메뉴 건너뛰기




Volumn 288, Issue 43, 2013, Pages 31093-31104

Conformational plasticity and ligand binding of bacterial monoacylglycerol lipase

Author keywords

[No Author keywords available]

Indexed keywords

CONFORMATIONAL CHANGE; CONFORMATIONAL PLASTICITY; DIFFERENT SUBSTRATES; HYDROLASE ACTIVITIES; HYDROLYTIC REACTIONS; SITE DIRECTED MUTAGENESIS; STRUCTURAL SIMILARITY; THREE-DIMENSIONAL STRUCTURE;

EID: 84886673603     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.491415     Document Type: Article
Times cited : (43)

References (46)
  • 4
    • 0026550733 scopus 로고
    • Catalysis at the interface, the anatomy of a conformational change in a triglyceride lipase
    • Derewenda, U., Brzozowski, A. M., Lawson, D. M., and Derewenda, Z. S. (1992) Catalysis at the interface, the anatomy of a conformational change in a triglyceride lipase. Biochemistry 31, 1532-1541
    • (1992) Biochemistry , vol.31 , pp. 1532-1541
    • Derewenda, U.1    Brzozowski, A.M.2    Lawson, D.M.3    Derewenda, Z.S.4
  • 5
    • 84864311544 scopus 로고    scopus 로고
    • Molecular basis for substrate selectivity of a mono- and diacylglycerol lipase from Malassezia globosa
    • Liu, L., Gao, C., Lan, D., Yang, B., and Wang, Y. (2012) Molecular basis for substrate selectivity of a mono- and diacylglycerol lipase from Malassezia globosa. Biochem. Biophys. Res. Commun. 424, 285-289
    • (2012) Biochem. Biophys. Res. Commun. , vol.424 , pp. 285-289
    • Liu, L.1    Gao, C.2    Lan, D.3    Yang, B.4    Wang, Y.5
  • 6
    • 84861481172 scopus 로고    scopus 로고
    • Crystal structure of a mono- and diacylglycerol lipase from Malassezia globosa reveals a novel lid conformation and insights into the substrate specificity
    • Xu, T., Liu, L., Hou, S., Xu, J., Yang, B., Wang, Y., and Liu, J. (2012) Crystal structure of a mono- and diacylglycerol lipase from Malassezia globosa reveals a novel lid conformation and insights into the substrate specificity. J. Struct. Biol. 178, 363-369
    • (2012) J. Struct. Biol. , vol.178 , pp. 363-369
    • Xu, T.1    Liu, L.2    Hou, S.3    Xu, J.4    Yang, B.5    Wang, Y.6    Liu, J.7
  • 7
    • 0019481108 scopus 로고
    • Hormonesensitive lipase of rat adipose tissue. Purification and some properties
    • Fredrikson, G., Strålfors, P., Nilsson, N. O., and Belfrage, P. (1981) Hormonesensitive lipase of rat adipose tissue. Purification and some properties. J. Biol. Chem. 256, 6311-6320
    • (1981) J. Biol. Chem. , vol.256 , pp. 6311-6320
    • Fredrikson, G.1    Strålfors, P.2    Nilsson, N.O.3    Belfrage, P.4
  • 8
    • 84886685918 scopus 로고
    • The specificity of an intestinal lipase for monoglycerides
    • Pope, J. L., Askins, R. E., and McPherson, J. C. (1962) The specificity of an intestinal lipase for monoglycerides. Fed. Proc. 21, 259
    • (1962) Fed. Proc. , vol.21 , pp. 259
    • Pope, J.L.1    Askins, R.E.2    McPherson, J.C.3
  • 9
    • 37549043542 scopus 로고    scopus 로고
    • Characterization of an exported monoglyceride lipase from Mycobacterium tuberculosis possibly involved in the metabolism of host cell membrane lipids
    • Côtes, K., Dhouib, R., Douchet, I., Chahinian, H., de Caro, A., Carrière, F., and Canaan, S. (2007) Characterization of an exported monoglyceride lipase from Mycobacterium tuberculosis possibly involved in the metabolism of host cell membrane lipids. Biochem. J. 408, 417-427
    • (2007) Biochem. J. , vol.408 , pp. 417-427
    • Côtes, K.1    Dhouib, R.2    Douchet, I.3    Chahinian, H.4    De Caro, A.5    Carrière, F.6    Canaan, S.7
  • 10
    • 77956544548 scopus 로고    scopus 로고
    • A monoacylglycerol lipase from Mycobacterium smegmatis involved in bacterial cell interaction
    • Dhouib, R., Laval, F., Carrière, F., Daffé, M., and Canaan, S. (2010) A monoacylglycerol lipase from Mycobacterium smegmatis involved in bacterial cell interaction. J. Bacteriol. 192, 4776-4785
    • (2010) J. Bacteriol. , vol.192 , pp. 4776-4785
    • Dhouib, R.1    Laval, F.2    Carrière, F.3    Daffé, M.4    Canaan, S.5
  • 12
    • 0034049622 scopus 로고    scopus 로고
    • Expression, purification, and characterization of histidine-tagged mouse monoglyceride lipase from baculovirus-infected insect cells
    • Karlsson, M., Tornqvist, H., and Holm, C. (2000) Expression, purification, and characterization of histidine-tagged mouse monoglyceride lipase from baculovirus-infected insect cells. Protein Expr. Purif. 18, 286-292
    • (2000) Protein Expr. Purif. , vol.18 , pp. 286-292
    • Karlsson, M.1    Tornqvist, H.2    Holm, C.3
  • 15
    • 6944247598 scopus 로고    scopus 로고
    • RNA interference suggests a primary role for monoacylglycerol lipase in the degradation of the endocannabinoid 2-arachidonoylglycerol
    • Dinh, T. P., Kathuria, S., and Piomelli, D. (2004) RNA interference suggests a primary role for monoacylglycerol lipase in the degradation of the endocannabinoid 2-arachidonoylglycerol. Mol. Pharmacol. 66, 1260-1264
    • (2004) Mol. Pharmacol. , vol.66 , pp. 1260-1264
    • Dinh, T.P.1    Kathuria, S.2    Piomelli, D.3
  • 16
    • 77955614363 scopus 로고    scopus 로고
    • A review on the monoacylglycerol lipase: At the interface between fat and endocannabinoid signalling
    • Labar, G., Wouters, J., and Lambert, D. M. (2010) A review on the monoacylglycerol lipase: at the interface between fat and endocannabinoid signalling. Curr. Med. Chem. 17, 2588-2607
    • (2010) Curr. Med. Chem. , vol.17 , pp. 2588-2607
    • Labar, G.1    Wouters, J.2    Lambert, D.M.3
  • 18
    • 0015687319 scopus 로고
    • Antimicrobial action of esters of polyhydric alcohols
    • Conley, A. J., and Kabara, J. J. (1973) Antimicrobial action of esters of polyhydric alcohols. Antimicrob. Agents Chemother. 4, 501-506
    • (1973) Antimicrob. Agents Chemother. , vol.4 , pp. 501-506
    • Conley, A.J.1    Kabara, J.J.2
  • 20
    • 0017688869 scopus 로고
    • Antimicrobial lipids: Natural and synthetic fatty acids and monoglycerides
    • Kabara, J. J., and Vrable, R. (1977) Antimicrobial lipids: natural and synthetic fatty acids and monoglycerides. Lipids 12, 753-759
    • (1977) Lipids , vol.12 , pp. 753-759
    • Kabara, J.J.1    Vrable, R.2
  • 21
    • 76649126721 scopus 로고    scopus 로고
    • Crystal structure of the human monoacylglycerol lipase, a key actor in endocannabinoid signaling
    • Labar, G., Bauvois, C., Borel, F., Ferrer, J. L., Wouters, J., and Lambert, D. M. (2010) Crystal structure of the human monoacylglycerol lipase, a key actor in endocannabinoid signaling. ChemBioChem 11, 218-227
    • (2010) ChemBioChem , vol.11 , pp. 218-227
    • Labar, G.1    Bauvois, C.2    Borel, F.3    Ferrer, J.L.4    Wouters, J.5    Lambert, D.M.6
  • 25
    • 0034108930 scopus 로고    scopus 로고
    • Purification and characterization of a monoacylglycerol lipase from the moderately thermophilic Bacillus sp. H-257
    • Imamura, S., and Kitaura, S. (2000) Purification and characterization of a monoacylglycerol lipase from the moderately thermophilic Bacillus sp. H-257. J. Biochem. 127, 419-425
    • (2000) J. Biochem. , vol.127 , pp. 419-425
    • Imamura, S.1    Kitaura, S.2
  • 26
    • 0035046039 scopus 로고    scopus 로고
    • Monoacylglycerol lipase from moderately thermophilic Bacillus sp strain H-257: Molecular cloning, sequencing, and expression in Escherichia coli of the gene
    • Kitaura, S., Suzuki, K., and Imamura, S. (2001) Monoacylglycerol lipase from moderately thermophilic Bacillus sp. strain H-257: molecular cloning, sequencing, and expression in Escherichia coli of the gene. J. Biochem. 129, 397-402
    • (2001) J. Biochem. , vol.129 , pp. 397-402
    • Kitaura, S.1    Suzuki, K.2    Imamura, S.3
  • 27
    • 70349597601 scopus 로고    scopus 로고
    • Electronic ligand builder and optimization workbench (eLBOW): A tool for ligand coordinate and restraint generation
    • Moriarty, N. W., Grosse-Kunstleve, R. W., and Adams, P. D. (2009) Electronic ligand builder and optimization workbench (eLBOW): a tool for ligand coordinate and restraint generation. Acta Crystallogr. D Biol. Crystallogr. 65, 1074-1080
    • (2009) Acta Crystallogr. D Biol. Crystallogr. , vol.65 , pp. 1074-1080
    • Moriarty, N.W.1    Grosse-Kunstleve, R.W.2    Adams, P.D.3
  • 30
  • 38
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • Perrakis, A., Morris, R., and Lamzin, V. S. (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
  • 40
    • 0030874881 scopus 로고    scopus 로고
    • Lipases and α/β-hydrolase fold
    • Schrag, J. D., and Cygler, M. (1997) Lipases and α/β-hydrolase fold. Methods Enzymol. 284, 85-107
    • (1997) Methods Enzymol. , vol.284 , pp. 85-107
    • Schrag, J.D.1    Cygler, M.2
  • 41
    • 80052795491 scopus 로고    scopus 로고
    • Molecular basis of chiral acid recognition by Candida rugosa lipase: X-ray structure of transition state analog and modeling of the hydrolysis of methyl 2-methoxy-2-phenylacetate
    • Colton, I. J., Yin, D., Grochulski, P., and Kazlauskas, R. J. (2011) Molecular basis of chiral acid recognition by Candida rugosa lipase: x-ray structure of transition state analog and modeling of the hydrolysis of methyl 2-methoxy-2-phenylacetate. Advanced Synthesis and Catalysis 353, 2529-2544
    • (2011) Advanced Synthesis and Catalysis , vol.353 , pp. 2529-2544
    • Colton, I.J.1    Yin, D.2    Grochulski, P.3    Kazlauskas, R.J.4
  • 42
    • 0029161231 scopus 로고
    • The 2.46 Å resolution structure of the pancreatic lipase-colipase complex inhibited by a C11 alkyl phosphonate
    • Egloff, M. P., Marguet, F., Buono, G., Verger, R., Cambillau, C., and van Tilbeurgh, H. (1995) The 2.46 Å resolution structure of the pancreatic lipase-colipase complex inhibited by a C11 alkyl phosphonate. Biochemistry 34, 2751-2762
    • (1995) Biochemistry , vol.34 , pp. 2751-2762
    • Egloff, M.P.1    Marguet, F.2    Buono, G.3    Verger, R.4    Cambillau, C.5    Van Tilbeurgh, H.6
  • 45
    • 33749575838 scopus 로고    scopus 로고
    • A versatile library of activity-based probes for fluorescence detection and/or affinity isolation of lipolytic enzymes
    • Susani-Etzerodt, H., Schmidinger, H., Riesenhuber, G., Birner-Gruenberger, R., and Hermetter, A. (2006) A versatile library of activity-based probes for fluorescence detection and/or affinity isolation of lipolytic enzymes. Chem. Phys. Lipids 144, 60-68
    • (2006) Chem. Phys. Lipids , vol.144 , pp. 60-68
    • Susani-Etzerodt, H.1    Schmidinger, H.2    Riesenhuber, G.3    Birner-Gruenberger, R.4    Hermetter, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.