메뉴 건너뛰기




Volumn 272, Issue 5, 2005, Pages 1148-1159

Kinetic and binding studies with purified recombinant proteins ferredoxin reductase, ferredoxin and cytochrome P450 comprising the morpholine mono-oxygenase from Mycobacterium sp. strain HE5

Author keywords

Cytochrome P450; Ferredoxin; Ferredoxin reductase; Morpholine mono oxygenase; Mycobacterium

Indexed keywords

CYTOCHROME C; CYTOCHROME P450; FERREDOXIN; FERREDOXIN REDUCTASE; HYBRID PROTEIN; METYRAPONE; MORPHOLINE; NITROBLUE TETRAZOLIUM; OXIDOREDUCTASE; PIPERIDINE; PYRROLE DERIVATIVE; PYRROLIDINE DERIVATIVE; RECOMBINANT PROTEIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; UNCLASSIFIED DRUG; UNSPECIFIC MONOOXYGENASE;

EID: 14644429097     PISSN: 1742464X     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2005.04550.x     Document Type: Article
Times cited : (18)

References (49)
  • 1
    • 0032213230 scopus 로고    scopus 로고
    • Hydroxylation of macrolactones YC-17 and narbomycin is mediated by the pikC-encoded cytochrome P450 in Streptomyces venezuelae
    • Xue Y, Wilson D, Zhao L, Liu H & Sherman DH (1998) Hydroxylation of macrolactones YC-17 and narbomycin is mediated by the pikC-encoded cytochrome P450 in Streptomyces venezuelae. Chem Biol 5, 661-667.
    • (1998) Chem Biol , vol.5 , pp. 661-667
    • Xue, Y.1    Wilson, D.2    Zhao, L.3    Liu, H.4    Sherman, D.H.5
  • 2
    • 0028910531 scopus 로고
    • A cytochrome P450-like gene possibly involved in oleandomycin biosynthesis by Streptomyces antibioticus
    • Rodriguez AM, Olano C, Mendez C, Hutchinson CR & Salas JA (1995) A cytochrome P450-like gene possibly involved in oleandomycin biosynthesis by Streptomyces antibioticus. FEMS Microbiol Lett 127, 117-120.
    • (1995) FEMS Microbiol Lett , vol.127 , pp. 117-120
    • Rodriguez, A.M.1    Olano, C.2    Mendez, C.3    Hutchinson, C.R.4    Salas, J.A.5
  • 3
    • 0029883934 scopus 로고    scopus 로고
    • Organisation of the biosynthetic gene cluster for rapamycin in Streptomyces hygroscopicus: Analysis of genes flanking the polyketide synthase
    • Molnar I, Aparicio JF, Haydock SF, Khaw LE, Schwecke T, Konig A, Staunton J & Leadlay PF (1996) Organisation of the biosynthetic gene cluster for rapamycin in Streptomyces hygroscopicus: analysis of genes flanking the polyketide synthase. Gene 169, 1-7.
    • (1996) Gene , vol.169 , pp. 1-7
    • Molnar, I.1    Aparicio, J.F.2    Haydock, S.F.3    Khaw, L.E.4    Schwecke, T.5    Konig, A.6    Staunton, J.7    Leadlay, P.F.8
  • 4
    • 0036716276 scopus 로고    scopus 로고
    • Cloning and function of sanQ: A gene involved in nikkomycin biosynthesis of Streptomyces ansochromogenes
    • Zeng H, Tan H & Li J (2002) Cloning and function of sanQ: a gene involved in nikkomycin biosynthesis of Streptomyces ansochromogenes. Curr Microbiol 45, 175-179.
    • (2002) Curr Microbiol , vol.45 , pp. 175-179
    • Zeng, H.1    Tan, H.2    Li, J.3
  • 5
    • 0033527407 scopus 로고    scopus 로고
    • Cytochrome P450105D1 (CYP105D1) from Streptomyces griseus: Heterologous expression, activity, and activation effects of multiple xenobiotics
    • Taylor M, Lamb DC, Cannell R, Dawson M & Kelly SL (1999) Cytochrome P450105D1 (CYP105D1) from Streptomyces griseus: heterologous expression, activity, and activation effects of multiple xenobiotics. Biochem Biophys Res Commun 263, 838-842.
    • (1999) Biochem Biophys Res Commun , vol.263 , pp. 838-842
    • Taylor, M.1    Lamb, D.C.2    Cannell, R.3    Dawson, M.4    Kelly, S.L.5
  • 8
    • 0028950304 scopus 로고
    • Degradation of the thiocarbamate herbicide EPTC (S-ethyl dipropylcarbamothioate) and biosafening by Rhodococcus sp. strain NI86/21 involve an inducible cytochrome P-450 system and aldehyde dehydrogenase
    • Nagy I, Schoofs G, Compernolle F, Proost P, Vanderleyden J & de Mot R (1995) Degradation of the thiocarbamate herbicide EPTC (S-ethyl dipropylcarbamothioate) and biosafening by Rhodococcus sp. strain NI86/21 involve an inducible cytochrome P-450 system and aldehyde dehydrogenase. J Bacteriol 177, 676-687.
    • (1995) J Bacteriol , vol.177 , pp. 676-687
    • Nagy, I.1    Schoofs, G.2    Compernolle, F.3    Proost, P.4    Vanderleyden, J.5    De Mot, R.6
  • 9
    • 0024561947 scopus 로고
    • Purification and characterization of a soybean flour-induced cytochrome P-450 from Streptomyces griseus
    • Trower MK, Sariaslani FS & O'Keefe DP (1989) Purification and characterization of a soybean flour-induced cytochrome P-450 from Streptomyces griseus. J Bacteriol 171, 1781-1787.
    • (1989) J Bacteriol , vol.171 , pp. 1781-1787
    • Trower, M.K.1    Sariaslani, F.S.2    O'Keefe, D.P.3
  • 13
    • 0032821359 scopus 로고    scopus 로고
    • Degradation of morpholine, piperidine, and pyrrolidine by mycobacteria: Evidences for the involvement of a cytochrome P450
    • Poupin P, Godon JJ, Zumstein E & Truffaut N (1999) Degradation of morpholine, piperidine, and pyrrolidine by mycobacteria: evidences for the involvement of a cytochrome P450. Can J Microbiol 45, 209-216.
    • (1999) Can J Microbiol , vol.45 , pp. 209-216
    • Poupin, P.1    Godon, J.J.2    Zumstein, E.3    Truffaut, N.4
  • 14
    • 2542509407 scopus 로고    scopus 로고
    • High morpholine degradation rates and formation of cytochrome P450 during growth on different cyclic amines by newly isolated Mycobacterium sp. strain HE5
    • Schräder T, Schuffenhauer G, Sielaff B & Andreesen JR (2000) High morpholine degradation rates and formation of cytochrome P450 during growth on different cyclic amines by newly isolated Mycobacterium sp. strain HE5. Microbiology 146, 1091-1098.
    • (2000) Microbiology , vol.146 , pp. 1091-1098
    • Schräder, T.1    Schuffenhauer, G.2    Sielaff, B.3    Andreesen, J.R.4
  • 15
    • 0034892705 scopus 로고    scopus 로고
    • A cytochrome P450 and a ferredoxin isolated from Mycobacterium sp. strain HE5 after growth on morpholine
    • Sielaff B, Andreesen JR & Schräder T (2001) A cytochrome P450 and a ferredoxin isolated from Mycobacterium sp. strain HE5 after growth on morpholine. Appl Microbiol Biotechnol 56, 458-464.
    • (2001) Appl Microbiol Biotechnol , vol.56 , pp. 458-464
    • Sielaff, B.1    Andreesen, J.R.2    Schräder, T.3
  • 16
    • 0030009067 scopus 로고    scopus 로고
    • Bacterial cytochromes P-450
    • Munro AW & Lindsay JG (1996) Bacterial cytochromes P-450. Mol Microbiol 20, 1115-1125.
    • (1996) Mol Microbiol , vol.20 , pp. 1115-1125
    • Munro, A.W.1    Lindsay, J.G.2
  • 17
    • 0842346285 scopus 로고    scopus 로고
    • Molecular cloning, nucleotide sequencing and expression of genes encoding a cytochrome P450 system involved in secondary amine utilization in Mycobacterium sp. strain RP1
    • Trigui M, Pulvin S, Truffaut N, Thomas D & Poupin P (2004) Molecular cloning, nucleotide sequencing and expression of genes encoding a cytochrome P450 system involved in secondary amine utilization in Mycobacterium sp. strain RP1. Res Microbiol 155, 1-9.
    • (2004) Res Microbiol , vol.155 , pp. 1-9
    • Trigui, M.1    Pulvin, S.2    Truffaut, N.3    Thomas, D.4    Poupin, P.5
  • 18
    • 0024442346 scopus 로고
    • Purification and characterization of cytochrome P-450sca from Streptomyces carbophilus. ML-236B (compactin) induces a cytochrome P-450sca in Streptomyces carbophilus that hydroxylates ML-236B to pravastatin sodium (CS-514), a tissue-selective inhibitor of 3-hydroxy-3-methylglutarylcoenzyme-A reductase
    • Matsuoka T, Miyakoshi S, Tanzawa K, Nakahara K, Hosobuchi M & Serizawa N (1989) Purification and characterization of cytochrome P-450sca from Streptomyces carbophilus. ML-236B (compactin) induces a cytochrome P-450sca in Streptomyces carbophilus that hydroxylates ML-236B to pravastatin sodium (CS-514), a tissue-selective inhibitor of 3-hydroxy-3-methylglutarylcoenzyme-A reductase. Eur J Biochem 184, 707-713.
    • (1989) Eur J Biochem , vol.184 , pp. 707-713
    • Matsuoka, T.1    Miyakoshi, S.2    Tanzawa, K.3    Nakahara, K.4    Hosobuchi, M.5    Serizawa, N.6
  • 19
    • 0039700056 scopus 로고    scopus 로고
    • Purification and characterization of 2-ethoxyphenol-induced cytochrome P450 from Corynebacterium sp. strain EP1
    • Kawahara N, Ikatsu H, Kawata H, Miyoshi S, Tomochika K & Sinoda S (1999) Purification and characterization of 2-ethoxyphenol-induced cytochrome P450 from Corynebacterium sp. strain EP1. Can J Microbiol 45, 833-839.
    • (1999) Can J Microbiol , vol.45 , pp. 833-839
    • Kawahara, N.1    Ikatsu, H.2    Kawata, H.3    Miyoshi, S.4    Tomochika, K.5    Sinoda, S.6
  • 23
    • 0025257597 scopus 로고
    • Putidaredoxin reductase and putidaredoxin. Cloning, sequence determination, and heterologous expression of the proteins
    • Peterson JA, Lorence MC & Amarneh B (1990) Putidaredoxin reductase and putidaredoxin. Cloning, sequence determination, and heterologous expression of the proteins. J Biol Chem 265, 6066-6073.
    • (1990) J Biol Chem , vol.265 , pp. 6066-6073
    • Peterson, J.A.1    Lorence, M.C.2    Amarneh, B.3
  • 24
    • 0023654954 scopus 로고
    • BM-3, a catalytically self-sufficient monooxygenase induced by barbiturates in Bacillus megaterium
    • BM-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
  • 27
    • 0027979002 scopus 로고
    • C-Terminal region of adrenodoxin affects its structural integrity and determines differences in its electron transfer function to cytochrome P-450
    • Uhlmann H, Kraft R & Bernhardt R (1994) C-Terminal region of adrenodoxin affects its structural integrity and determines differences in its electron transfer function to cytochrome P-450. J Biol Chem 269, 22557-22564.
    • (1994) J Biol Chem , vol.269 , pp. 22557-22564
    • Uhlmann, H.1    Kraft, R.2    Bernhardt, R.3
  • 28
    • 0033529797 scopus 로고    scopus 로고
    • Characterization and catalytic properties of the sterol 14α-demethylase from Mycobacterium tuberculosis
    • Bellamine A, Mangla AT, Nes WD & Waterman MR (1999) Characterization and catalytic properties of the sterol 14α-demethylase from Mycobacterium tuberculosis. Proc Natl Acad Sci USA 96, 8937-8942.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 8937-8942
    • Bellamine, A.1    Mangla, A.T.2    Nes, W.D.3    Waterman, M.R.4
  • 30
    • 0141869098 scopus 로고    scopus 로고
    • Crystal structure of putidaredoxin, the [2Fe-2S] component of the P450cam monooxygenase system from Pseudomonas putida
    • Sevrioukova IF, Garcia C, Li H, Bhaskar B & Poulos TL (2003) Crystal structure of putidaredoxin, the [2Fe-2S] component of the P450cam monooxygenase system from Pseudomonas putida. J Mol Biol 333, 377-392.
    • (2003) J Mol Biol , vol.333 , pp. 377-392
    • Sevrioukova, I.F.1    Garcia, C.2    Li, H.3    Bhaskar, B.4    Poulos, T.L.5
  • 31
    • 0037245378 scopus 로고    scopus 로고
    • Expression, purification and characterisation of a Bacillus subtilis ferredoxin: A potential electron transfer donor to cytochrome P450 Biol
    • Green AJ, Munro AW, Cheesman MR, Reid GA, von Wachenfeldt C & Chapman SK (2003) Expression, purification and characterisation of a Bacillus subtilis ferredoxin: a potential electron transfer donor to cytochrome P450 Biol. J Inorg Biochem 93, 92-99.
    • (2003) J Inorg Biochem , vol.93 , pp. 92-99
    • Green, A.J.1    Munro, A.W.2    Cheesman, M.R.3    Reid, G.A.4    Von Wachenfeldt, C.5    Chapman, S.K.6
  • 32
    • 0021111647 scopus 로고
    • Purification and properties of putidaredoxin reductase
    • Roome PW Jr, Philley JC & Peterson JA (1983) Purification and properties of putidaredoxin reductase. J Biol Chem 258, 2593-2598.
    • (1983) J Biol Chem , vol.258 , pp. 2593-2598
    • Roome Jr., P.W.1    Philley, J.C.2    Peterson, J.A.3
  • 33
    • 0036310647 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis FprA, a novel bacterial NADPH-ferredoxin reductase
    • Fischer F, Raimondi D, Aliverti A & Zanetti G (2002) Mycobacterium tuberculosis FprA, a novel bacterial NADPH-ferredoxin reductase. Eur J Biochem 269, 3005-3013.
    • (2002) Eur J Biochem , vol.269 , pp. 3005-3013
    • Fischer, F.1    Raimondi, D.2    Aliverti, A.3    Zanetti, G.4
  • 34
    • 0017065078 scopus 로고
    • Adrenodoxin reductase. Properties of the complexes of reduced enzyme with NADP+ and NADPH
    • Lambeth JD & Kamin H (1976) Adrenodoxin reductase. Properties of the complexes of reduced enzyme with NADP+ and NADPH. J Biol Chem 251, 4299-4306.
    • (1976) J Biol Chem , vol.251 , pp. 4299-4306
    • Lambeth, J.D.1    Kamin, H.2
  • 35
    • 0032211496 scopus 로고    scopus 로고
    • Characterisation of flavodoxin NADP+ oxidoreductase and flavodoxin; key components of electron transfer in Escherichia coli
    • McIver L, Leadbeater C, Campopiano DJ, Baxter RL, Daff SN, Chapman SK & Munro AW (1998) Characterisation of flavodoxin NADP+ oxidoreductase and flavodoxin; key components of electron transfer in Escherichia coli. Eur J Biochem 257, 577-585.
    • (1998) Eur J Biochem , vol.257 , pp. 577-585
    • McIver, L.1    Leadbeater, C.2    Campopiano, D.J.3    Baxter, R.L.4    Daff, S.N.5    Chapman, S.K.6    Munro, A.W.7
  • 36
    • 0025840524 scopus 로고
    • Purification and characterization of a soybean flour-inducible ferredoxin reductase of Streptomyces griseus
    • Ramachandra M, Seetharam R, Emptage MH & Sariaslani FS (1991) Purification and characterization of a soybean flour-inducible ferredoxin reductase of Streptomyces griseus. J Bacteriol 173, 7106-7112.
    • (1991) J Bacteriol , vol.173 , pp. 7106-7112
    • Ramachandra, M.1    Seetharam, R.2    Emptage, M.H.3    Sariaslani, F.S.4
  • 37
    • 0034806268 scopus 로고    scopus 로고
    • Identification of the gene encoding NADH-rubredoxin oxidoreductase in Clostridium acetobutylicum
    • Guedon E & Petitdemange H (2001) Identification of the gene encoding NADH-rubredoxin oxidoreductase in Clostridium acetobutylicum. Biochem Biophys Res Commun 285, 496-502.
    • (2001) Biochem Biophys Res Commun , vol.285 , pp. 496-502
    • Guedon, E.1    Petitdemange, H.2
  • 38
    • 0032575274 scopus 로고    scopus 로고
    • Roles of negatively charged surface residues of putidaredoxin in interactions with redox partners in p450cam monooxygenase system
    • Aoki M, Ishimori K & Morishima I (1998) Roles of negatively charged surface residues of putidaredoxin in interactions with redox partners in p450cam monooxygenase system. Biochim Biophys Acta 1386, 157-167.
    • (1998) Biochim Biophys Acta , vol.1386 , pp. 157-167
    • Aoki, M.1    Ishimori, K.2    Morishima, I.3
  • 39
    • 14644394700 scopus 로고    scopus 로고
    • Cytochrome P450
    • (Messerschmidt A, Huber R, Poulos T & Wieghardt K, eds). Wiley, Chichester
    • Li H (2001) Cytochrome P450. In Handbook of Metalloproteins (Messerschmidt A, Huber R, Poulos T & Wieghardt K, eds). Wiley, Chichester.
    • (2001) Handbook of Metalloproteins
    • Li, H.1
  • 40
    • 0034801865 scopus 로고    scopus 로고
    • Molecular characterization of the 56-kDa CYP153 from Acinetobacter sp. EB104
    • Maier T, Forster HH, Asperger O & Hahn U (2001) Molecular characterization of the 56-kDa CYP153 from Acinetobacter sp. EB104. Biochem Biophys Res Commun 286, 652-658.
    • (2001) Biochem Biophys Res Commun , vol.286 , pp. 652-658
    • Maier, T.1    Forster, H.H.2    Asperger, O.3    Hahn, U.4
  • 42
    • 0017170343 scopus 로고
    • Coupling of spin, substrate, and redox equilibria in cytochrome P450
    • Sligar SG (1976) Coupling of spin, substrate, and redox equilibria in cytochrome P450. Biochemistry 15, 5399-5406.
    • (1976) Biochemistry , vol.15 , pp. 5399-5406
    • Sligar, S.G.1
  • 44
    • 0034708263 scopus 로고    scopus 로고
    • Substrate binding to 15α-hydroxylase (CYP106A2) probed by FT infrared spectroscopic studies of the iron ligand CO stretch vibration
    • Simgen B, Contzen J, Schwarzer R, Bernhardt R & Jung C (2000) Substrate binding to 15α-hydroxylase (CYP106A2) probed by FT infrared spectroscopic studies of the iron ligand CO stretch vibration. Biochem Biophys Res Commun 269, 737-742.
    • (2000) Biochem Biophys Res Commun , vol.269 , pp. 737-742
    • Simgen, B.1    Contzen, J.2    Schwarzer, R.3    Bernhardt, R.4    Jung, C.5
  • 48
  • 49
    • 0031757074 scopus 로고    scopus 로고
    • Biodegradation of N-methylmorpholine-jV-oxide
    • Meister G & Wechsler M (1998) Biodegradation of N-methylmorpholine- jV-oxide. Biodegradation 9, 91-102.
    • (1998) Biodegradation , vol.9 , pp. 91-102
    • Meister, G.1    Wechsler, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.