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Volumn 18, Issue 7, 2009, Pages 1552-1563

Mutations of key hydrophobic surface residues of 11β-hydroxysteroid dehydrogenase type 1 increase solubility and monodispersity in a bacterial expression system

Author keywords

11 hydroxysteroid dehydrogenase type 1 (11 HSD1); Hydrophobicity; Mutation; Recombinant protein expression

Indexed keywords

11BETA HYDROXYSTEROID DEHYDROGENASE 1; OXIDOREDUCTASE; RECOMBINANT ENZYME; STEROID;

EID: 67650047734     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.150     Document Type: Article
Times cited : (10)

References (43)
  • 2
    • 0025606269 scopus 로고
    • Characterization of 11 β-hydroxysteroid dehydrogenase gene expression: Identification of multiple unique forms of messenger ribonucleic acid in the rat kidney
    • Krozowski Z, Stuchbery S, White P, Monder C, Funder JW (1990) Characterization of 11 β-hydroxysteroid dehydrogenase gene expression: identification of multiple unique forms of messenger ribonucleic acid in the rat kidney. Endocrinology 127: 3009-3013.
    • (1990) Endocrinology , vol.127 , pp. 3009-3013
    • Krozowski, Z.1    Stuchbery, S.2    White, P.3    Monder, C.4    Funder, J.W.5
  • 3
    • 23844516967 scopus 로고    scopus 로고
    • 11 β-Hydroxysteroid dehydrogenase and the pre-receptor regulation of corticosteroid hormone action
    • Draper N, Stewart PM (2005) 11 β-Hydroxysteroid dehydrogenase and the pre-receptor regulation of corticosteroid hormone action. J Endocrinol 186: 251-271.
    • (2005) J Endocrinol , vol.186 , pp. 251-271
    • Draper, N.1    Stewart, P.M.2
  • 4
    • 33745771031 scopus 로고    scopus 로고
    • Mechanisms of disease: Selective inhibition of 11 β-hydroxysteroid dehydrogenase type 1 as a novel treatment for the metabolic syndrome
    • Tomlinson JW, Stewart PM (2005) Mechanisms of disease: selective inhibition of 11 β-hydroxysteroid dehydrogenase type 1 as a novel treatment for the metabolic syndrome. Nat Clin Pract Endocrinol Metab 1: 92-99.
    • (2005) Nat Clin Pract Endocrinol Metab , vol.1 , pp. 92-99
    • Tomlinson, J.W.1    Stewart, P.M.2
  • 9
    • 0035798621 scopus 로고    scopus 로고
    • Improved lipid and lipoprotein profile, hepatic insulin sensitivity, and glucose tolerance in 11 β-hydroxysteroid dehydrogenase type 1 null mice
    • Morton NM, Holmes MC, Fievet C, Staels B, Tailleux A, Mullins JJ, Seckl JR (2001) Improved lipid and lipoprotein profile, hepatic insulin sensitivity, and glucose tolerance in 11 β-hydroxysteroid dehydrogenase type 1 null mice. J Biol Chem 276: 41293-41300.
    • (2001) J Biol Chem , vol.276 , pp. 41293-41300
    • Morton, N.M.1    Holmes, M.C.2    Fievet, C.3    Staels, B.4    Tailleux, A.5    Mullins, J.J.6    Seckl, J.R.7
  • 11
    • 42549158294 scopus 로고    scopus 로고
    • Demonstration of proof of mechanism and pharmacokinetics and pharmacodynamic relationship with PF-915275, an inhibitor of 11{β}HSD1, in cynomolgus monkeys
    • Bhat BG, Hosea N, Fanjul A, Herrera J, Chapman J, Thalacker F, Stewart PM, Rejto P (2007) Demonstration of proof of mechanism and pharmacokinetics and pharmacodynamic relationship with PF-915275, an inhibitor of 11{β}HSD1, in cynomolgus monkeys. J Pharmacol Exp Ther 5: 5.
    • (2007) J Pharmacol Exp Ther , vol.5 , pp. 5
    • Bhat, B.G.1    Hosea, N.2    Fanjul, A.3    Herrera, J.4    Chapman, J.5    Thalacker, F.6    Stewart, P.M.7    Rejto, P.8
  • 12
    • 0028899788 scopus 로고
    • Lumenal orientation and post-translational modifications of the liver microsomal 11 β-hydroxysteroid dehydrogenase
    • Ozols J (1995) Lumenal orientation and post-translational modifications of the liver microsomal 11 β-hydroxysteroid dehydrogenase. J Biol Chem 270: 10360.
    • (1995) J Biol Chem , vol.270 , pp. 10360
    • Ozols, J.1
  • 13
    • 0037133133 scopus 로고    scopus 로고
    • 11 β-Hydroxysteroid dehydrogenase type 1 from human liver: Dimerization and enzyme cooperativity support its postulated role as glucocorticoid reductase
    • Maser E, Volker B, Friebertshauser J (2002) 11 β-Hydroxysteroid dehydrogenase type 1 from human liver: dimerization and enzyme cooperativity support its postulated role as glucocorticoid reductase. Biochemistry 41: 2459-2465.
    • (2002) Biochemistry , vol.41 , pp. 2459-2465
    • Maser, E.1    Volker, B.2    Friebertshauser, J.3
  • 14
    • 14244252559 scopus 로고    scopus 로고
    • Conformational flexibility in crystal structures of human 11 β-hydroxysteroid dehydrogenase type I provide insights into glucocorticoid interconversion and enzyme regulation
    • Hosfield DJ, Wu Y, Skene RJ, Hilgers M, Jennings A, Snell GP, Aertgeerts K (2005) Conformational flexibility in crystal structures of human 11 β-hydroxysteroid dehydrogenase type I provide insights into glucocorticoid interconversion and enzyme regulation. J Biol Chem 280: 4639-4648.
    • (2005) J Biol Chem , vol.280 , pp. 4639-4648
    • Hosfield, D.J.1    Wu, Y.2    Skene, R.J.3    Hilgers, M.4    Jennings, A.5    Snell, G.P.6    Aertgeerts, K.7
  • 15
    • 0033553424 scopus 로고    scopus 로고
    • Targeting proteins to the lumen of endoplasmic reticulum using N-terminal domains of 11 β-hydroxysteroid dehydrogenase and the 50-kDa esterase
    • Mziaut H, Korza G, Hand AR, Gerard C, Ozols J (1999) Targeting proteins to the lumen of endoplasmic reticulum using N-terminal domains of 11 β-hydroxysteroid dehydrogenase and the 50-kDa esterase. J Biol Chem 274: 14122-14129.
    • (1999) J Biol Chem , vol.274 , pp. 14122-14129
    • Mziaut, H.1    Korza, G.2    Hand, A.R.3    Gerard, C.4    Ozols, J.5
  • 16
    • 0033214482 scopus 로고    scopus 로고
    • The N-terminal anchor sequences of 11 β-hydroxysteroid dehydrogenases determine their orientation in the endoplasmic reticulum membrane
    • Odermatt A, Arnold P, Stauffer A, Frey BM, Frey FJ (1999) The N-terminal anchor sequences of 11 β-hydroxysteroid dehydrogenases determine their orientation in the endoplasmic reticulum membrane. J Biol Chem 274: 28762-28770.
    • (1999) J Biol Chem , vol.274 , pp. 28762-28770
    • Odermatt, A.1    Arnold, P.2    Stauffer, A.3    Frey, B.M.4    Frey, F.J.5
  • 17
    • 0035877598 scopus 로고    scopus 로고
    • Functional expression, characterization, and purification of the catalytic domain of human 11-β-hydroxysteroid dehydrogenase type 1
    • Walker EA, Clark AM, Hewison M, Ride JP, Stewart PM (2001) Functional expression, characterization, and purification of the catalytic domain of human 11-β-hydroxysteroid dehydrogenase type 1. J Biol Chem 276: 21343-21350.
    • (2001) J Biol Chem , vol.276 , pp. 21343-21350
    • Walker, E.A.1    Clark, A.M.2    Hewison, M.3    Ride, J.P.4    Stewart, P.M.5
  • 19
    • 0034710774 scopus 로고    scopus 로고
    • Human 11 β-hydroxysteroid dehydrogenase type 1 is enzymatically active in its nonglycosylated form
    • Blum A, Martin HJ, Maser E (2000) Human 11 β-hydroxysteroid dehydrogenase type 1 is enzymatically active in its nonglycosylated form. Biochem Biophys Res Commun 276: 428-434.
    • (2000) Biochem Biophys Res Commun , vol.276 , pp. 428-434
    • Blum, A.1    Martin, H.J.2    Maser, E.3
  • 22
    • 0029738872 scopus 로고    scopus 로고
    • Experimentally determined hydrophobicity scale for proteins at membrane interfaces
    • Wimley WC, White SH (1996) Experimentally determined hydrophobicity scale for proteins at membrane interfaces. Nat Struct Biol 3: 842-848.
    • (1996) Nat Struct Biol , vol.3 , pp. 842-848
    • Wimley, W.C.1    White, S.H.2
  • 24
    • 13644269232 scopus 로고    scopus 로고
    • The crystal structure of guinea pig 11 β-hydroxysteroid dehydrogenase type 1 provides a model for enzyme-lipid bilayer interactions
    • Ogg D, Elleby B, Norstrom C, Stefansson K, Abrahmsen L, Oppermann U, Svensson S (2005) The crystal structure of guinea pig 11 β-hydroxysteroid dehydrogenase type 1 provides a model for enzyme-lipid bilayer interactions. J Biol Chem 280: 3789-3794.
    • (2005) J Biol Chem , vol.280 , pp. 3789-3794
    • Ogg, D.1    Elleby, B.2    Norstrom, C.3    Stefansson, K.4    Abrahmsen, L.5    Oppermann, U.6    Svensson, S.7
  • 25
    • 0033970047 scopus 로고    scopus 로고
    • Mammalian microsomal cytochrome P450 monooxygenase: Structural adaptations for membrane binding and functional diversity
    • Williams PA, Cosme J, Sridhar V, Johnson EF, McRee DE (2000) Mammalian microsomal cytochrome P450 monooxygenase: structural adaptations for membrane binding and functional diversity. Mol Cell 5: 121-131.
    • (2000) Mol Cell , vol.5 , pp. 121-131
    • Williams, P.A.1    Cosme, J.2    Sridhar, V.3    Johnson, E.F.4    McRee, D.E.5
  • 26
    • 0027497950 scopus 로고
    • Expression of truncated forms of liver microsomal P450 cytochromes 2B4 and 2E1 in Escherichia coli: Influence of NH2-terminal region on localization in cytosol and membranes
    • Pernecky SJ, Larson JR, Philpot RM, Coon MJ (1993) Expression of truncated forms of liver microsomal P450 cytochromes 2B4 and 2E1 in Escherichia coli: influence of NH2-terminal region on localization in cytosol and membranes. Proc Natl Acad Sci USA 90: 2651-2655.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 2651-2655
    • Pernecky, S.J.1    Larson, J.R.2    Philpot, R.M.3    Coon, M.J.4
  • 27
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling
    • Schuck P (2000) Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling. Biophys J 78: 1606-1619.
    • (2000) Biophys J , vol.78 , pp. 1606-1619
    • Schuck, P.1
  • 30
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel E, Henrick K (2007) Inference of macromolecular assemblies from crystalline state. J Mol Biol 372: 774-797.
    • (2007) J Mol Biol , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 31
    • 0033545521 scopus 로고    scopus 로고
    • Amino acid substitutions affecting protein solubility: High level expression of Streptomyces clavuligerus isopenicillin N synthase in Escherichia coli
    • Sim J, Sim TS (1999) Amino acid substitutions affecting protein solubility: high level expression of Streptomyces clavuligerus isopenicillin N synthase in Escherichia coli. J Mol Catal B 6: 133-143.
    • (1999) J Mol Catal B , vol.6 , pp. 133-143
    • Sim, J.1    Sim, T.S.2
  • 33
    • 0344874146 scopus 로고    scopus 로고
    • Structure-based substitutions for increased solubility of a designed protein
    • Mosavi LK, Peng ZY (2003) Structure-based substitutions for increased solubility of a designed protein. Protein Eng 16: 739-745.
    • (2003) Protein Eng , vol.16 , pp. 739-745
    • Mosavi, L.K.1    Peng, Z.Y.2
  • 34
    • 0028103565 scopus 로고
    • Improving protein solubility through rationally designed amino-acid replacements-solubilization of the trimethoprim-resistant type S1 dihydrofolate-reductase
    • Dale GE, Broger C, Langen H, Darcy A, Stuber D (1994) Improving protein solubility through rationally designed amino-acid replacements-solubilization of the trimethoprim-resistant type S1 dihydrofolate-reductase. Protein Eng 7: 933-939.
    • (1994) Protein Eng , vol.7 , pp. 933-939
    • Dale, G.E.1    Broger, C.2    Langen, H.3    Darcy, A.4    Stuber, D.5
  • 35
    • 0030965970 scopus 로고    scopus 로고
    • Disrupting the hydrophobic patches at the antibody variable/ constant domain interface: Improved in vivo folding and physical characterization of an engineered scFv fragment
    • Nieba L, Honegger A, Krebber C, Pluckthun A (1997) Disrupting the hydrophobic patches at the antibody variable/ constant domain interface: improved in vivo folding and physical characterization of an engineered scFv fragment. Protein Eng 10: 435-444.
    • (1997) Protein Eng , vol.10 , pp. 435-444
    • Nieba, L.1    Honegger, A.2    Krebber, C.3    Pluckthun, A.4
  • 38
    • 34247132757 scopus 로고    scopus 로고
    • Assay optimization and kinetic profile of the human and the rabbit isoforms of 11 β-HSD1
    • Castro A, Zhu JX, Alton GR, Rejto P, Ermolieff J (2007) Assay optimization and kinetic profile of the human and the rabbit isoforms of 11 β-HSD1. Biochem Biophys Res Commun 357: 561-566.
    • (2007) Biochem Biophys Res Commun , vol.357 , pp. 561-566
    • Castro, A.1    Zhu, J.X.2    Alton, G.R.3    Rejto, P.4    Ermolieff, J.5
  • 39
    • 0037449710 scopus 로고    scopus 로고
    • Comparative enzymology of 11 β-hydroxysteroid dehydrogenase type 1 from glucocorticoid resistant (Guinea pig) versus sensitive (human) species
    • Shafqat N, Elleby B, Svensson S, Shafqat J, Jornvall H, Abrahmsen L, Oppermann U (2003) Comparative enzymology of 11 β-hydroxysteroid dehydrogenase type 1 from glucocorticoid resistant (Guinea pig) versus sensitive (human) species. J Biol Chem 278: 2030-2035.
    • (2003) J Biol Chem , vol.278 , pp. 2030-2035
    • Shafqat, N.1    Elleby, B.2    Svensson, S.3    Shafqat, J.4    Jornvall, H.5    Abrahmsen, L.6    Oppermann, U.7
  • 41
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch W (1993) Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J Appl Cryst 26: 795-800.
    • (1993) J Appl Cryst , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 42
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • Perrakis A, Morris R, Lamzin VS (1999) Automated protein model building combined with iterative structure refinement. Nat Struct Biol 6: 458-463.
    • (1999) Nat Struct Biol , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.