메뉴 건너뛰기




Volumn 385, Issue 2, 2009, Pages 170-175

Purification, characterization, and directed evolution study of a vitamin D3 hydroxylase from Pseudonocardia autotrophica

Author keywords

1 ,25 Dihydroxyvitamin D3; 25 Hydroxyvitamin D3; Cytochrome P450 monooxygenase; Pseudonocardia autotrophica; Vdh; Vitamin D3 hydroxylase

Indexed keywords

AMINO ACID; BACTERIAL ENZYME; COLECALCIFEROL; COLECALCIFEROL HYDROXYLASE; CYTOCHROME P450; CYTOCHROME P450 107; DNA; MUTANT PROTEIN; UNCLASSIFIED DRUG; VITAMIN D3 HYDROXYLASE K1;

EID: 67349154411     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.05.033     Document Type: Article
Times cited : (62)

References (17)
  • 8
    • 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 ML236B to pravastatin sodium (CS-514), a tissue-selective inhibitor of 3-hydroxy-3-methylglutaryl-coenzyme-A reductase
    • Matsuoka T., Miyakoshi S., Tanzawa K., Nakahara K., Hosobuchi M., and Serizawa N. Purification and characterization of cytochrome P-450sca from Streptomyces carbophilus. ML-236B (compactin) induces a cytochrome P-450sca in Streptomyces carbophilus that hydroxylates ML236B 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
  • 10
    • 0000369624 scopus 로고
    • A method for the determination of the amino acid sequence in peptides
    • Edman P. A method for the determination of the amino acid sequence in peptides. Arch. Biochem. Biophys. 22 (1949) 475-476
    • (1949) Arch. Biochem. Biophys. , vol.22 , pp. 475-476
    • Edman, P.1
  • 11
    • 32044440744 scopus 로고    scopus 로고
    • Biocatalytic conversion of avermectin to 4′′-oxo-avermectin: characterization of biocatalytically active bacterial strains and of cytochrome P450 monooxygenase enzymes and their genes
    • Jungmann V., Molnar I., Hammer P.E., Hill D.S., Zirkle R., Buckel T.G., Buckel D., Ligon J.M., and Pachlatko J.P. Biocatalytic conversion of avermectin to 4′′-oxo-avermectin: characterization of biocatalytically active bacterial strains and of cytochrome P450 monooxygenase enzymes and their genes. Appl. Environ. Microbiol. 71 (2005) 6968-6976
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 6968-6976
    • Jungmann, V.1    Molnar, I.2    Hammer, P.E.3    Hill, D.S.4    Zirkle, R.5    Buckel, T.G.6    Buckel, D.7    Ligon, J.M.8    Pachlatko, J.P.9
  • 12
    • 4544258603 scopus 로고    scopus 로고
    • Purification and characterization of mouse CYP27B1 overproduced by an Escherichia coli system coexpressing molecular chaperonins GroEL/ES
    • Uchida E., Kagawa N., Sakaki T., Urushino N., Sawada N., Kamakura M., Ohta M., Kato S., and Inouye K. Purification and characterization of mouse CYP27B1 overproduced by an Escherichia coli system coexpressing molecular chaperonins GroEL/ES. Biochem. Biophys. Res. Commun. 323 (2004) 505-511
    • (2004) Biochem. Biophys. Res. Commun. , vol.323 , pp. 505-511
    • Uchida, E.1    Kagawa, N.2    Sakaki, T.3    Urushino, N.4    Sawada, N.5    Kamakura, M.6    Ohta, M.7    Kato, S.8    Inouye, K.9
  • 13
    • 0034042416 scopus 로고    scopus 로고
    • Cyclodextrins to increase the utility of enzymes in organic synthesis
    • Harper J.B., Easton C.J., and Lincoln S.F. Cyclodextrins to increase the utility of enzymes in organic synthesis. Curr. Org. Chem. 4 (2000) 429-454
    • (2000) Curr. Org. Chem. , vol.4 , pp. 429-454
    • Harper, J.B.1    Easton, C.J.2    Lincoln, S.F.3
  • 14
    • 0029763188 scopus 로고    scopus 로고
    • Transcriptional regulation of the Rhodococcus rhodochrous J1 nitA gene encoding a nitrilase
    • Komeda H., Hori Y., Kobayashi M., and Shimizu S. Transcriptional regulation of the Rhodococcus rhodochrous J1 nitA gene encoding a nitrilase. Proc. Natl. Acad. Sci. USA 93 (1996) 10572-10577
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 10572-10577
    • Komeda, H.1    Hori, Y.2    Kobayashi, M.3    Shimizu, S.4
  • 15
    • 33748750539 scopus 로고    scopus 로고
    • The structural basis for substrate anchoring, active site selectivity, and product formation by P450 PikC from Streptomyces venezuelae
    • Sherman D.H., Li S., Yermalitskaya L.V., Kim Y., Smith J.A., Waterman M.R., and Podust L.M. The structural basis for substrate anchoring, active site selectivity, and product formation by P450 PikC from Streptomyces venezuelae. J. Biol. Chem. 281 (2006) 26289-26297
    • (2006) J. Biol. Chem. , vol.281 , pp. 26289-26297
    • Sherman, D.H.1    Li, S.2    Yermalitskaya, L.V.3    Kim, Y.4    Smith, J.A.5    Waterman, M.R.6    Podust, L.M.7
  • 16
    • 0034724310 scopus 로고    scopus 로고
    • Crystal structures of ligand complexes of P450eryF exhibiting homotropic cooperativity
    • Cupp-Vickery J., Anderson R., and Hatziris Z. Crystal structures of ligand complexes of P450eryF exhibiting homotropic cooperativity. Proc. Natl. Acad. Sci. USA 97 (2000) 3050-3055
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 3050-3055
    • Cupp-Vickery, J.1    Anderson, R.2    Hatziris, Z.3
  • 17
    • 0029586252 scopus 로고
    • Structure of cytochrome P450eryF involved in erythromycin biosynthesis
    • Cupp-Vickery J.R., and Poulos T.L. Structure of cytochrome P450eryF involved in erythromycin biosynthesis. Nat. Struct. Biol. 2 (1995) 144-153
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 144-153
    • Cupp-Vickery, J.R.1    Poulos, T.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.