메뉴 건너뛰기




Volumn 90, Issue 11-12, 2008, Pages 1637-1646

Effects of removing a conserved disulfide bond on the biological characteristics of rat lipocalin-type prostaglandin D synthase

Author keywords

Disulfide bond; Lipocalin type prostaglandin D synthase; NMR; Variant

Indexed keywords

ALANINE; CYSTEINE; LIPOCALIN; PROSTAGLANDIN D SYNTHASE;

EID: 55349087538     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2008.06.003     Document Type: Article
Times cited : (12)

References (28)
  • 1
    • 0033594990 scopus 로고    scopus 로고
    • Binding of biliverdin, bilirubin, and thyroid hormones to lipocalin-type prostaglandin D synthase
    • Beuckmann C.T., Aoyagi M., and Urade Y. Binding of biliverdin, bilirubin, and thyroid hormones to lipocalin-type prostaglandin D synthase. Biochemistry 38 (1999) 8006-8013
    • (1999) Biochemistry , vol.38 , pp. 8006-8013
    • Beuckmann, C.T.1    Aoyagi, M.2    Urade, Y.3
  • 2
    • 0034684216 scopus 로고    scopus 로고
    • Biochemical, structural, genetic, physiological, and pathophysiological features of lipocalin-type prostaglandin D synthase
    • Urade Y., and Hayaishi O. Biochemical, structural, genetic, physiological, and pathophysiological features of lipocalin-type prostaglandin D synthase. Biochim. Biophys. Acta 1482 (2000) 259-271
    • (2000) Biochim. Biophys. Acta , vol.1482 , pp. 259-271
    • Urade, Y.1    Hayaishi, O.2
  • 3
    • 0037284054 scopus 로고    scopus 로고
    • Cloning, expression, crystallization, and preliminary X-ray analysis of recombinant mouse lipocalin-type Prostaglandin D Synthase, a somnogen-producing enzyme
    • Irikura D., Kumasaka T., Yamamoto M., Ago H., Miyano M., Kubata K.B., Sakai H., Hayaishi O., and Urade Y. Cloning, expression, crystallization, and preliminary X-ray analysis of recombinant mouse lipocalin-type Prostaglandin D Synthase, a somnogen-producing enzyme. J. Biochem. 133 (2003) 29-32
    • (2003) J. Biochem. , vol.133 , pp. 29-32
    • Irikura, D.1    Kumasaka, T.2    Yamamoto, M.3    Ago, H.4    Miyano, M.5    Kubata, K.B.6    Sakai, H.7    Hayaishi, O.8    Urade, Y.9
  • 4
    • 0030472209 scopus 로고    scopus 로고
    • Glutathione-independent prostaglandin D synthase as a lead molecule for designing new functional proteins
    • Toh H., Kubodera H., Nakajima N., Sekiya T., Eguchi N., Tanaka T., Urade Y., and Hayaishi O. Glutathione-independent prostaglandin D synthase as a lead molecule for designing new functional proteins. Protein Eng. 9 (1996) 1067-1082
    • (1996) Protein Eng. , vol.9 , pp. 1067-1082
    • Toh, H.1    Kubodera, H.2    Nakajima, N.3    Sekiya, T.4    Eguchi, N.5    Tanaka, T.6    Urade, Y.7    Hayaishi, O.8
  • 6
    • 0031853060 scopus 로고    scopus 로고
    • Protein dynamics from NMR
    • Kay L.E. Protein dynamics from NMR. Nat. Struct. Biol. 5 (1998) 513-517
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 513-517
    • Kay, L.E.1
  • 7
    • 0026320866 scopus 로고
    • The energy landscapes and motions of proteins
    • Frauenfelder H., Sligar S.G., and Wolynes P.G. The energy landscapes and motions of proteins. Science 254 (1991) 1598-1603
    • (1991) Science , vol.254 , pp. 1598-1603
    • Frauenfelder, H.1    Sligar, S.G.2    Wolynes, P.G.3
  • 8
    • 33646596978 scopus 로고    scopus 로고
    • Highly efficient expression and purification system of small-size protein domains in Escherichia coli for biochemical characterization
    • Bao W.J., Gao Y.G., Chang Y.G., Zhang T.Y., Lin X.J., Yan X.Z., and Hu H.Y. Highly efficient expression and purification system of small-size protein domains in Escherichia coli for biochemical characterization. Protein Expr. Purif. 47 (2006) 599-606
    • (2006) Protein Expr. Purif. , vol.47 , pp. 599-606
    • Bao, W.J.1    Gao, Y.G.2    Chang, Y.G.3    Zhang, T.Y.4    Lin, X.J.5    Yan, X.Z.6    Hu, H.Y.7
  • 9
    • 0034992645 scopus 로고    scopus 로고
    • A method for efficient isotopic labeling of recombinant proteins
    • Marley J., Lu M., and Bracken C. A method for efficient isotopic labeling of recombinant proteins. J. Biomol. NMR 20 (2001) 71-75
    • (2001) J. Biomol. NMR , vol.20 , pp. 71-75
    • Marley, J.1    Lu, M.2    Bracken, C.3
  • 10
    • 0037481089 scopus 로고    scopus 로고
    • Association of fluorescent probes 1-anilinonaphthalene-8-sulfonate and 4,4′-dianilino-1,1′-binaphthyl-5,5′-disulfonic acid with T7 RNA polymerase
    • Ghosh U., Das M., and Dasgupta D. Association of fluorescent probes 1-anilinonaphthalene-8-sulfonate and 4,4′-dianilino-1,1′-binaphthyl-5,5′-disulfonic acid with T7 RNA polymerase. Biopolymers 72 (2003) 249-255
    • (2003) Biopolymers , vol.72 , pp. 249-255
    • Ghosh, U.1    Das, M.2    Dasgupta, D.3
  • 11
    • 0030048046 scopus 로고    scopus 로고
    • A simple assay for intracellular lipid-binding proteins using displacement of 1-anilinonaphthalene 8-sulfonic acid
    • Kane C.D., and Bernlohr D.A. A simple assay for intracellular lipid-binding proteins using displacement of 1-anilinonaphthalene 8-sulfonic acid. Anal. Biochem. 233 (1996) 197-204
    • (1996) Anal. Biochem. , vol.233 , pp. 197-204
    • Kane, C.D.1    Bernlohr, D.A.2
  • 12
    • 0033135193 scopus 로고    scopus 로고
    • 1-Anilino-8-naphthalene sulfonate as a protein conformational tightening agent
    • Matulis D., Baumann C.G., Bloomfield V.A., and Lovrien R.E. 1-Anilino-8-naphthalene sulfonate as a protein conformational tightening agent. Biopolymers 49 (1999) 451-458
    • (1999) Biopolymers , vol.49 , pp. 451-458
    • Matulis, D.1    Baumann, C.G.2    Bloomfield, V.A.3    Lovrien, R.E.4
  • 14
    • 0028053016 scopus 로고
    • Equilibrium unfolding studies of barstar: evidence for an alternative conformation which resembles a molten globule
    • Khurana R., and Udgaonkar J.B. Equilibrium unfolding studies of barstar: evidence for an alternative conformation which resembles a molten globule. Biochemistry 33 (1994) 106-115
    • (1994) Biochemistry , vol.33 , pp. 106-115
    • Khurana, R.1    Udgaonkar, J.B.2
  • 15
    • 33644506112 scopus 로고    scopus 로고
    • Comparative ligand-binding analysis of ten human lipocalins
    • Breustedt D.A., Schönfeld D.L., and Skerra A. Comparative ligand-binding analysis of ten human lipocalins. Biochim. Biophys. Acta 1764 (2006) 161-173
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 161-173
    • Breustedt, D.A.1    Schönfeld, D.L.2    Skerra, A.3
  • 16
    • 35248888536 scopus 로고    scopus 로고
    • Accumulation of partly folded states in the equilibrium unfolding of ervatamin A: spectroscopic description of the native, intermediate, and unfolded states
    • Nallamsetty S., Dubey V.K., Pande M., Ambasht P.K., and Jagannadham M.V. Accumulation of partly folded states in the equilibrium unfolding of ervatamin A: spectroscopic description of the native, intermediate, and unfolded states. Biochimie 89 (2007) 1416-1424
    • (2007) Biochimie , vol.89 , pp. 1416-1424
    • Nallamsetty, S.1    Dubey, V.K.2    Pande, M.3    Ambasht, P.K.4    Jagannadham, M.V.5
  • 17
    • 0037077265 scopus 로고    scopus 로고
    • Identification of a substrate recognition site on ubc9
    • Lin D., Tatham M.H., Yu B., Kim S., Hay R.T., and Chen Y. Identification of a substrate recognition site on ubc9. J. Biol. Chem. 277 (2002) 21740-21748
    • (2002) J. Biol. Chem. , vol.277 , pp. 21740-21748
    • Lin, D.1    Tatham, M.H.2    Yu, B.3    Kim, S.4    Hay, R.T.5    Chen, Y.6
  • 18
    • 0029790266 scopus 로고    scopus 로고
    • The lipocalin protein family: structure and function
    • Flower D.R. The lipocalin protein family: structure and function. Biochem. J. 318 (1996) 1-14
    • (1996) Biochem. J. , vol.318 , pp. 1-14
    • Flower, D.R.1
  • 19
    • 35748980301 scopus 로고    scopus 로고
    • NMR solution structure of lipocalin-type prostaglandin D synthase: evidence for partial overlapping of catalytic pocket and retinoic acid-binding pocket within the central cavity
    • Shimamoto S., Yoshida T., Inui T., Gohda K., Kobayashi Y., Fujimori K., Tsurumura T., Aritake K., Urade Y., and Ohkubo T. NMR solution structure of lipocalin-type prostaglandin D synthase: evidence for partial overlapping of catalytic pocket and retinoic acid-binding pocket within the central cavity. J. Biol. Chem. 282 (2007) 31373-31379
    • (2007) J. Biol. Chem. , vol.282 , pp. 31373-31379
    • Shimamoto, S.1    Yoshida, T.2    Inui, T.3    Gohda, K.4    Kobayashi, Y.5    Fujimori, K.6    Tsurumura, T.7    Aritake, K.8    Urade, Y.9    Ohkubo, T.10
  • 20
    • 0001911969 scopus 로고    scopus 로고
    • Sreerama N., Woody R.W., Berova N., Nakanishi K., and Woody R.W. (Eds), John Wiley and Sons, New York
    • In: Sreerama N., Woody R.W., Berova N., Nakanishi K., and Woody R.W. (Eds). Circular Dichroism - Principles and Applications (2000), John Wiley and Sons, New York 601-620
    • (2000) Circular Dichroism - Principles and Applications , pp. 601-620
  • 21
    • 0019005874 scopus 로고
    • Determination of protein secondary structure in solution by vacuum ultraviolet circular dichroism
    • Brahms S., and Brahms J. Determination of protein secondary structure in solution by vacuum ultraviolet circular dichroism. J. Mol. Biol. 138 (1980) 149-178
    • (1980) J. Mol. Biol. , vol.138 , pp. 149-178
    • Brahms, S.1    Brahms, J.2
  • 22
    • 0041341891 scopus 로고    scopus 로고
    • Competitive binding of fatty acids and the fluorescent probe 1-8-anilinonaphthalene sulfonate to bovine β-lactoglobulin
    • Collini M., D'Alfonso L., Molinari H., Ragona L., Catalano M., and Baldini G. Competitive binding of fatty acids and the fluorescent probe 1-8-anilinonaphthalene sulfonate to bovine β-lactoglobulin. Protein Sci. 12 (2003) 1596-1603
    • (2003) Protein Sci. , vol.12 , pp. 1596-1603
    • Collini, M.1    D'Alfonso, L.2    Molinari, H.3    Ragona, L.4    Catalano, M.5    Baldini, G.6
  • 23
    • 0032103101 scopus 로고    scopus 로고
    • Subtypes of odorant-binding proteins - heterologous expression and ligand binding
    • Löbel D., Marchese S., Krieger J., Pelosi P., and Breer H. Subtypes of odorant-binding proteins - heterologous expression and ligand binding. Eur. J. Biochem. 254 (1998) 318-324
    • (1998) Eur. J. Biochem. , vol.254 , pp. 318-324
    • Löbel, D.1    Marchese, S.2    Krieger, J.3    Pelosi, P.4    Breer, H.5
  • 24
    • 0026514355 scopus 로고
    • Spectrofluorimetric assessment of the surface hydrophobicity of proteins
    • Cardamone M., and Puri N.K. Spectrofluorimetric assessment of the surface hydrophobicity of proteins. Biochem. J. 282 (1992) 589-593
    • (1992) Biochem. J. , vol.282 , pp. 589-593
    • Cardamone, M.1    Puri, N.K.2
  • 25
    • 0024963570 scopus 로고
    • Conformational states of beta-lactamase: molten-globule states at acidic and alkaline pH with high salt
    • Goto Y., and Fink A.L. Conformational states of beta-lactamase: molten-globule states at acidic and alkaline pH with high salt. Biochemistry 28 (1989) 945-952
    • (1989) Biochemistry , vol.28 , pp. 945-952
    • Goto, Y.1    Fink, A.L.2
  • 26
    • 0029115374 scopus 로고
    • Kinetics of interaction of partially folded proteins with a hydrophobic dye: evidence that molten globule character is maximal in early folding intermediate
    • Engelhard M., and Evans P.A. Kinetics of interaction of partially folded proteins with a hydrophobic dye: evidence that molten globule character is maximal in early folding intermediate. Protein Sci. 4 (1995) 1553-1562
    • (1995) Protein Sci. , vol.4 , pp. 1553-1562
    • Engelhard, M.1    Evans, P.A.2
  • 27
    • 0032573356 scopus 로고    scopus 로고
    • Sequential unfolding of papain in molten globule state
    • Edwin F., and Jagannadham M.V. Sequential unfolding of papain in molten globule state. Biochem. Biophys. Res. Commun. 252 (1998) 654-660
    • (1998) Biochem. Biophys. Res. Commun. , vol.252 , pp. 654-660
    • Edwin, F.1    Jagannadham, M.V.2
  • 28
    • 0142031484 scopus 로고    scopus 로고
    • Differences in the unfolding of procerain induced by pH, guanidine hydrochloride, urea and temperature
    • Dubey V.K., and Jagannadham M.V. Differences in the unfolding of procerain induced by pH, guanidine hydrochloride, urea and temperature. Biochemistry 42 (2003) 12287-12297
    • (2003) Biochemistry , vol.42 , pp. 12287-12297
    • Dubey, V.K.1    Jagannadham, M.V.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.