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Volumn 45, Issue 3, 2006, Pages 755-762

Human cytochrome b5 requires residues E48 and E49 to stimulate the 17,20-lyase activity of cytochrome P450c17

Author keywords

[No Author keywords available]

Indexed keywords

BIOSYNTHESIS; ELECTRON TRANSITIONS; HORMONES; MUTAGENESIS;

EID: 31044440024     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi051623y     Document Type: Article
Times cited : (62)

References (38)
  • 1
    • 0019874673 scopus 로고
    • Microsomal cytochrome P450 from neonatal pig testis: Two enzymatic activities (17α-hydroxylase and C17,20-lyase) associated with one protein
    • Nakajin, S., Shively, J. E., Yuan, P., and Hall, P. F. (1981) Microsomal cytochrome P450 from neonatal pig testis: Two enzymatic activities (17α-hydroxylase and C17,20-lyase) associated with one protein, Biochemistry 20, 4037-4042.
    • (1981) Biochemistry , vol.20 , pp. 4037-4042
    • Nakajin, S.1    Shively, J.E.2    Yuan, P.3    Hall, P.F.4
  • 2
    • 0032488666 scopus 로고    scopus 로고
    • 5 augments the 17,20 lyase activity of human P450c17 without direct electron transfer
    • 5 augments the 17,20 lyase activity of human P450c17 without direct electron transfer, J. Biol. Chem. 273, 3158-3165.
    • (1998) J. Biol. Chem. , vol.273 , pp. 3158-3165
    • Auchus, R.J.1    Lee, T.C.2    Miller, W.L.3
  • 4
    • 0031252385 scopus 로고    scopus 로고
    • The genetic and functional basis of isolated 17,20 lyase deficiency
    • Geller, D. H., Auchus, R. J., Mendonça, B. B., and Miller, W. L. (1997) The genetic and functional basis of isolated 17,20 lyase deficiency, Nat. Genet. 17, 201-205.
    • (1997) Nat. Genet. , vol.17 , pp. 201-205
    • Geller, D.H.1    Auchus, R.J.2    Mendonça, B.B.3    Miller, W.L.4
  • 5
    • 1542782363 scopus 로고    scopus 로고
    • CYP17 mutation E305G causes isolated 17,20-lyase deficiency by selectively altering substrate binding
    • Sherbet, D. P., Tiosano, D., Kwist, K. M., Hochberg, Z., and Auchus, R. J. (2003) CYP17 mutation E305G causes isolated 17,20-lyase deficiency by selectively altering substrate binding, J. Biol. Chem. 278, 48563-48569.
    • (2003) J. Biol. Chem. , vol.278 , pp. 48563-48569
    • Sherbet, D.P.1    Tiosano, D.2    Kwist, K.M.3    Hochberg, Z.4    Auchus, R.J.5
  • 8
    • 0033346398 scopus 로고    scopus 로고
    • Molecular modeling of human P450c17 (17α-hydroxylase/17,20-lyase): Insights into reaction mechanisms and effects of mutations
    • Auchus, R. J., and Miller, W. L. (1999) Molecular modeling of human P450c17 (17α-hydroxylase/17,20-lyase): Insights into reaction mechanisms and effects of mutations, Mol. Endocrinol. 13, 1169-1182.
    • (1999) Mol. Endocrinol. , vol.13 , pp. 1169-1182
    • Auchus, R.J.1    Miller, W.L.2
  • 9
    • 0028786656 scopus 로고
    • Serine phosphorylation of human P450c17 increases 17,20 lyase activity: Implications for adrenarche and for the polycystic ovary syndrome
    • Zhang, L., Rodriguez, H., Ohno, S., and Miller, W. L. (1995) Serine phosphorylation of human P450c17 increases 17,20 lyase activity: Implications for adrenarche and for the polycystic ovary syndrome, Proc. Natl. Acad. Sci. U.S.A. 92, 10619-10623.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 10619-10623
    • Zhang, L.1    Rodriguez, H.2    Ohno, S.3    Miller, W.L.4
  • 10
    • 0037474198 scopus 로고    scopus 로고
    • Protein phosphatase 2A and phosphoprotein SET regulate androgen production by P450c17
    • Pandey, A. V., Mellon, S. H., and Miller, W. L. (2003) Protein phosphatase 2A and phosphoprotein SET regulate androgen production by P450c17, J. Biol. Chem. 278, 2837-2844.
    • (2003) J. Biol. Chem. , vol.278 , pp. 2837-2844
    • Pandey, A.V.1    Mellon, S.H.2    Miller, W.L.3
  • 11
    • 0022997597 scopus 로고
    • Role of electron transport in the regulation of the lyase activity of C-21 side-chain cleavage P450 from porcine adrenal and testicular microsomes
    • Yanagibashi, K., and Hall, P. F. (1986) Role of electron transport in the regulation of the lyase activity of C-21 side-chain cleavage P450 from porcine adrenal and testicular microsomes, J. Biol. Chem. 261, 8429-8433.
    • (1986) J. Biol. Chem. , vol.261 , pp. 8429-8433
    • Yanagibashi, K.1    Hall, P.F.2
  • 18
    • 0034493776 scopus 로고    scopus 로고
    • Developmental changes in steroidogenic enzymes in human postnatal adrenal cortex: Immunohistochemical studies
    • Suzuki, T., Sasano, H., Takeyama, J., Kaneko, C., Freije, W. A., Carr, B. R., and Rainey, W. E. (2000) Developmental changes in steroidogenic enzymes in human postnatal adrenal cortex: Immunohistochemical studies, Clin. Endocrinol. (Oxford) 53, 739-747.
    • (2000) Clin. Endocrinol. (Oxford) , vol.53 , pp. 739-747
    • Suzuki, T.1    Sasano, H.2    Takeyama, J.3    Kaneko, C.4    Freije, W.A.5    Carr, B.R.6    Rainey, W.E.7
  • 19
    • 0021112846 scopus 로고
    • 5 in hepatic microsomal fatty acid chain elongation. Electron input in the first reduction step
    • 5 in hepatic microsomal fatty acid chain elongation. Electron input in the first reduction step, J. Biol. Chem. 258, 14823-14828.
    • (1983) J. Biol. Chem. , vol.258 , pp. 14823-14828
    • Nagi, M.1    Cook, L.2    Prasad, M.R.3    Cinti, D.L.4
  • 20
    • 0027506875 scopus 로고
    • Concise review: Methemoglobinemia
    • Mansouri, A., and Lurie, A. A. (1993) Concise review: Methemoglobinemia, Am. J. Hematol. 42, 7-12.
    • (1993) Am. J. Hematol. , vol.42 , pp. 7-12
    • Mansouri, A.1    Lurie, A.A.2
  • 30
    • 0034840366 scopus 로고    scopus 로고
    • Pitfalls in characterizing P450c17 mutations associated with isolated 17,20-lyase deficiency
    • Gupta, M. K., Geller, D. H., and Auchus, R. J. (2001) Pitfalls in characterizing P450c17 mutations associated with isolated 17,20-lyase deficiency, J. Clin. Endocrinol. Metab. 86, 4416-4423.
    • (2001) J. Clin. Endocrinol. Metab. , vol.86 , pp. 4416-4423
    • Gupta, M.K.1    Geller, D.H.2    Auchus, R.J.3
  • 31
    • 0026062961 scopus 로고
    • The hydrophobic amino-terminal sequence of bovine 17α-hydroxylase is required for the expression of a functional hemoprotein in COS 1 cells
    • Clark, B. J., and Waterman, M. R. (1991) The hydrophobic amino-terminal sequence of bovine 17α-hydroxylase is required for the expression of a functional hemoprotein in COS 1 cells, J. Biol. Chem. 266, 5898-5904.
    • (1991) J. Biol. Chem. , vol.266 , pp. 5898-5904
    • Clark, B.J.1    Waterman, M.R.2
  • 35
    • 0035032081 scopus 로고    scopus 로고
    • The genetics, pathophysiology, and management of human deficiencies of P450c17
    • Auchus, R. J. (2001) The genetics, pathophysiology, and management of human deficiencies of P450c17, Endocrinol Metab. Clin. North Am. 30, 101-119.
    • (2001) Endocrinol Metab. Clin. North Am. , vol.30 , pp. 101-119
    • Auchus, R.J.1
  • 38
    • 17144426051 scopus 로고    scopus 로고
    • 5 and by serine phosphorylation of P450c17
    • 5 and by serine phosphorylation of P450c17, J. Biol. Chem. 280, 13265-13271.
    • (2005) J. Biol. Chem. , vol.280 , pp. 13265-13271
    • Pandey, A.V.1    Miller, W.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.