Pathway of Cytochrome P450cam at Atomic Resolution. Science 2000;287:1615-1622.
    • (2000) Science , vol.287 , pp. 1615-1622
    • Schlichting, I.1
  • 47
    • 77449094112 scopus 로고    scopus 로고
    • Crystal structure of CYP24A1, a mitochondrial cytochrome P450 involved in vitamin D metabolism
    • Annalora AJ, Goodin DB, Hong W-X, Zhang Q, Johnson EF, Stout CD. Crystal structure of CYP24A1, a mitochondrial cytochrome P450 involved in vitamin D metabolism. J Mol Biol 2010;396:441-451.
    • (2010) J Mol Biol , vol.396 , pp. 441-451
    • Annalora, A.J.1    Goodin, D.B.2    Hong, W.-X.3    Zhang, Q.4    Johnson, E.F.5    Stout, C.D.6
  • 48
    • 0027216444 scopus 로고
    • Role of lysine and arginine residues of cytochrome P450 in the interaction between cytochrome P4502B1 and NADPH-cytochrome P450 reductase
    • Shen SJ, Strobel HW. Role of lysine and arginine residues of cytochrome P450 in the interaction between cytochrome P4502B1 and NADPH-cytochrome P450 reductase. Arch Biochem Biophys 1993;304:257-265.
    • (1993) Arch Biochem Biophys , vol.304 , pp. 257-265
    • Shen, S.J.1    Strobel, H.W.2
  • 49
    • 0025755694 scopus 로고
    • Probing the role of lysines and arginines in the catalytic function of cytochrome P450d by site-directed mutagenesis
    • Shimizu T, Tateishi T, Hatano M, Fujii-Kuriyama Y. Probing the role of lysines and arginines in the catalytic function of cytochrome P450d by site-directed mutagenesis. J Biol Chem 1991;266:3372-3375.
    • (1991) J Biol Chem , vol.266 , pp. 3372-3375
    • Shimizu, T.1    Tateishi, T.2    Hatano, M.3    Fujii-Kuriyama, Y.4
  • 50
    • 12444335982 scopus 로고    scopus 로고
    • Functional interaction of cytochrome P450 with its redox partners: a critical assessment and update of the topology of predicted contact regions
    • Hlavica P, Schulze J, Lewis DF V. Functional interaction of cytochrome P450 with its redox partners: a critical assessment and update of the topology of predicted contact regions. J Inorg Biochem 2003;96:279-297.
    • (2003) J Inorg Biochem , vol.96 , pp. 279-297
    • Hlavica, P.1    Schulze, J.2    Lewis, D.V.3
  • 51
    • 0025195188 scopus 로고
    • The cytochrome P-450cam binding surface as defined by site-directed mutagenesis and electrostatic modeling
    • Stayton PS, Sligar SG. The cytochrome P-450cam binding surface as defined by site-directed mutagenesis and electrostatic modeling. Biochemistry. 1990;29:7381-7386.
    • (1990) Biochemistry. , vol.29 , pp. 7381-7386
    • Stayton, P.S.1    Sligar, S.G.2
  • 52
    • 79955833019 scopus 로고    scopus 로고
    • Uncovering the role of hydrophobic residues in cytochrome P450-cytochrome P450 reductase interactions
    • Kenaan C, Zhang H, Shea E V, Hollenberg PF. Uncovering the role of hydrophobic residues in cytochrome P450-cytochrome P450 reductase interactions. Biochemistry 2011;50:3957-3967.
    • (2011) Biochemistry , vol.50 , pp. 3957-3967
    • Kenaan, C.1    Zhang, H.2    Shea, E.V.3    Hollenberg, P.F.4
  • 54
    • 0037408258 scopus 로고    scopus 로고
    • Organization of multiple cytochrome P450s with NADPH-cytochrome P450 reductase in membranes
    • Backes WL, Kelley RW. Organization of multiple cytochrome P450s with NADPH-cytochrome P450 reductase in membranes. Pharmacol Therapeut 2003;98:221-233.
    • (2003) Pharmacol Therapeut , vol.98 , pp. 221-233
    • Backes, W.L.1    Kelley, R.W.2
  • 55
    • 0034693705 scopus 로고    scopus 로고
    • Interactions between redox partners in various cytochrome P450 systems: functional and structural aspects
    • Lewis DF, Hlavica P. Interactions between redox partners in various cytochrome P450 systems: functional and structural aspects. Biochim Biophys Acta 2000;1460:353-374.
    • (2000) Biochim Biophys Acta , vol.1460 , pp. 353-374
    • Lewis, D.F.1    Hlavica, P.2
  • 56
    • 14744270949 scopus 로고    scopus 로고
    • Unexpectedly strong energy stabilization inside the hydrophobic core of small protein rubredoxin mediated by aromatic residues: correlated ab initio quantum chemical calculations
    • Vondrásek J, Bendová L, Klusák V, Hobza P. Unexpectedly strong energy stabilization inside the hydrophobic core of small protein rubredoxin mediated by aromatic residues: correlated ab initio quantum chemical calculations. J Am Chem Soc 2005;127:2615-2619.
    • (2005) J Am Chem Soc , vol.127 , pp. 2615-2619
    • Vondrásek, J.1    Bendová, L.2    Klusák, V.3    Hobza, P.4
  • 57
    • 0022419375 scopus 로고
    • Aromatic-aromatic interaction: a mechanism of protein structure stabilization
    • Burley SK, Petsko GA. Aromatic-aromatic interaction: a mechanism of protein structure stabilization. Science 1985;229:23-28.
    • (1985) Science , vol.229 , pp. 23-28
    • Burley, S.K.1    Petsko, G.A.2
  • 58
    • 0029666288 scopus 로고    scopus 로고
    • Role of Arg 112 of cytochrome P450 cam in the electron transfer from reduced putidaredoxin
    • Unno M, Shimada H, Toba Y, Makino R, Ishimura Y. Role of Arg 112 of cytochrome P450 cam in the electron transfer from reduced putidaredoxin. J Biol Chem 1996;271:17869-17874.
    • (1996) J Biol Chem , vol.271 , pp. 17869-17874
    • Unno, M.1    Shimada, H.2    Toba, Y.3    Makino, R.4    Ishimura, Y.5
  • 59
    • 26944462419 scopus 로고    scopus 로고
    • Structures of human microsomal cytochrome P450 2A6 complexed with coumarin and methoxsalen
    • Yano JK, Hsu M-H, Griffin KJ, Stout CD, Johnson EF. Structures of human microsomal cytochrome P450 2A6 complexed with coumarin and methoxsalen. Nat Struct Mol Biol. 2005;12:822-823.
    • (2005) Nat Struct Mol Biol. , vol.12 , pp. 822-823
    • Yano, J.K.1    Hsu, M.-H.2    Griffin, K.J.3    Stout, C.D.4    Johnson, E.F.5


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