메뉴 건너뛰기




Volumn 4, Issue 5, 2006, Pages 789-798

Structure-guided recombination creates an artificial family of cytochromes P450

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; CHIMERIC PROTEIN; CYTOCHROME P450; HEMOPROTEIN; LAURIC ACID DERIVATIVE; P NITROPHENOXYDODECANOIC ACID; P-NITROPHENOXYDODECANOIC ACID; RECOMBINANT PROTEIN;

EID: 33646753362     PISSN: 15457885     EISSN: 15457885     Source Type: Journal    
DOI: 10.1371/journal.pbio.0040112     Document Type: Article
Times cited : (128)

References (52)
  • 1
    • 0033536602 scopus 로고    scopus 로고
    • Evolutionarily conserved pathways of energetic connectivity in protein families
    • Lockless SW, Ranganathan R (1999) Evolutionarily conserved pathways of energetic connectivity in protein families. Science 286: 295-299.
    • (1999) Science , vol.286 , pp. 295-299
    • Lockless, S.W.1    Ranganathan, R.2
  • 2
    • 0042767572 scopus 로고    scopus 로고
    • Using multiple sequence correlation analysis to characterize functionally important protein regions
    • Saraf MC, Moore GL, Maranas CD (2003) Using multiple sequence correlation analysis to characterize functionally important protein regions. Protein Eng 16: 397-406.
    • (2003) Protein Eng , vol.16 , pp. 397-406
    • Saraf, M.C.1    Moore, G.L.2    Maranas, C.D.3
  • 3
    • 0035471132 scopus 로고    scopus 로고
    • De novo proteins from combinatorial libraries
    • Moffet DA, Hecht MH (2001) De novo proteins from combinatorial libraries. Chem Rev 101: 3191-3203.
    • (2001) Chem Rev , vol.101 , pp. 3191-3203
    • Moffet, D.A.1    Hecht, M.H.2
  • 5
    • 0035810165 scopus 로고    scopus 로고
    • Functional proteins from a random-sequence library
    • Keefe AD, Szostak JW (2001) Functional proteins from a random-sequence library. Nature 410: 715-718.
    • (2001) Nature , vol.410 , pp. 715-718
    • Keefe, A.D.1    Szostak, J.W.2
  • 6
    • 4143074011 scopus 로고    scopus 로고
    • Estimating the prevalence of protein sequences adopting functional enzyme folds
    • Axe DD (2004) Estimating the prevalence of protein sequences adopting functional enzyme folds. J Mol Biol 341: 1295-1315.
    • (2004) J Mol Biol , vol.341 , pp. 1295-1315
    • Axe, D.D.1
  • 8
    • 3042681604 scopus 로고    scopus 로고
    • Protein tolerance to random amino acid change
    • Guo HH, Choe J, Loeb LA (2004) Protein tolerance to random amino acid change. Proc Natl Acad Sci USA 101: 9205-9210.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 9205-9210
    • Guo, H.H.1    Choe, J.2    Loeb, L.A.3
  • 9
    • 23444436172 scopus 로고
    • Protein design by binary patterning of polar and nonpolar amino acids
    • Kamtekar S, Schiffer JM, Xiong H, Babik JM, Hecht MH (1993) Protein design by binary patterning of polar and nonpolar amino acids. Science 262: 1680-1685.
    • (1993) Science , vol.262 , pp. 1680-1685
    • Kamtekar, S.1    Schiffer, J.M.2    Xiong, H.3    Babik, J.M.4    Hecht, M.H.5
  • 11
    • 0034625013 scopus 로고    scopus 로고
    • DNA polymerase active site is highly mutable: Evolutionary consequences
    • Patel PH, Loeb LA (2000) DNA polymerase active site is highly mutable: Evolutionary consequences. Proc Natl Acad Sci USA 97: 5095-5100.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 5095-5100
    • Patel, P.H.1    Loeb, L.A.2
  • 13
    • 3042655537 scopus 로고    scopus 로고
    • Computational design of a biologically active enzyme
    • Dwyer MA, Looger LL, Hellinga HW (2004) Computational design of a biologically active enzyme. Science 304: 1967-1971.
    • (2004) Science , vol.304 , pp. 1967-1971
    • Dwyer, M.A.1    Looger, L.L.2    Hellinga, H.W.3
  • 19
    • 0346662942 scopus 로고    scopus 로고
    • Nelson D (2006) Cytochrome P450 Homepage. Available: http://drnelson. utmem.edu/CytochromeP450.html. Accessed 6 March 2006.
    • (2006) Cytochrome P450 Homepage
    • Nelson, D.1
  • 22
    • 2442552990 scopus 로고    scopus 로고
    • Expression, purification, and characterization of bacillus subtilis cytochromes P450 CYP102A2 and CYP102A3: Flavocytochrome homologues of P450 BM3 from Bacillus megaterium
    • Gustafsson MC, Roitel O, Marshall KR, Noble MA, Chapman SK, et al. (2004) Expression, purification, and characterization of bacillus subtilis cytochromes P450 CYP102A2 and CYP102A3: Flavocytochrome homologues of P450 BM3 from Bacillus megaterium. Biochemistry 43: 5474-5487.
    • (2004) Biochemistry , vol.43 , pp. 5474-5487
    • Gustafsson, M.C.1    Roitel, O.2    Marshall, K.R.3    Noble, M.A.4    Chapman, S.K.5
  • 23
    • 0011171217 scopus 로고    scopus 로고
    • Regioselectivity and activity of cytochrome P450 BM-3 and mutant F87A in reactions driven by hydrogen peroxide
    • Cirino PC, Arnold FH (2002) Regioselectivity and activity of cytochrome P450 BM-3 and mutant F87A in reactions driven by hydrogen peroxide. Adv Synth Catal 344: 932-937.
    • (2002) Adv Synth Catal , vol.344 , pp. 932-937
    • Cirino, P.C.1    Arnold, F.H.2
  • 25
    • 4043109994 scopus 로고    scopus 로고
    • Functional evolution and structural conservation in chimeric cytochromes p450: Calibrating a structure-guided approach
    • Otey CR, Silberg JJ, Voigt CA, Endelman JB, Bandara G, et al. (2004) Functional evolution and structural conservation in chimeric cytochromes p450: Calibrating a structure-guided approach. Chem Biol 11: 309-318.
    • (2004) Chem Biol , vol.11 , pp. 309-318
    • Otey, C.R.1    Silberg, J.J.2    Voigt, C.A.3    Endelman, J.B.4    Bandara, G.5
  • 27
    • 0030816707 scopus 로고    scopus 로고
    • Molecular dynamics study of timecorrelated protein domain motions and molecular flexibility: Cytochrome P450BM-3
    • Arnold GE, Ornstein RL (1997) Molecular dynamics study of timecorrelated protein domain motions and molecular flexibility: Cytochrome P450BM-3. Biophys J 73: 1147-1159.
    • (1997) Biophys J , vol.73 , pp. 1147-1159
    • Arnold, G.E.1    Ornstein, R.L.2
  • 28
    • 0032728219 scopus 로고    scopus 로고
    • Fatty acid metabolism, conformational change, and electron transfer in cytochrome P-450(BM-3)
    • Li H, Poulos TL (1999) Fatty acid metabolism, conformational change, and electron transfer in cytochrome P-450(BM-3). Biochim Biophys Acta 1441: 141-149.
    • (1999) Biochim Biophys Acta , vol.1441 , pp. 141-149
    • Li, H.1    Poulos, T.L.2
  • 29
    • 0031013972 scopus 로고    scopus 로고
    • The structure of the cytochrome p450BM-3 haem domain complexed with the fatty acid substrate, palmitoleic acid
    • Li H, Poulos TL (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
  • 30
    • 0038799745 scopus 로고    scopus 로고
    • General method for sequence-independent site-directed chimeragenesis
    • Hiraga K, Arnold FH (2003) General method for sequence-independent site-directed chimeragenesis. J Mol Biol 330: 287-296.
    • (2003) J Mol Biol , vol.330 , pp. 287-296
    • Hiraga, K.1    Arnold, F.H.2
  • 31
    • 0042815927 scopus 로고    scopus 로고
    • Analysis of shuffled libraries by oligonucleotide probe hybridization
    • Meinhold P, Joern JM, Silberg JJ (2003) Analysis of shuffled libraries by oligonucleotide probe hybridization. Methods Mol Biol 231: 177-187.
    • (2003) Methods Mol Biol , vol.231 , pp. 177-187
    • Meinhold, P.1    Joern, J.M.2    Silberg, J.J.3
  • 32
    • 0141888967 scopus 로고    scopus 로고
    • High-throughput carbon monoxide binding assay for cytochromes P450
    • Otey CR (2003) High-throughput carbon monoxide binding assay for cytochromes P450. Methods Mol Biol 230: 137-139.
    • (2003) Methods Mol Biol , vol.230 , pp. 137-139
    • Otey, C.R.1
  • 33
    • 0026683129 scopus 로고
    • Resonance Raman investigations of Escherichia coli-expressed Pseudomonas putida cytochrome P450 and P420
    • Wells AV, Li P, Champion PM, Martinis SA, Sligar SG (1992) Resonance Raman investigations of Escherichia coli-expressed Pseudomonas putida cytochrome P450 and P420. Biochemistry 31: 4384-4393.
    • (1992) Biochemistry , vol.31 , pp. 4384-4393
    • Wells, A.V.1    Li, P.2    Champion, P.M.3    Martinis, S.A.4    Sligar, S.G.5
  • 34
    • 0030445739 scopus 로고    scopus 로고
    • Probing the heme iron coordination structure of pressure-induced cytochrome P420cam
    • Martinis SA, Blanke SR, Hager LP, Sligar SG, Hoa GH, et al. (1996) Probing the heme iron coordination structure of pressure-induced cytochrome P420cam. Biochemistry 35: 14530-14536.
    • (1996) Biochemistry , vol.35 , pp. 14530-14536
    • Martinis, S.A.1    Blanke, S.R.2    Hager, L.P.3    Sligar, S.G.4    Hoa, G.H.5
  • 35
    • 0141992696 scopus 로고    scopus 로고
    • High-throughput screen for aromatic hydroxylation
    • Otey CR, Joern JM (2003) High-throughput screen for aromatic hydroxylation. Methods Mol Biol 230: 141-148.
    • (2003) Methods Mol Biol , vol.230 , pp. 141-148
    • Otey, C.R.1    Joern, J.M.2
  • 36
    • 0034667190 scopus 로고    scopus 로고
    • High efficiency family shuffling based on multi-step PCR and in vivo DNA recombination in yeast: Statistical and functional analysis of a combinatorial library between human cytochrome P450 1A1 and 1A2
    • Abecassis V, Pompon D, Truan G (2000) High efficiency family shuffling based on multi-step PCR and in vivo DNA recombination in yeast: Statistical and functional analysis of a combinatorial library between human cytochrome P450 1A1 and 1A2. Nucleic Acids Res 28: E88.
    • (2000) Nucleic Acids Res , vol.28
    • Abecassis, V.1    Pompon, D.2    Truan, G.3
  • 37
    • 0141460411 scopus 로고    scopus 로고
    • Thermostabilization of a cytochrome p450 peroxygenase
    • Salazar O, Cirino PC, Arnold FH (2003) Thermostabilization of a cytochrome p450 peroxygenase. Chembiochem 4: 891-893.
    • (2003) Chembiochem , vol.4 , pp. 891-893
    • Salazar, O.1    Cirino, P.C.2    Arnold, F.H.3
  • 38
    • 0034650885 scopus 로고    scopus 로고
    • The use of random chimeragenesis to study structure/function properties of rat and human P450c17
    • Brock BJ, Waterman MR (2000) The use of random chimeragenesis to study structure/function properties of rat and human P450c17. Arch Biochem Biophys 373: 401-408.
    • (2000) Arch Biochem Biophys , vol.373 , pp. 401-408
    • Brock, B.J.1    Waterman, M.R.2
  • 39
    • 0011365787 scopus 로고
    • Hybrid cytochromes P-450 identify a substrate binding domain in P-450IIC5 and P-450IIC4
    • Kronbach T, Larabee TM, Johnson EF (1989) Hybrid cytochromes P-450 identify a substrate binding domain in P-450IIC5 and P-450IIC4. Proc Natl Acad Sci USA 86: 8262-8265.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 8262-8265
    • Kronbach, T.1    Larabee, T.M.2    Johnson, E.F.3
  • 40
    • 0036721218 scopus 로고    scopus 로고
    • Mapping pathways of allosteric communication in GroEL by analysis of correlated mutations
    • Kass I, Horovitz A (2002) Mapping pathways of allosteric communication in GroEL by analysis of correlated mutations. Proteins 48: 611-617.
    • (2002) Proteins , vol.48 , pp. 611-617
    • Kass, I.1    Horovitz, A.2
  • 41
    • 3042842115 scopus 로고    scopus 로고
    • Influence of conservation on calculations of amino acid covariance in multiple sequence alignments
    • Fodor AA, Aldrich RW (2004) Influence of conservation on calculations of amino acid covariance in multiple sequence alignments. Proteins 56: 211-221.
    • (2004) Proteins , vol.56 , pp. 211-221
    • Fodor, A.A.1    Aldrich, R.W.2
  • 42
    • 0037219686 scopus 로고    scopus 로고
    • Evolutionarily conserved networks of residues mediate allosteric communication in proteins
    • Suel GM, Lockless SW, Wall MA, Ranganathan R (2003) Evolutionarily conserved networks of residues mediate allosteric communication in proteins. Nat Struct Biol 10: 59-69.
    • (2003) Nat Struct Biol , vol.10 , pp. 59-69
    • Suel, G.M.1    Lockless, S.W.2    Wall, M.A.3    Ranganathan, R.4
  • 45
    • 0031021585 scopus 로고    scopus 로고
    • An active site substitution, F87V, converts cytochrome P450 BM-3 into a regioand stereoselective (14S,15R)-arachidonic acid epoxygenase
    • Graham-Lorence S, Truan G, Peterson JA, Falck JR, Wei S, et al. (1997) An active site substitution, F87V, converts cytochrome P450 BM-3 into a regioand stereoselective (14S,15R)-arachidonic acid epoxygenase. J Biol Chem 272: 1127-1135.
    • (1997) J Biol Chem , vol.272 , pp. 1127-1135
    • Graham-Lorence, S.1    Truan, G.2    Peterson, J.A.3    Falck, J.R.4    Wei, S.5
  • 46
    • 0034819837 scopus 로고    scopus 로고
    • Protein engineering of Bacillus megaterium CYP102.The oxidation of polycyclic aromatic hydrocarbons
    • Carmichael AB, Wong LL (2001) Protein engineering of Bacillus megaterium CYP102.The oxidation of polycyclic aromatic hydrocarbons. Eur J Biochem 268: 3117-3125.
    • (2001) Eur J Biochem , vol.268 , pp. 3117-3125
    • Carmichael, A.B.1    Wong, L.L.2
  • 48
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties, and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ (1994) CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties, and weight matrix choice. Nucleic Acids Res 22: 4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 49
    • 0025994649 scopus 로고
    • Expression and enzymatic activity of recombinant cytochrome P450 17 alpha-hydroxylase in Escherichia coli
    • Barnes HJ, Arlotto MP, Waterman MR (1991) Expression and enzymatic activity of recombinant cytochrome P450 17 alpha-hydroxylase in Escherichia coli. Proc Natl Acad Sci USA 88: 5597-5601.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 5597-5601
    • Barnes, H.J.1    Arlotto, M.P.2    Waterman, M.R.3
  • 50
    • 0030093840 scopus 로고    scopus 로고
    • Construction of catalase deficient Escherichia coli strains for the production of uricase
    • Nakagawa S, Ishino S, Teshiba S (1996) Construction of catalase deficient Escherichia coli strains for the production of uricase. Biosci Biotechnol Biochem 60: 415-420.
    • (1996) Biosci Biotechnol Biochem , vol.60 , pp. 415-420
    • Nakagawa, S.1    Ishino, S.2    Teshiba, S.3
  • 51
    • 0043269709 scopus 로고    scopus 로고
    • A self-sufficient peroxide-driven hydroxylation biocatalyst
    • Cirino PC, Arnold FH (2003) A self-sufficient peroxide-driven hydroxylation biocatalyst. Angew Chem Int Ed Engl 42: 3299-3301.
    • (2003) Angew Chem Int Ed Engl , vol.42 , pp. 3299-3301
    • Cirino, P.C.1    Arnold, F.H.2
  • 52
    • 0023684064 scopus 로고
    • A general method of in vitro preparation and specific mutagenesis of DNA fragments: Study of protein and DNA interactions
    • Higuchi R, Krummel B, Saiki RK (1988) A general method of in vitro preparation and specific mutagenesis of DNA fragments: Study of protein and DNA interactions. Nucleic Acids Res 16: 7351-7367.
    • (1988) Nucleic Acids Res , vol.16 , pp. 7351-7367
    • Higuchi, R.1    Krummel, B.2    Saiki, R.K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.