메뉴 건너뛰기




Volumn 92, Issue 8, 2010, Pages 949-957

The hormone-sensitive lipase from Psychrobacter sp. TA144: New insight in the structural/functional characterization

Author keywords

hydrolase fold; Cold active enzymes; Ester synthesis; Esterases; Lipases; Psychrophilic micro organisms

Indexed keywords

ACETONITRILE; BACTERIAL ENZYME; CARBON; COPPER; ESTER; FATTY ACID; GENOMIC DNA; HORMONE SENSITIVE LIPASE; IRON; MANGANESE; MERCURY; METHANOL; PSYCHROBACTER HORMONE SENSITIVE LIPASE; RECOMBINANT PROTEIN; SEA WATER; UNCLASSIFIED DRUG; VALERIC ACID; ZINC;

EID: 77954658506     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2010.04.001     Document Type: Article
Times cited : (31)

References (31)
  • 2
    • 4644368803 scopus 로고    scopus 로고
    • The crystal structure of an EST2 mutant unveils structural insights on the H group of the carboxylesterase/lipase family
    • De Simone G., Menchise V., Alterio V., Mandrich L., Rossi M., Manco G., Pedone C. The crystal structure of an EST2 mutant unveils structural insights on the H group of the carboxylesterase/lipase family. Journal Molecular Biology 2004, 343:137-146.
    • (2004) Journal Molecular Biology , vol.343 , pp. 137-146
    • De Simone, G.1    Menchise, V.2    Alterio, V.3    Mandrich, L.4    Rossi, M.5    Manco, G.6    Pedone, C.7
  • 3
    • 0031866670 scopus 로고    scopus 로고
    • ACHEdb: the database system for ESTHER, the alpha/beta fold family of proteins and the Cholinesterase gene server
    • Cousin X., Hotelier T., Gliles K., Toutant J.P., Chatonnet A. aCHEdb: the database system for ESTHER, the alpha/beta fold family of proteins and the Cholinesterase gene server. Nucleic Acids Research 1998, 26:226-228.
    • (1998) Nucleic Acids Research , vol.26 , pp. 226-228
    • Cousin, X.1    Hotelier, T.2    Gliles, K.3    Toutant, J.P.4    Chatonnet, A.5
  • 5
    • 0034844565 scopus 로고    scopus 로고
    • Structure-function relationships of hormone-sensitive lipase
    • Osterlund T. Structure-function relationships of hormone-sensitive lipase. European Journal of Biochemistry 2001, 268:1899-1907.
    • (2001) European Journal of Biochemistry , vol.268 , pp. 1899-1907
    • Osterlund, T.1
  • 6
    • 0027198857 scopus 로고
    • Gene organization and primary structure of human hormone-sensitive lipase: possible significance of a sequence homology with a lipase of Moraxella TA144, an Antarctic bacterium
    • Langin D., Laurell H., Holst L.S., Belfrage P., Holm C. Gene organization and primary structure of human hormone-sensitive lipase: possible significance of a sequence homology with a lipase of Moraxella TA144, an Antarctic bacterium. Proceeding National Academy Science U.S.A. 1993, 90:4897-4901.
    • (1993) Proceeding National Academy Science U.S.A. , vol.90 , pp. 4897-4901
    • Langin, D.1    Laurell, H.2    Holst, L.S.3    Belfrage, P.4    Holm, C.5
  • 7
    • 0033214082 scopus 로고    scopus 로고
    • Bacterial lipolytic enzymes: classification and properties
    • Arpigny J.L., Jaeger K.E. Bacterial lipolytic enzymes: classification and properties. Biochemical Journal 1999, 343:177-183.
    • (1999) Biochemical Journal , vol.343 , pp. 177-183
    • Arpigny, J.L.1    Jaeger, K.E.2
  • 9
    • 69549084345 scopus 로고    scopus 로고
    • Alpha/beta hydrolase fold; an update
    • Carr P.D., Ollis D.L. Alpha/beta hydrolase fold; an update. Protein Peptide Letters 2009, 16:1137-1148.
    • (2009) Protein Peptide Letters , vol.16 , pp. 1137-1148
    • Carr, P.D.1    Ollis, D.L.2
  • 10
    • 1842855257 scopus 로고    scopus 로고
    • Hormone-sensitive lipase-new roles for an old enzyme
    • Yeaman S.J. Hormone-sensitive lipase-new roles for an old enzyme. Biochemical Journal 2004, 379:11-22.
    • (2004) Biochemical Journal , vol.379 , pp. 11-22
    • Yeaman, S.J.1
  • 11
    • 0036794551 scopus 로고    scopus 로고
    • Hormone-sensitive lipase: control of intracellular tri- (di-) acylglycerol and cholesteryl ester hydrolysis
    • Kraemer F.B., Shen W.J. Hormone-sensitive lipase: control of intracellular tri- (di-) acylglycerol and cholesteryl ester hydrolysis. Journal Lipid Research 2002, 43:1585-1594.
    • (2002) Journal Lipid Research , vol.43 , pp. 1585-1594
    • Kraemer, F.B.1    Shen, W.J.2
  • 12
    • 34248340524 scopus 로고    scopus 로고
    • The role of neutral lipases in human adipose tissue lipolysis
    • Arner P., Langin D. The role of neutral lipases in human adipose tissue lipolysis. Current Opinion Lipidology 2007, 18:246-250.
    • (2007) Current Opinion Lipidology , vol.18 , pp. 246-250
    • Arner, P.1    Langin, D.2
  • 15
    • 23944463152 scopus 로고    scopus 로고
    • A thermostable phosphotriesterase from the archaeon Sulfolobus solfataricus: cloning, overexpression and properties
    • Merone L., Mandrich L., Rossi M., Manco G. A thermostable phosphotriesterase from the archaeon Sulfolobus solfataricus: cloning, overexpression and properties. Extremophiles 2005, 9:297-305.
    • (2005) Extremophiles , vol.9 , pp. 297-305
    • Merone, L.1    Mandrich, L.2    Rossi, M.3    Manco, G.4
  • 16
    • 9644275365 scopus 로고    scopus 로고
    • Role of the N-terminus in enzyme activity, stability and specificity in thermophilic esterases belonging to the HSL family
    • Mandrich L., Merone L., Pezzullo M., Cipolla L., Nicotra F., Rossi M., Manco G. Role of the N-terminus in enzyme activity, stability and specificity in thermophilic esterases belonging to the HSL family. Journal Molecular Biology 2005, 345:501-512.
    • (2005) Journal Molecular Biology , vol.345 , pp. 501-512
    • Mandrich, L.1    Merone, L.2    Pezzullo, M.3    Cipolla, L.4    Nicotra, F.5    Rossi, M.6    Manco, G.7
  • 17
    • 31044446981 scopus 로고    scopus 로고
    • Substrate specificity and kinetic properties of enzymes belonging to the hormone-sensitive lipase family: comparison with non-lipolytic and lipolytic carboxylesterases
    • Chahinian H., Ali Y.B., Abousalham A., Petry S., Mandrich L., Manco G., Canaan S., Sarda L. Substrate specificity and kinetic properties of enzymes belonging to the hormone-sensitive lipase family: comparison with non-lipolytic and lipolytic carboxylesterases. Biochemical Biophysical Acta 2005, 1738:29-36.
    • (2005) Biochemical Biophysical Acta , vol.1738 , pp. 29-36
    • Chahinian, H.1    Ali, Y.B.2    Abousalham, A.3    Petry, S.4    Mandrich, L.5    Manco, G.6    Canaan, S.7    Sarda, L.8
  • 18
    • 0023066978 scopus 로고
    • Cystathionine beta-lyase from Escherichia coli
    • Uren J.R. Cystathionine beta-lyase from Escherichia coli. Methods Enzymology 1987, 143:483-486.
    • (1987) Methods Enzymology , vol.143 , pp. 483-486
    • Uren, J.R.1
  • 23
    • 0036168995 scopus 로고    scopus 로고
    • Dichroweb: an interactive website for the analysis of secondary structure from circular dichroism data
    • Lobley A., Whitmore A.L., Wallace B.A. Dichroweb: an interactive website for the analysis of secondary structure from circular dichroism data. Bioinformatics 2002, 18:211-212.
    • (2002) Bioinformatics , vol.18 , pp. 211-212
    • Lobley, A.1    Whitmore, A.L.2    Wallace, B.A.3
  • 24
    • 1242284208 scopus 로고    scopus 로고
    • Cold-active esterase from Psychrobacter sp. Ant300: gene cloning, characterization, and the effects of Gly->Pro substitution near the active site on its catalytic activity and stability
    • Kulakova L., Galkin A., Nakayama T., Nishino T., Esaki N. Cold-active esterase from Psychrobacter sp. Ant300: gene cloning, characterization, and the effects of Gly->Pro substitution near the active site on its catalytic activity and stability. Biochemical Biophysical Acta 2004, 1696:59-65.
    • (2004) Biochemical Biophysical Acta , vol.1696 , pp. 59-65
    • Kulakova, L.1    Galkin, A.2    Nakayama, T.3    Nishino, T.4    Esaki, N.5
  • 25
    • 59849106371 scopus 로고    scopus 로고
    • Protein promiscuity and its implications for biotechnology
    • Nobeli I., Favia A.D., Thornton J.M. Protein promiscuity and its implications for biotechnology. Nature Biotechnology 2009, 27:157-167.
    • (2009) Nature Biotechnology , vol.27 , pp. 157-167
    • Nobeli, I.1    Favia, A.D.2    Thornton, J.M.3
  • 26
    • 0024747511 scopus 로고
    • Catalytic activity and denaturation of enzymes in water/organic cosolvent mixtures: a-chymotrypsin and laccase in mixed water/alcohol; water/glycol and water/formamide solvents
    • Mozhaev V.V., Khmelnitsky Y.L., Sergeeva M.V., Belova N.L., Klyachko N.L., Levashov A.V., Martinek K. Catalytic activity and denaturation of enzymes in water/organic cosolvent mixtures: a-chymotrypsin and laccase in mixed water/alcohol; water/glycol and water/formamide solvents. European Journal Biochemistry 1989, 184:597-602.
    • (1989) European Journal Biochemistry , vol.184 , pp. 597-602
    • Mozhaev, V.V.1    Khmelnitsky, Y.L.2    Sergeeva, M.V.3    Belova, N.L.4    Klyachko, N.L.5    Levashov, A.V.6    Martinek, K.7
  • 27
    • 49349093802 scopus 로고    scopus 로고
    • Molecular cloning and expression of a cold-adapted lipase gene from an Antarctic deep sea psychrotrophic bacterium Pseudomonas sp. 7323
    • Zhang J., Zeng R. Molecular cloning and expression of a cold-adapted lipase gene from an Antarctic deep sea psychrotrophic bacterium Pseudomonas sp. 7323. Marine Biotechnology 2008, 10:612-621.
    • (2008) Marine Biotechnology , vol.10 , pp. 612-621
    • Zhang, J.1    Zeng, R.2
  • 28
    • 0025732362 scopus 로고
    • Nucleotide sequence of the lipase gene lip2 from the Antarctic psychrotroph Moraxella TA144 and site-specific mutagenesis of the conserved serine and histidine residues
    • Feller G., Thiry M., Gerday C. Nucleotide sequence of the lipase gene lip2 from the Antarctic psychrotroph Moraxella TA144 and site-specific mutagenesis of the conserved serine and histidine residues. DNA Cell Biology 1991, 10:381-388.
    • (1991) DNA Cell Biology , vol.10 , pp. 381-388
    • Feller, G.1    Thiry, M.2    Gerday, C.3
  • 29
    • 0032847322 scopus 로고    scopus 로고
    • Homology modeling and active-site residues probing of the thermophilic Alicyclobacillus acidocaldarius esterase 2
    • Manco G., Febbraio F., Adinolfi E., Rossi M. Homology modeling and active-site residues probing of the thermophilic Alicyclobacillus acidocaldarius esterase 2. Protein Science 1999, 8:1789-1796.
    • (1999) Protein Science , vol.8 , pp. 1789-1796
    • Manco, G.1    Febbraio, F.2    Adinolfi, E.3    Rossi, M.4
  • 30
    • 0033958727 scopus 로고    scopus 로고
    • Cloning, overexpression, and properties of a new thermophilic and thermostable esterase with sequence similarity to hormone-sensitive lipase subfamily from the archaeon Archaeoglobus fulgidus
    • Manco G., Giosuè E., D'Auria S., Herman P., Carrea G., Rossi M. Cloning, overexpression, and properties of a new thermophilic and thermostable esterase with sequence similarity to hormone-sensitive lipase subfamily from the archaeon Archaeoglobus fulgidus. Archives Biochemistry Biophysical 2000, 373:182-192.
    • (2000) Archives Biochemistry Biophysical , vol.373 , pp. 182-192
    • Manco, G.1    Giosuè, E.2    D'Auria, S.3    Herman, P.4    Carrea, G.5    Rossi, M.6
  • 31
    • 1842509102 scopus 로고    scopus 로고
    • Psychrophilic enzymes: hot topics in cold adaptation
    • Feller G., Gerday C. Psychrophilic enzymes: hot topics in cold adaptation. Nature Review Microbiology 2003, 1:200-208.
    • (2003) Nature Review Microbiology , vol.1 , pp. 200-208
    • Feller, G.1    Gerday, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.