메뉴 건너뛰기




Volumn 13, Issue 7, 2012, Pages 8500-8513

Structural analysis of cytochrome P450 105N1 involved in the biosynthesis of the zincophore, coelibactin

Author keywords

CYP105N1; Cytochrome P450; Siderophore; Streptomyces coelicolor A3(2); Zinc chelation

Indexed keywords

COELIBACTIN; CYTOCHROME P450; NONRIBOSOMAL PEPTIDE SYNTHETASE; UNCLASSIFIED DRUG; ZINC; BACTERIAL PROTEIN; OXAZOLE DERIVATIVE; SIDEROPHORE; THIAZOLE DERIVATIVE;

EID: 84864352700     PISSN: 16616596     EISSN: 14220067     Source Type: Journal    
DOI: 10.3390/ijms13078500     Document Type: Article
Times cited : (35)

References (36)
  • 1
    • 0346662942 scopus 로고    scopus 로고
    • Available online, accessed on 3 July 2012
    • Nelson, D.R. The cytochrome P450 homepage. Available online: http://drnelson.uthsc.edu/CytochromeP450.html (accessed on 3 July 2012).
    • The Cytochrome P450 Homepage
    • Nelson, D.R.1
  • 3
    • 77249084638 scopus 로고    scopus 로고
    • Structural diversity of cytochrome P450 enzyme system
    • Omura, T. Structural diversity of cytochrome P450 enzyme system. J. Biochem. 2010, 147, 297-306.
    • (2010) J. Biochem , vol.147 , pp. 297-306
    • Omura, T.1
  • 4
    • 78149373621 scopus 로고    scopus 로고
    • Cytochrome P450 compound I: Capture, characterization and C-H bond activation kinetics
    • Rittle, J.; Green, M.T. Cytochrome P450 compound I: Capture, characterization and C-H bond activation kinetics. Science 2010, 330, 933-937.
    • (2010) Science , vol.330 , pp. 933-937
    • Rittle, J.1    Green, M.T.2
  • 6
    • 0034973773 scopus 로고    scopus 로고
    • Common and uncommon cytochrome P450 reactions related to metabolism and toxicity
    • Guengerich, F.P. Common and uncommon cytochrome P450 reactions related to metabolism and toxicity. Chem. Res. Toxicol. 2001, 14, 611-650.
    • (2001) Chem. Res. Toxicol , vol.14 , pp. 611-650
    • Guengerich, F.P.1
  • 10
    • 0032879027 scopus 로고    scopus 로고
    • Forty years of genetics with Streptomyces, from in vivo through in vitro to in silico
    • Hopwood, D.A. Forty years of genetics with Streptomyces, from in vivo through in vitro to in silico. Microbiology 1999, 145, 2183-2202.
    • (1999) Microbiology , vol.145 , pp. 2183-2202
    • Hopwood, D.A.1
  • 11
    • 33846234743 scopus 로고    scopus 로고
    • Exploiting Streptomyces coelicolor A3(2) P450s as a model for application in drug discovery
    • Lamb, D.C.; Guengerich, F.P.; Kelly, S.L.; Waterman, M.R. Exploiting Streptomyces coelicolor A3(2) P450s as a model for application in drug discovery. Expert Opin. Drug Metab. Toxicol. 2006, 2, 27-40.
    • (2006) Expert Opin. Drug Metab. Toxicol , vol.2 , pp. 27-40
    • Lamb, D.C.1    Guengerich, F.P.2    Kelly, S.L.3    Waterman, M.R.4
  • 12
    • 0023944782 scopus 로고    scopus 로고
    • Purification and reconstitution of the electron transport components for 6-deoxyerythronolide B hydroxylase, a cytochrome P-450 enzyme of macrolide antibiotic (erythromycin) biosynthesis
    • Shafiee, A.; Hutchinson, C.R. Purification and reconstitution of the electron transport components for 6-deoxyerythronolide B hydroxylase, a cytochrome P-450 enzyme of macrolide antibiotic (erythromycin) biosynthesis. J. Bacteriol. 2007, 170, 1548-1553.
    • (2007) J. Bacteriol , vol.170 , pp. 1548-1553
    • Shafiee, A.1    Hutchinson, C.R.2
  • 13
    • 0032552963 scopus 로고    scopus 로고
    • Characterization of the macrolide P-450 hydroxylase from Streptomyces venezuelae which converts narbomycin to picromycin
    • Betlach, M.C.; Kealey, J.T.; Ashley, G.W.; McDaniel, R. Characterization of the macrolide P-450 hydroxylase from Streptomyces venezuelae which converts narbomycin to picromycin. Biochemistry 1998, 37, 14937-14942.
    • (1998) Biochemistry , vol.37 , pp. 14937-14942
    • Betlach, M.C.1    Kealey, J.T.2    Ashley, G.W.3    McDaniel, R.4
  • 14
    • 0024561947 scopus 로고
    • Purification and characterization of a soybean flour-induced cytochrome P-450 from Streptomyces griseus
    • Trower, M.K.; Sariaslani, F.S.; O'Keefe, D.P. Purification and characterization of a soybean flour-induced cytochrome P-450 from Streptomyces griseus. J. Bacteriol. 1989, 171, 1781-1787.
    • (1989) J. Bacteriol , vol.171 , pp. 1781-1787
    • Trower, M.K.1    Sariaslani, F.S.2    O'Keefe, D.P.3
  • 15
    • 77952754570 scopus 로고    scopus 로고
    • Regio- and stereospecificity of filipin hydroxylation sites revealed by crystal structures of cytochrome P450 105P1 and 105D6 from Streptomyces avermitilis
    • Xu, L.H.; Fushinobu, S.; Takamatsu, S.; Wakagi, T.; Ikeda, H.; Shoun, H. Regio- and stereospecificity of filipin hydroxylation sites revealed by crystal structures of cytochrome P450 105P1 and 105D6 from Streptomyces avermitilis. J. Biol. Chem. 2010, 285, 16844-16853.
    • (2010) J. Biol. Chem , vol.285 , pp. 16844-16853
    • Xu, L.H.1    Fushinobu, S.2    Takamatsu, S.3    Wakagi, T.4    Ikeda, H.5    Shoun, H.6
  • 18
    • 43749088055 scopus 로고    scopus 로고
    • Biosynthesis of the sesquiterpene antibiotic albaflavenone in Streptomyces coelicolor A3(2)
    • Zhao, B.; Lin, X.; Lei, L.; Lamb, D.C.; Kelly, S.L.; Waterman, M.R.; Cane, D.E. Biosynthesis of the sesquiterpene antibiotic albaflavenone in Streptomyces coelicolor A3(2). J. Biol. Chem. 2008, 283, 8183-8189.
    • (2008) J. Biol. Chem , vol.283 , pp. 8183-8189
    • Zhao, B.1    Lin, X.2    Lei, L.3    Lamb, D.C.4    Kelly, S.L.5    Waterman, M.R.6    Cane, D.E.7
  • 19
    • 73649089294 scopus 로고    scopus 로고
    • Crystal structure of albaflavenone monooxygenase containing a moonlighting terpene synthase active site
    • Zhao, B.; Lei, L.; Vassylyev, D.G.; Lin, X.; Cane, D.E.; Kelly, S.L.; Yuan, H.; Lamb, D.C.; Waterman, M.R. Crystal structure of albaflavenone monooxygenase containing a moonlighting terpene synthase active site. J. Biol. Chem. 2009, 284, 36711-36719.
    • (2009) J. Biol. Chem , vol.284 , pp. 36711-36719
    • Zhao, B.1    Lei, L.2    Vassylyev, D.G.3    Lin, X.4    Cane, D.E.5    Kelly, S.L.6    Yuan, H.7    Lamb, D.C.8    Waterman, M.R.9
  • 20
    • 72049104812 scopus 로고    scopus 로고
    • The role of absC, a novel regulatory gene for secondary metabolism, in zinc-dependent antibiotic production in Streptomyces coelicolor A3(2)
    • Hesketh, A.; Kock, H.; Mootien, S.; Bibb, M. The role of absC, a novel regulatory gene for secondary metabolism, in zinc-dependent antibiotic production in Streptomyces coelicolor A3(2). Mol. Microbiol. 2009, 74, 1427-1444.
    • (2009) Mol. Microbiol , vol.74 , pp. 1427-1444
    • Hesketh, A.1    Kock, H.2    Mootien, S.3    Bibb, M.4
  • 21
    • 73649136810 scopus 로고    scopus 로고
    • The zinc-responsive regulator Zur controls expression of the coelibactin gene cluster in Streptomyces coelicolor
    • Kallifidas, D.; Pascoe, B.; Owen, G.A.; Strain-Damerell, C.M.; Hong, H.J.; Paget, M.S. The zinc-responsive regulator Zur controls expression of the coelibactin gene cluster in Streptomyces coelicolor. J. Bacteriol. 2010, 192, 608-611.
    • (2010) J. Bacteriol , vol.192 , pp. 608-611
    • Kallifidas, D.1    Pascoe, B.2    Owen, G.A.3    Strain-Damerell, C.M.4    Hong, H.J.5    Paget, M.S.6
  • 24
    • 13044258884 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray diffraction analysis of cytochrome P450sca-2 from Streptomyces carbophilus involved in production of pravastatin sodium, a tissue-selective inhibitor of HMG-CoA reductase
    • Ito, S.; Matsuoka, T.; Watanabe, I.; Kagasaki, T.; Serizawa, N.; Hata, T. Crystallization and preliminary X-ray diffraction analysis of cytochrome P450sca-2 from Streptomyces carbophilus involved in production of pravastatin sodium, a tissue-selective inhibitor of HMG-CoA reductase. Acta Crystallogr. D 1999, 55, 1209-1211.
    • (1999) Acta Crystallogr. D , vol.55 , pp. 1209-1211
    • Ito, S.1    Matsuoka, T.2    Watanabe, I.3    Kagasaki, T.4    Serizawa, N.5    Hata, T.6
  • 26
    • 33646030623 scopus 로고    scopus 로고
    • Purification and characterization of bovine steroid 21-hydroxylase (P450c21) efficiently expressed in Escherichia coli
    • Arase, M.; Waterman, M.R.; Kawaga, N. Purification and characterization of bovine steroid 21-hydroxylase (P450c21) efficiently expressed in Escherichia coli. Biochem. Biophys. Res. Commun. 2006, 344, 400-405.
    • (2006) Biochem. Biophys. Res. Commun , vol.344 , pp. 400-405
    • Arase, M.1    Waterman, M.R.2    Kawaga, N.3
  • 27
    • 0346662942 scopus 로고    scopus 로고
    • Available online, accessed on 3 July 2012
    • Cytochrome P450 Homepage. Available online: http://drnelson.uthsc.edu/bacterial.P450s.2011.htm (accessed on 3 July 2012).
    • Cytochrome P450 Homepage
  • 28
    • 77951981537 scopus 로고    scopus 로고
    • Chemistry and biology of siderophores
    • Hider, R.C.; Kong, X. Chemistry and biology of siderophores. Nat. Prod. Rep. 2010, 27, 637-657.
    • (2010) Nat. Prod. Rep , vol.27 , pp. 637-657
    • Hider, R.C.1    Kong, X.2
  • 29
    • 0019588236 scopus 로고
    • Pyochelin: Novel structure of an iron-chelating growth promoter for Pseudomonas aeruginosa
    • Cox, C.D.; Rinehart, K.L.; Moore, M.L.; Cook, J.C. Pyochelin: Novel structure of an iron-chelating growth promoter for Pseudomonas aeruginosa. Proc. Natl. Acad. Sci. USA 1981, 78, 4256-4260.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 4256-4260
    • Cox, C.D.1    Rinehart, K.L.2    Moore, M.L.3    Cook, J.C.4
  • 30
    • 0024440645 scopus 로고
    • Thiazostatin A and thiazostatin B, new antioxidants produced by Streptomyces tolurosus
    • Shindo, K.; Takenaka, A.; Noguchi, T.; Hayakawa, Y.; Seto, H. Thiazostatin A and thiazostatin B, new antioxidants produced by Streptomyces tolurosus. J. Antibiot. 1989, 42, 1526-1529.
    • (1989) J. Antibiot , vol.42 , pp. 1526-1529
    • Shindo, K.1    Takenaka, A.2    Noguchi, T.3    Hayakawa, Y.4    Seto, H.5
  • 35
    • 79955574923 scopus 로고    scopus 로고
    • Version 1.2r3pre; Schrödinger LLC: New York, NY, USA
    • The PyMOL Molecular Graphics System, Version 1.2r3pre; Schrödinger LLC: New York, NY, USA.
    • The PyMOL Molecular Graphics System
  • 36
    • 78651165715 scopus 로고
    • The carbon monoxide binding pigment of liver microsomes. I. Evidence for its hemoprotein in nature
    • Omura, T.; Sato, R. The carbon monoxide binding pigment of liver microsomes. I. Evidence for its hemoprotein in nature. J. Biol. Chem. 1964, 239, 2370-2378.
    • (1964) J. Biol. Chem , vol.239 , pp. 2370-2378
    • Omura, T.1    Sato, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.