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Volumn 1814, Issue 1, 2011, Pages 249-256

Bioconversion of vitamin D to its active form by bacterial or mammalian cytochrome P450

Author keywords

Bioconversion; Cytochrome P450; Practical application; Vitamin D hydroxylase

Indexed keywords

CALCITRIOL; COLECALCIFEROL; CYTOCHROME P450; CYTOCHROME P450 105A1; CYTOCHROME P450 107; CYTOCHROME P450 27B1; UNCLASSIFIED DRUG; VITAMIN D;

EID: 78649448443     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2010.07.014     Document Type: Review
Times cited : (38)

References (53)
  • 1
    • 0030896478 scopus 로고    scopus 로고
    • Advances in microbial steroid biotransformation
    • S.B. Mahato, and S. Garai Advances in microbial steroid biotransformation Steroids 62 1997 332 345
    • (1997) Steroids , vol.62 , pp. 332-345
    • Mahato, S.B.1    Garai, S.2
  • 2
    • 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-methylglutaryl-coenzyme-A reductase
    • T. Matsuoka, S. Miyakoshi, K. Tanzawa, K. Nakahara, M. Hosobuchi, and N. Serizawa 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-methylglutaryl-coenzyme-A reductase Eur. J. Biochem. 184 1989 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
  • 3
    • 0025767694 scopus 로고
    • A two component-type cytochrome P-450 monooxygenase system in a prokaryote that catalyzes hydroxylation of ML-236B to pravastatin, a tissue-selective inhibitor of 3-hydroxy-3-methylglutaryl coenzyme A reductase
    • N. Serizawa, and T. Matsuoka A two component-type cytochrome P-450 monooxygenase system in a prokaryote that catalyzes hydroxylation of ML-236B to pravastatin, a tissue-selective inhibitor of 3-hydroxy-3-methylglutaryl coenzyme A reductase Biochim. Biophys. Acta 1084 1991 35 40
    • (1991) Biochim. Biophys. Acta , vol.1084 , pp. 35-40
    • Serizawa, N.1    Matsuoka, T.2
  • 4
    • 0029133802 scopus 로고
    • Cloning, characterization and expression of the gene encoding cytochrome P-450sca-2 from Streptomyces carbophilus involved in production of pravastatin, a specific HMG-CoA reductase inhibitor
    • I. Watanabe, F. Nara, and N. Serizawa Cloning, characterization and expression of the gene encoding cytochrome P-450sca-2 from Streptomyces carbophilus involved in production of pravastatin, a specific HMG-CoA reductase inhibitor Gene 163 1995 81 85
    • (1995) Gene , vol.163 , pp. 81-85
    • Watanabe, I.1    Nara, F.2    Serizawa, N.3
  • 5
    • 0026018240 scopus 로고
    • Transformation of 25- and 1 alpha-hydroxyvitamin D3 to 1 alpha, 25-dihydroxyvitamin D3 by using Streptomyces sp. strains
    • J. Sasaki, A. Mikami, K. Mizoue, and S. Omura Transformation of 25- and 1 alpha-hydroxyvitamin D3 to 1 alpha, 25-dihydroxyvitamin D3 by using Streptomyces sp. strains Appl. Environ. Microbiol. 57 1991 2841 2846
    • (1991) Appl. Environ. Microbiol. , vol.57 , pp. 2841-2846
    • Sasaki, J.1    Mikami, A.2    Mizoue, K.3    Omura, S.4
  • 6
    • 0026614795 scopus 로고
    • Transformation of vitamin D3 to 1 alpha,25-dihydroxyvitamin D3 via 25-hydroxyvitamin D3 using Amycolata sp. strains
    • J. Sasaki, A. Miyazaki, M. Saito, T. Adachi, K. Mizoue, K. Hanada, and S. Omura Transformation of vitamin D3 to 1 alpha,25-dihydroxyvitamin D3 via 25-hydroxyvitamin D3 using Amycolata sp. strains Appl. Microbiol. Biotechnol. 38 1992 152 157
    • (1992) Appl. Microbiol. Biotechnol. , vol.38 , pp. 152-157
    • Sasaki, J.1    Miyazaki, A.2    Saito, M.3    Adachi, T.4    Mizoue, K.5    Hanada, K.6    Omura, S.7
  • 7
    • 0028142621 scopus 로고
    • Cloning and nucleotide sequence of a bacterial cytochrome P-450VD25 gene encoding vitamin D-3 25-hydroxylase
    • H. Kawauchi, J. Sasaki, T. Adachi, K. Hanada, T. Beppu, and S. Horinouchi Cloning and nucleotide sequence of a bacterial cytochrome P-450VD25 gene encoding vitamin D-3 25-hydroxylase Biochim. Biophys. Acta 1219 1994 179 183
    • (1994) Biochim. Biophys. Acta , vol.1219 , pp. 179-183
    • Kawauchi, H.1    Sasaki, J.2    Adachi, T.3    Hanada, K.4    Beppu, T.5    Horinouchi, S.6
  • 11
    • 0141732321 scopus 로고    scopus 로고
    • De-orphanization of cytochrome P450 2R1: A microsomal vitamin D 25-hydroxilase
    • J.B. Cheng, D.L. Motola, D.J. Mangelsdorf, and D.W. Russell De-orphanization of cytochrome P450 2R1: a microsomal vitamin D 25-hydroxilase J. Biol. Chem. 278 2003 38084 38093
    • (2003) J. Biol. Chem. , vol.278 , pp. 38084-38093
    • Cheng, J.B.1    Motola, D.L.2    Mangelsdorf, D.J.3    Russell, D.W.4
  • 15
    • 0030782757 scopus 로고    scopus 로고
    • Cloning of human 25-hydroxyvitamin D-1 alpha-hydroxylase and mutations causing vitamin D-dependent rickets type 1
    • G.K. Fu, D. Lin, M.Y. Zhang, D.D. Bikle, C.H. Shackleton, W.L. Miller, and A.A. Portale Cloning of human 25-hydroxyvitamin D-1 alpha-hydroxylase and mutations causing vitamin D-dependent rickets type 1 Mol. Endocrinol. 11 1997 1961 1970
    • (1997) Mol. Endocrinol. , vol.11 , pp. 1961-1970
    • Fu, G.K.1    Lin, D.2    Zhang, M.Y.3    Bikle, D.D.4    Shackleton, C.H.5    Miller, W.L.6    Portale, A.A.7
  • 16
    • 0028093170 scopus 로고
    • Further oxidation of hydroxycalcidiol by calcidiol 24-hydroxylase. A study with the mature enzyme expressed in Escherichia coli
    • M. Akiyoshi-Shibata, T. Sakaki, Y. Ohyama, M. Noshiro, K. Okuda, and Y. Yabusaki Further oxidation of hydroxycalcidiol by calcidiol 24-hydroxylase. A study with the mature enzyme expressed in Escherichia coli Eur. J. Biochem. 224 1994 335 343
    • (1994) Eur. J. Biochem. , vol.224 , pp. 335-343
    • Akiyoshi-Shibata, M.1    Sakaki, T.2    Ohyama, Y.3    Noshiro, M.4    Okuda, K.5    Yabusaki, Y.6
  • 17
    • 0021880264 scopus 로고
    • Expression of rat liver cytochrome P-450MC cDNA in Saccharomyces cerevisiae
    • K. Oeda, T. Sakaki, and H. Ohkawa Expression of rat liver cytochrome P-450MC cDNA in Saccharomyces cerevisiae DNA 4 1985 203 210 (Pubitemid 15027392)
    • (1985) DNA , vol.4 , Issue.3 , pp. 203-210
    • Oeda, K.1    Sakaki, T.2    Ohkawa, H.3
  • 18
    • 0026254583 scopus 로고
    • Progesterone metabolism in recombinant yeast simultaneously expressing bovine cytochromes P450c17 (CYP17A1) and P450c21 (CYP21B1) and yeast NADPH-P450 oxidoreductase
    • T. Sakaki, M. Akiyoshi-Shibata, Y. Yabusaki, K. Manabe, H. Murakami, and H. Ohkawa Progesterone metabolism in recombinant yeast simultaneously expressing bovine cytochromes P450c17 (CYP17A1) and P450c21 (CYP21B1) and yeast NADPH-P450 oxidoreductase Pharmacogenetics 1 1991 86 93
    • (1991) Pharmacogenetics , vol.1 , pp. 86-93
    • Sakaki, T.1    Akiyoshi-Shibata, M.2    Yabusaki, Y.3    Manabe, K.4    Murakami, H.5    Ohkawa, H.6
  • 19
    • 0037133263 scopus 로고    scopus 로고
    • Functional expression of human mitochondrial CYP11B2 in fission yeast and identification of a new internal electron transfer protein, etp1
    • M. Bureik, B. Schiffler, Y. Hiraoka, F. Vogel, and R. Bernhardt Functional expression of human mitochondrial CYP11B2 in fission yeast and identification of a new internal electron transfer protein, etp1 Biochemistry 41 2002 2311 2321
    • (2002) Biochemistry , vol.41 , pp. 2311-2321
    • Bureik, M.1    Schiffler, B.2    Hiraoka, Y.3    Vogel, F.4    Bernhardt, R.5
  • 21
    • 37349007629 scopus 로고    scopus 로고
    • Coexpression of redox partners increases the hydrocortisone (cortisol) production efficiency in CYP11B1 expressing fission yeast Schizosaccharomyces pombe
    • T. Hakki, S. Zearo, C.A. Dragan, M. Bureik, and R. Bernhardt Coexpression of redox partners increases the hydrocortisone (cortisol) production efficiency in CYP11B1 expressing fission yeast Schizosaccharomyces pombe J. Biotechnol. 133 2008 351 359
    • (2008) J. Biotechnol. , vol.133 , pp. 351-359
    • Hakki, T.1    Zearo, S.2    Dragan, C.A.3    Bureik, M.4    Bernhardt, R.5
  • 22
    • 0026672248 scopus 로고
    • Organella-targeted expression of rat liver cytochrome P450c27 in yeast. Genetically engineered alteration of mitochondrial P450 into a microsomal form creates a novel functional electron transport chain
    • T. Sakaki, M. Akiyoshi-Shibata, Y. Yabusaki, and H. Ohkawa Organella-targeted expression of rat liver cytochrome P450c27 in yeast. Genetically engineered alteration of mitochondrial P450 into a microsomal form creates a novel functional electron transport chain J. Biol. Chem. 267 1992 16497 16502
    • (1992) J. Biol. Chem. , vol.267 , pp. 16497-16502
    • Sakaki, T.1    Akiyoshi-Shibata, M.2    Yabusaki, Y.3    Ohkawa, H.4
  • 23
    • 0002819595 scopus 로고    scopus 로고
    • Enzymatic properties of mouse 25-hydroxyvitamin D3 1 alpha-hydroxylase expressed in Escherichia coli
    • T. Sakaki, N. Sawada, K. Takeyama, S. Kato, and K. Inouye Enzymatic properties of mouse 25-hydroxyvitamin D3 1 alpha-hydroxylase expressed in Escherichia coli Eur. J. Biochem. 259 1999 731 738
    • (1999) Eur. J. Biochem. , vol.259 , pp. 731-738
    • Sakaki, T.1    Sawada, N.2    Takeyama, K.3    Kato, S.4    Inouye, K.5
  • 24
    • 1942447828 scopus 로고    scopus 로고
    • Enzymatic properties of human 25-hydroxyvitamin D3 1alpha-hydroxylase coexpression with adrenodoxin and NADPH-adrenodoxin reductase in Escherichia coli
    • N. Sawada, T. Sakaki, S. Kitanaka, K. Takeyama, S. Kato, and K. Inouye Enzymatic properties of human 25-hydroxyvitamin D3 1alpha-hydroxylase coexpression with adrenodoxin and NADPH-adrenodoxin reductase in Escherichia coli Eur. J. Biochem. 265 1999 950 956
    • (1999) Eur. J. Biochem. , vol.265 , pp. 950-956
    • Sawada, N.1    Sakaki, T.2    Kitanaka, S.3    Takeyama, K.4    Kato, S.5    Inouye, K.6
  • 26
  • 28
    • 0035834602 scopus 로고    scopus 로고
    • The importance of residues in substrate recognition site 3 for the catalytic function of CYP2D25 (vitamin D 25-hydroxylase)
    • F. Hosseinpour, M. Hidestrand, M. Ingelman-Sundberg, and K. Wikvall The importance of residues in substrate recognition site 3 for the catalytic function of CYP2D25 (vitamin D 25-hydroxylase) Biochem. Biophys. Res. Commun. 288 2001 1059 1063
    • (2001) Biochem. Biophys. Res. Commun. , vol.288 , pp. 1059-1063
    • Hosseinpour, F.1    Hidestrand, M.2    Ingelman-Sundberg, M.3    Wikvall, K.4
  • 29
    • 0038694560 scopus 로고    scopus 로고
    • Metabolism of 25-hydroxyvitamin D3 by microsomal and mitochondrial vitamin D3 25-hydroxylases (CYP2D25 and CYP27A1): A novel reaction by CYP27A1
    • Z. Araya, F. Hosseinpour, K. Bodin, and K. Wikvall Metabolism of 25-hydroxyvitamin D3 by microsomal and mitochondrial vitamin D3 25-hydroxylases (CYP2D25 and CYP27A1): a novel reaction by CYP27A1 Biochim. Biophys. Acta 1632 2003 40 47
    • (2003) Biochim. Biophys. Acta , vol.1632 , pp. 40-47
    • Araya, Z.1    Hosseinpour, F.2    Bodin, K.3    Wikvall, K.4
  • 31
    • 2542433007 scopus 로고    scopus 로고
    • Identification of a novel rat microsomal vitamin D3 25-hydroxylase
    • T. Yamasaki, S. Izumi, H. Ide, and Y. Ohyama Identification of a novel rat microsomal vitamin D3 25-hydroxylase J. Biol. Chem. 279 2004 22848 22856
    • (2004) J. Biol. Chem. , vol.279 , pp. 22848-22856
    • Yamasaki, T.1    Izumi, S.2    Ide, H.3    Ohyama, Y.4
  • 32
    • 0035663972 scopus 로고    scopus 로고
    • Structure-function analysis of CYP27B1 and CYP27A1. Studies on mutants from patients with vitamin D-dependent rickets type i (VDDR-I) and cerebrotendinous xanthomatosis (CTX)
    • N. Sawada, T. Sakaki, S. Kitanaka, S. Kato, and K. Inouye Structure-function analysis of CYP27B1 and CYP27A1. Studies on mutants from patients with vitamin D-dependent rickets type I (VDDR-I) and cerebrotendinous xanthomatosis (CTX) Eur. J. Biochem. 268 2001 6607 6615
    • (2001) Eur. J. Biochem. , vol.268 , pp. 6607-6615
    • Sawada, N.1    Sakaki, T.2    Kitanaka, S.3    Kato, S.4    Inouye, K.5
  • 34
    • 0027729037 scopus 로고
    • Efficiency and substrate specificity of Streptomyces griseolus cytochromes P-450SUI and P-450SU2 mono-oxygenase reactions
    • D.P. O'Keefe, S.M. Lau, and P.A. Harder Efficiency and substrate specificity of Streptomyces griseolus cytochromes P-450SUI and P-450SU2 mono-oxygenase reactions Biochem. Soc. Trans. 21 1993 1073 1077
    • (1993) Biochem. Soc. Trans. , vol.21 , pp. 1073-1077
    • O'Keefe, D.P.1    Lau, S.M.2    Harder, P.A.3
  • 38
    • 0031013972 scopus 로고    scopus 로고
    • The structure of the cytochrome p450BM-3 haem domain complexed with the fatty acid substrate, palmitoleic acid
    • H. Li, and T.L. Poulos The structure of the cytochrome p450BM-3 haem domain complexed with the fatty acid substrate, palmitoleic acid Nat. Struct. Biol. 4 1997 140 146
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 140-146
    • Li, H.1    Poulos, T.L.2
  • 39
    • 0037646516 scopus 로고    scopus 로고
    • Substrate recognition and molecular mechanism of fatty acid hydroxylation by cytochrome P450 from Bacillus subtilis. Crystallographic, spectroscopic, and mutational studies
    • D.S. Lee, A. Yamada, H. Sugimoto, I. Matsunaga, H. Ogura, K. Ichihara, S. Adachi, S.Y. Park, and Y. Shiro Substrate recognition and molecular mechanism of fatty acid hydroxylation by cytochrome P450 from Bacillus subtilis. Crystallographic, spectroscopic, and mutational studies J. Biol. Chem. 278 2003 9761 9767
    • (2003) J. Biol. Chem. , vol.278 , pp. 9761-9767
    • Lee, D.S.1    Yamada, A.2    Sugimoto, H.3    Matsunaga, I.4    Ogura, H.5    Ichihara, K.6    Adachi, S.7    Park, S.Y.8    Shiro, Y.9
  • 40
    • 77449094112 scopus 로고    scopus 로고
    • Crystal structure of CYP24A1, a mitochondrial cytochrome P450 involved in vitamin D metabolism
    • A.J. Annalora, D.B. Goodin, W.X. Hong, Q. Zhang, E.F. Johnson, and C.D. Stout Crystal structure of CYP24A1, a mitochondrial cytochrome P450 involved in vitamin D metabolism J. Mol. Biol. 396 2010 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
  • 42
    • 4644301430 scopus 로고    scopus 로고
    • The structure of human microsomal cytochrome P450 3A4 determined by X-ray crystallography to 2.05-A resolution
    • J.K. Yano, M.R. Wester, G.A. Schoch, K.J. Griffin, C.D. Stout, and E.F. Johnson The structure of human microsomal cytochrome P450 3A4 determined by X-ray crystallography to 2.05-A resolution J. Biol. Chem. 279 2004 38091 38094
    • (2004) J. Biol. Chem. , vol.279 , pp. 38091-38094
    • Yano, J.K.1    Wester, M.R.2    Schoch, G.A.3    Griffin, K.J.4    Stout, C.D.5    Johnson, E.F.6
  • 45
    • 64149098795 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray diffraction studies of vitamin D3 hydroxylase, a novel cytochrome P450 isolated from Pseudonocardia autotrophica
    • Y. Yasutake, Y. Fujii, W.K. Cheon, A. Arisawa, and T. Tamura Crystallization and preliminary X-ray diffraction studies of vitamin D3 hydroxylase, a novel cytochrome P450 isolated from Pseudonocardia autotrophica Acta Crystallogr. F Struct. Biol. Cryst. Commun. 65 2009 372 375
    • (2009) Acta Crystallogr. F Struct. Biol. Cryst. Commun. , vol.65 , pp. 372-375
    • Yasutake, Y.1    Fujii, Y.2    Cheon, W.K.3    Arisawa, A.4    Tamura, T.5
  • 46
    • 0028003885 scopus 로고
    • Liver mitochondrial cytochrome P450 CYP27 and recombinant-expressed human CYP27 catalyze 1 alpha-hydroxylation of 25-hydroxyvitamin D3
    • E. Axen, H. Postlind, H. Sjoberg, and K. Wikvall Liver mitochondrial cytochrome P450 CYP27 and recombinant-expressed human CYP27 catalyze 1 alpha-hydroxylation of 25-hydroxyvitamin D3 Proc. Natl Acad. Sci. USA 91 1994 10014 10018
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 10014-10018
    • Axen, E.1    Postlind, H.2    Sjoberg, H.3    Wikvall, K.4
  • 47
    • 24044511803 scopus 로고    scopus 로고
    • Identification of the amino acid residue of CYP27B1 responsible for binding of 25-hydroxyvitamin D3 whose mutation causes vitamin D-dependent rickets type 1
    • K. Yamamoto, E. Uchida, N. Urushino, T. Sakaki, N. Kagawa, N. Sawada, M. Kamakura, S. Kato, K. Inouye, and S. Yamada Identification of the amino acid residue of CYP27B1 responsible for binding of 25-hydroxyvitamin D3 whose mutation causes vitamin D-dependent rickets type 1 J. Biol. Chem. 280 2005 30511 30516
    • (2005) J. Biol. Chem. , vol.280 , pp. 30511-30516
    • Yamamoto, K.1    Uchida, E.2    Urushino, N.3    Sakaki, T.4    Kagawa, N.5    Sawada, N.6    Kamakura, M.7    Kato, S.8    Inouye, K.9    Yamada, S.10
  • 48
    • 67149096046 scopus 로고    scopus 로고
    • Efficient biotransformations using Escherichia coli with tolC acrAB mutations expressing cytochrome P450 genes
    • T. Fujii, Y. Fujii, K. Machida, A. Ochiai, and M. Ito Efficient biotransformations using Escherichia coli with tolC acrAB mutations expressing cytochrome P450 genes Biosci. Biotechnol. Biochem. 73 2009 805 810
    • (2009) Biosci. Biotechnol. Biochem. , vol.73 , pp. 805-810
    • Fujii, T.1    Fujii, Y.2    MacHida, K.3    Ochiai, A.4    Ito, M.5
  • 49
    • 0023184975 scopus 로고
    • A genetically engineered P450 monooxygenase: Construction of the functional fused enzyme between rat cytochrome P450c and NADPH-cytochrome P450 reductase
    • H. Murakami, Y. Yabusaki, T. Sakaki, M. Shibata, and H. Ohkawa A genetically engineered P450 monooxygenase: construction of the functional fused enzyme between rat cytochrome P450c and NADPH-cytochrome P450 reductase DNA 6 1987 189 197
    • (1987) DNA , vol.6 , pp. 189-197
    • Murakami, H.1    Yabusaki, Y.2    Sakaki, T.3    Shibata, M.4    Ohkawa, H.5
  • 50
    • 0029859961 scopus 로고    scopus 로고
    • Molecular engineering study on electron transfer from NADPH-P450 reductase to rat mitochondrial P450c27 in yeast microsomes
    • T. Sakaki, S. Kominami, K. Hayashi, M. Akiyoshi-Shibata, and Y. Yabusaki Molecular engineering study on electron transfer from NADPH-P450 reductase to rat mitochondrial P450c27 in yeast microsomes J. Biol. Chem. 271 1996 26209 26213
    • (1996) J. Biol. Chem. , vol.271 , pp. 26209-26213
    • Sakaki, T.1    Kominami, S.2    Hayashi, K.3    Akiyoshi-Shibata, M.4    Yabusaki, Y.5
  • 51
    • 0035951779 scopus 로고    scopus 로고
    • Adrenodoxin reductase-adrenodoxin complex structure suggests electron transfer path in steroid biosynthesis
    • J.J. Muller, A. Lapko, G. Bourenkov, K. Ruckpaul, and U. Heinemann Adrenodoxin reductase-adrenodoxin complex structure suggests electron transfer path in steroid biosynthesis J. Biol. Chem. 276 2001 2786 2789
    • (2001) J. Biol. Chem. , vol.276 , pp. 2786-2789
    • Muller, J.J.1    Lapko, A.2    Bourenkov, G.3    Ruckpaul, K.4    Heinemann, U.5


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