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Volumn 1771, Issue 9, 2007, Pages 1254-1261

Distinct metabolic handling of 3β-hydroxy-17a-oxa-D-homo-5α-androstan-17-one by the filamentous fungus Aspergillus tamarii KITA: Evidence in support of steroid/hydroxylase binding hypothesis

Author keywords

Aspergillus tamarii; Binding orientation; Enzymatic dehydration; Hydroxylation; Microbiological transformation; Steroid hydroxylase; Steroidal lactone

Indexed keywords

3BETA HYDROXY 17A OXA DEXTRO 5ALPHA ANDROSTAN 17 ONE; ANDROSTANE DERIVATIVE; LACTONE DERIVATIVE; STEROID MONOOXYGENASE; TESTOLACTONE; UNCLASSIFIED DRUG;

EID: 34548647595     PISSN: 13881981     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbalip.2007.07.001     Document Type: Article
Times cited : (22)

References (24)
  • 2
    • 0011801051 scopus 로고
    • Pathway of progesterone oxidation by Cladosporium resinae
    • Fonken G.S., Murray H.C., and Reineke L.M. Pathway of progesterone oxidation by Cladosporium resinae. J. Am. Chem. Soc. 82 (1960) 5507-5508
    • (1960) J. Am. Chem. Soc. , vol.82 , pp. 5507-5508
    • Fonken, G.S.1    Murray, H.C.2    Reineke, L.M.3
  • 4
    • 0347362546 scopus 로고    scopus 로고
    • Flexibility of the endogenous progesterone lactonisation pathway in Aspergillus tamarii KITA: transformation of a series of cortical steroid analogues
    • Hunter A.C., and Carragher N.E. Flexibility of the endogenous progesterone lactonisation pathway in Aspergillus tamarii KITA: transformation of a series of cortical steroid analogues. J. Steroid Biochem. Mol. Biol. 87 (2003) 301-308
    • (2003) J. Steroid Biochem. Mol. Biol. , vol.87 , pp. 301-308
    • Hunter, A.C.1    Carragher, N.E.2
  • 5
    • 33646157481 scopus 로고    scopus 로고
    • Ring-B functionalized androst-4-en-3-ones and ring-C substituted pregn-4-en-3-ones undergo differential transformation in Aspergillus tamarii KITA: Ring-A transformation with all C-6 substituted steroids and ring-D transformation with C-11 substituents
    • Hunter A.C., Elsom J., Ross L., and Barrett R. Ring-B functionalized androst-4-en-3-ones and ring-C substituted pregn-4-en-3-ones undergo differential transformation in Aspergillus tamarii KITA: Ring-A transformation with all C-6 substituted steroids and ring-D transformation with C-11 substituents. Biochim. Biophys. Acta 1761 (2006) 360-366
    • (2006) Biochim. Biophys. Acta , vol.1761 , pp. 360-366
    • Hunter, A.C.1    Elsom, J.2    Ross, L.3    Barrett, R.4
  • 6
    • 0014086343 scopus 로고
    • Microbiological transformation of a series of androgens with Aspergillus tamarii
    • Brannon D.R., Parrish F.W., Wiley B.J., and Long L. Microbiological transformation of a series of androgens with Aspergillus tamarii. J. Org. Chem. 32 (1967) 1521-1527
    • (1967) J. Org. Chem. , vol.32 , pp. 1521-1527
    • Brannon, D.R.1    Parrish, F.W.2    Wiley, B.J.3    Long, L.4
  • 7
    • 19444382188 scopus 로고    scopus 로고
    • Fate of novel Quasi reverse steroidal substrates by Aspergillus tamarii KITA: Bypass of lactonisation and an exclusive role for the minor hydroxylation pathway
    • Hunter A.C., Kennedy S., Clabby S.-J., and Elsom J. Fate of novel Quasi reverse steroidal substrates by Aspergillus tamarii KITA: Bypass of lactonisation and an exclusive role for the minor hydroxylation pathway. Biochim. Biophys. Acta 1734 (2005) 190-197
    • (2005) Biochim. Biophys. Acta , vol.1734 , pp. 190-197
    • Hunter, A.C.1    Kennedy, S.2    Clabby, S.-J.3    Elsom, J.4
  • 8
    • 0015536381 scopus 로고
    • The microbiological hydroxylation of steroids and related compounds
    • Jones E.R.H. The microbiological hydroxylation of steroids and related compounds. Pure Appl. Chem. 33 (1973) 39-52
    • (1973) Pure Appl. Chem. , vol.33 , pp. 39-52
    • Jones, E.R.H.1
  • 9
    • 37049138213 scopus 로고
    • Microbiological hydroxylation of 17-norkauran-16-one and ent-17-norkauran-16-one with the fungus Rhizopus nigricans
    • McCrindle R., Turnbull J.K., and Anderson A.B. Microbiological hydroxylation of 17-norkauran-16-one and ent-17-norkauran-16-one with the fungus Rhizopus nigricans. J. Chem. Soc., Perkin Trans. 1. 13 (1975) 1202-1208
    • (1975) J. Chem. Soc., Perkin Trans. , vol.1 13 , pp. 1202-1208
    • McCrindle, R.1    Turnbull, J.K.2    Anderson, A.B.3
  • 10
    • 0020263883 scopus 로고
    • The mechanism of microbiological hydroxylation of steroids
    • Holland H.L. The mechanism of microbiological hydroxylation of steroids. Chem. Soc. Rev 11 (1982) 371-395
    • (1982) Chem. Soc. Rev , vol.11 , pp. 371-395
    • Holland, H.L.1
  • 11
    • 0032414210 scopus 로고    scopus 로고
    • The hydroxylation of steroidal ring D lactones by Cephalosporium aphidicola
    • Hanson J.R., and Hunter A.C. The hydroxylation of steroidal ring D lactones by Cephalosporium aphidicola. Phytochemistry 49 (1998) 2349-2353
    • (1998) Phytochemistry , vol.49 , pp. 2349-2353
    • Hanson, J.R.1    Hunter, A.C.2
  • 12
    • 84986738357 scopus 로고
    • 13C NMR spectra of steroids-A survey and commentary
    • 13C NMR spectra of steroids-A survey and commentary. Org. Magn. Reson. 9 (1977) 439-463
    • (1977) Org. Magn. Reson. , vol.9 , pp. 439-463
    • Blunt, J.W.1    Stothers, J.B.2
  • 15
    • 17744371628 scopus 로고    scopus 로고
    • Filamentous fungi: potentially useful catalysts for the biohydroxylations of non-activated carbon centres
    • Lehman L.R., and Stewart J.D. Filamentous fungi: potentially useful catalysts for the biohydroxylations of non-activated carbon centres. Curr. Org. Chem. 5 (2001) 439-470
    • (2001) Curr. Org. Chem. , vol.5 , pp. 439-470
    • Lehman, L.R.1    Stewart, J.D.2
  • 16
    • 25144473534 scopus 로고    scopus 로고
    • Two states and two more in the mechanisms of hydroxylation and epoxidation by cytochrome P450
    • Hirao H., Kumar D., Thiel W., and Shaik S. Two states and two more in the mechanisms of hydroxylation and epoxidation by cytochrome P450. J. Am. Chem. Soc. 127 (2005) 13007-13018
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 13007-13018
    • Hirao, H.1    Kumar, D.2    Thiel, W.3    Shaik, S.4
  • 17
    • 33847057353 scopus 로고    scopus 로고
    • Metabolism of 4-hydroxyandrostenedione and 4-hydroxytestosterone: mass spectrometric identification of urinary metabolites
    • Kohler M., Parr M.K., Opfermann G., Thevis M., Schlörer N., Marner F.-J., and Schänzer W. Metabolism of 4-hydroxyandrostenedione and 4-hydroxytestosterone: mass spectrometric identification of urinary metabolites. Steroids 72 (2007) 278-286
    • (2007) Steroids , vol.72 , pp. 278-286
    • Kohler, M.1    Parr, M.K.2    Opfermann, G.3    Thevis, M.4    Schlörer, N.5    Marner, F.-J.6    Schänzer, W.7
  • 18
    • 0036772150 scopus 로고    scopus 로고
    • Molecular and functional characterization of the kst D2 gene of Rhodococcus erythropolis SQ1 encoding a second 3-ketosteroid delta(1)-dehydrogenase isoenzyme
    • van der Geize R., Hessels G.I., and Dijkhuizen L. Molecular and functional characterization of the kst D2 gene of Rhodococcus erythropolis SQ1 encoding a second 3-ketosteroid delta(1)-dehydrogenase isoenzyme. Microbiology-SGM 148 (2002) 3285-3292
    • (2002) Microbiology-SGM , vol.148 , pp. 3285-3292
    • van der Geize, R.1    Hessels, G.I.2    Dijkhuizen, L.3
  • 20
    • 0029741876 scopus 로고    scopus 로고
    • Microbial transformation of steroids-X. Cytochromes P-450 11α-hydroxylase and C17-C20 lyase and a 1-ene dehydrogenase transform steroids in Nectria haematococca
    • Ahmed F., Williams R.A.D., and Smith K.E. Microbial transformation of steroids-X. Cytochromes P-450 11α-hydroxylase and C17-C20 lyase and a 1-ene dehydrogenase transform steroids in Nectria haematococca. J. Steroid Biochem. Mol. Biol. 58 (1996) 337-349
    • (1996) J. Steroid Biochem. Mol. Biol. , vol.58 , pp. 337-349
    • Ahmed, F.1    Williams, R.A.D.2    Smith, K.E.3
  • 21
    • 0025753954 scopus 로고
    • 4-dehydrogenase from Nocardia coralline: purification and characterization
    • 4-dehydrogenase from Nocardia coralline: purification and characterization. J. Biochem. 109 (1991) 581-586
    • (1991) J. Biochem. , vol.109 , pp. 581-586
    • Hatta, T.1    Wakabayashi, T.2    Itagaki, E.3
  • 22
    • 33846380189 scopus 로고    scopus 로고
    • What common structural features and variations of mammalian P450s are known to date?
    • Otyepka M., Skopalik J., Anzenbacheroá E., and Anzenbacher P. What common structural features and variations of mammalian P450s are known to date?. Biochim. Biophys. Acta 1770 (2007) 376-389
    • (2007) Biochim. Biophys. Acta , vol.1770 , pp. 376-389
    • Otyepka, M.1    Skopalik, J.2    Anzenbacheroá, E.3    Anzenbacher, P.4
  • 23
    • 22344439844 scopus 로고    scopus 로고
    • Possible pathway(s) of testosterone egress from the active site of cytochrome P450 2B1: a steered molecular dynamics simulation
    • Li W., Liu H., Scott E.E., Gräter F., Halpert J.R., Luo X., Shen J., and Jiang H. Possible pathway(s) of testosterone egress from the active site of cytochrome P450 2B1: a steered molecular dynamics simulation. Drug Metab. Dispos. 33 (2005) 910-919
    • (2005) Drug Metab. Dispos. , vol.33 , pp. 910-919
    • Li, W.1    Liu, H.2    Scott, E.E.3    Gräter, F.4    Halpert, J.R.5    Luo, X.6    Shen, J.7    Jiang, H.8
  • 24
    • 0035045942 scopus 로고    scopus 로고
    • Recognition by macrophages and liver cells of opsonized phospholipids vesicles and phospholipid headgroups
    • Moghimi S.M., and Hunter A.C. Recognition by macrophages and liver cells of opsonized phospholipids vesicles and phospholipid headgroups. Pharm. Res. 18 (2000) 1-8
    • (2000) Pharm. Res. , vol.18 , pp. 1-8
    • Moghimi, S.M.1    Hunter, A.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.