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Volumn 75, Issue 18, 2009, Pages 5871-5883

Anaerobic fermentation of glycerol in Paenibacillus macerans: Metabolic pathways and environmental determinants

Author keywords

[No Author keywords available]

Indexed keywords

ACIDIC PH; ANAEROBIC FERMENTATION; CELLULAR COMPONENTS; DEGREE OF REDUCTION; ENERGY REQUIREMENTS; ENVIRONMENTAL DETERMINANTS; ENZYME ASSAYS; EXTRACELLULAR METABOLITES; FERMENTATION PRODUCTS; GLYCEROL FERMENTATION; LOW CONCENTRATIONS; MAXIMUM SPECIFIC GROWTH RATES; METABOLIC CAPABILITIES; METABOLIC PATHWAYS; METABOLIC RATES; NMR SPECTROSCOPY; PAENIBACILLUS MACERANS; PROPANEDIOLS; PROTEINOGENIC AMINO ACIDS; REDOX BALANCES;

EID: 70149098733     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.01246-09     Document Type: Article
Times cited : (41)

References (44)
  • 1
    • 0032984973 scopus 로고    scopus 로고
    • Metabolic engineering of a 1,2-propanediol pathway in Escherichia coli
    • Altaras, N. E., and D. C. Cameron. 1999. Metabolic engineering of a 1,2-propanediol pathway in Escherichia coli. Appl. Environ. Microbiol. 65:1180-1185.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 1180-1185
    • Altaras, N.E.1    Cameron, D.C.2
  • 2
    • 0001134202 scopus 로고
    • Requirements for transformation in Bacillus subtilis
    • Anagnostopoulos, C., and J. Spizizen. 1961. Requirements for transformation in Bacillus subtilis. J. Bacteriol. 81:741-746.
    • (1961) J. Bacteriol. , vol.81 , pp. 741-746
    • Anagnostopoulos, C.1    Spizizen, J.2
  • 3
    • 0030738343 scopus 로고    scopus 로고
    • Anaerobic pathways of glycerol dissimilation by Enterobacter agglomerans CNCM 1210: Limitations and regulations
    • Barbirato, F., S. Astruc, P. Soucaille, C. Camarasa, J. M. Salmon, and A. Bories. 1997. Anaerobic pathways of glycerol dissimilation by Enterobacter agglomerans CNCM 1210: limitations and regulations. Microbiology 143:2423-2432.
    • (1997) Microbiology , vol.143 , pp. 2423-2432
    • Barbirato, F.1    Astruc, S.2    Soucaille, P.3    Camarasa, C.4    Salmon, J.M.5    Bories, A.6
  • 4
    • 0003030519 scopus 로고
    • A simple method for the calibration of the decoupler radiofrequency field-strength
    • Bax, A. 1983. A simple method for the calibration of the decoupler radiofrequency field-strength. J. Magn. Res. 52:76-80.
    • (1983) J. Magn. Res. , vol.52 , pp. 76-80
    • Bax, A.1
  • 5
    • 0037258569 scopus 로고    scopus 로고
    • The effect of carbon sources and lactate dehydrogenase deletion on 1,2-propanediol production in Escherichia coli
    • Berrios-Rivera, S. J., K. Y. San, and G. N. Bennett. 2003. The effect of carbon sources and lactate dehydrogenase deletion on 1,2-propanediol production in Escherichia coli. J. Ind. Microbiol. Biotechnol. 30:34-40. (Pubitemid 36169615)
    • (2003) Journal of Industrial Microbiology and Biotechnology , vol.30 , Issue.1 , pp. 34-40
    • Berrios-Rivera, S.J.1    San, K.-Y.2    Bennett, G.N.3
  • 6
    • 33746867314 scopus 로고    scopus 로고
    • Glycerol and methylglyoxal metabolism
    • March posting date. Chapter 3.4.3, R. Curtis III et al. (ed.), ASM Press, Washington, DC
    • Booth, I. R. March 2005, posting date. Chapter 3.4.3, Glycerol and methylglyoxal metabolism. In R. Curtis III et al. (ed.), EcoSal - Escherichia coli and Salmonella: cellular and molecular biology. ASM Press, Washington, DC. http://www.ecosal.org/.
    • (2005) EcoSal - Escherichia Coli and Salmonella: Cellular and Molecular Biology
    • Booth, I.R.1
  • 7
    • 0035956936 scopus 로고    scopus 로고
    • Reconstitution and functional comparison of purified GlpF and AqpZ, the glycerol and water channels from Escherichia coli
    • Borgnia, M. J., and P. Agre. 2001. Reconstitution and functional comparison of purified GlpF and AqpZ, the glycerol and water channels from Escherichia coli. Proc. Natl. Acad. Sci. USA 98:2888-2893.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 2888-2893
    • Borgnia, M.J.1    Agre, P.2
  • 8
    • 0018566823 scopus 로고
    • Rhamnose-induced propanediol oxidoreductase in Escherichia coli: Purification, properties, and comparison with the fucose-induced enzyme
    • Boronat, A., and J. Aguilar. 1979. Rhamnose-induced propanediol oxidoreductase in Escherichia coli: purification, properties, and comparison with the fucose-induced enzyme. J. Bacteriol. 140:320-326.
    • (1979) J. Bacteriol. , vol.140 , pp. 320-326
    • Boronat, A.1    Aguilar, J.2
  • 9
    • 0029014958 scopus 로고
    • Taxonomic diversity of anaerobic glycerol dissimilation in the Enterobacteriaceae
    • Bouvet, O. M. M., P. Lenormand, E. Ageron, and P. A. D. Grimont. 1995. Taxonomic diversity of anaerobic glycerol dissimilation in the Enterobacteriaceae. Res. Microbiol. 146:279-290.
    • (1995) Res. Microbiol. , vol.146 , pp. 279-290
    • Bouvet, O.M.M.1    Lenormand, P.2    Ageron, E.3    Grimont, P.A.D.4
  • 10
    • 0028268929 scopus 로고
    • Phenotypic diversity of anaerobic glycerol dissimilation shown by 7 enterobacterial species
    • Bouvet, O. M. M., P. Lenormand, J. P. Carlier, and P. A. D. Grimont. 1994. Phenotypic diversity of anaerobic glycerol dissimilation shown by 7 enterobacterial species. Res. Microbiol. 145:129-139.
    • (1994) Res. Microbiol. , vol.145 , pp. 129-139
    • Bouvet, O.M.M.1    Lenormand, P.2    Carlier, J.P.3    Grimont, P.A.D.4
  • 11
    • 0032537479 scopus 로고    scopus 로고
    • Structure and properties of pyruvate decarboxylase and site-directed mutagenesis of the Zymomonas mobilis enzyme
    • Candy, J. M., and R. G. Duggleby. 1998. Structure and properties of pyruvate decarboxylase and site-directed mutagenesis of the Zymomonas mobilis enzyme. Biochim. Biophys. Acta 1385:323-338.
    • (1998) Biochim. Biophys. Acta , vol.1385 , pp. 323-338
    • Candy, J.M.1    Duggleby, R.G.2
  • 12
    • 0021195497 scopus 로고
    • Metabolism of methylglyoxal in microorganisms
    • Cooper, R. A. 1984. Metabolism of methylglyoxal in microorganisms. Annu. Rev. Microbiol. 38:49-68.
    • (1984) Annu. Rev. Microbiol. , vol.38 , pp. 49-68
    • Cooper, R.A.1
  • 13
    • 33746868000 scopus 로고    scopus 로고
    • Anaerobic fermentation of glycerol by Escherichia coli: A new platform for metabolic engineering
    • Dharmadi, Y., A. Murarka, and R. Gonzalez. 2006. Anaerobic fermentation of glycerol by Escherichia coli: a new platform for metabolic engineering. Biotechnol. Bioeng. 94:821-829.
    • (2006) Biotechnol. Bioeng. , vol.94 , pp. 821-829
    • Dharmadi, Y.1    Murarka, A.2    Gonzalez, R.3
  • 14
    • 15744400448 scopus 로고    scopus 로고
    • A better global resolution function and a novel iterative stochastic search method for optimization of high-performance liquid chromatographic separation
    • DOI 10.1016/j.chroma.2005.02.075, PII S0021967305003262
    • Dharmadi, Y., and R. Gonzalez. 2005. A better global resolution function and a novel iterative stochastic search method for optimization of high-performance liquid chromatographic separation. J. Chromatogr. A 1070:89-101. (Pubitemid 40417771)
    • (2005) Journal of Chromatography a , vol.1070 , Issue.1-2 , pp. 89-101
    • Dharmadi, Y.1    Gonzalez, R.2
  • 15
    • 50249129588 scopus 로고    scopus 로고
    • A new model for the anaerobic fermentation of glycerol in enteric bacteria: Trunk and auxiliary pathways in Escherichia coli
    • Gonzalez, R., A. Murarka, Y. Dharmadi, and S. S. Yazdani. 2008. A new model for the anaerobic fermentation of glycerol in enteric bacteria: trunk and auxiliary pathways in Escherichia coli. Metab. Eng. 10:234-245.
    • (2008) Metab. Eng. , vol.10 , pp. 234-245
    • Gonzalez, R.1    Murarka, A.2    Dharmadi, Y.3    Yazdani, S.S.4
  • 16
    • 0014197885 scopus 로고
    • Purification and properties of glycerol kinase from Escherichia coli
    • Hayashi, S., and E. C. C. Lin. 1967. Purification and properties of glycerol kinase from Escherichia coli. J. Biol. Chem. 242:1030-1035.
    • (1967) J. Biol. Chem. , vol.242 , pp. 1030-1035
    • Hayashi, S.1    Lin, E.C.C.2
  • 17
    • 0029818079 scopus 로고    scopus 로고
    • A polyphasic reassessment of the genus Paenibacillus, reclassification of Bacillus lautus (Nakamura 1984) as Paenibacillus lautus comb. nov. and of Bacillus peoriae (Montefusco et al. 1993.) as Paenibacillus peoriae comb. nov., and emended descriptions of P. lautus and of P. peoriae
    • Heyndrickx, M., K. Vandemeulebroecke, P. Scheldeman, K. Kersters, P. DeVos, N. A. Logan, A. M. Aziz, N. Ali, and R. C. W. Berkeley. 1996. A polyphasic reassessment of the genus Paenibacillus, reclassification of Bacillus lautus (Nakamura 1984) as Paenibacillus lautus comb. nov. and of Bacillus peoriae (Montefusco et al. 1993.) as Paenibacillus peoriae comb. nov., and emended descriptions of P. lautus and of P. peoriae. Int. J. Syst. Evol. Microbiol. 46:988-1003.
    • (1996) Int. J. Syst. Evol. Microbiol. , vol.46 , pp. 988-1003
    • Heyndrickx, M.1    Vandemeulebroecke, K.2    Scheldeman, P.3    Kersters, K.4    DeVos, P.5    Logan, N.A.6    Aziz, A.M.7    Ali, N.8    Berkeley, R.C.W.9
  • 18
    • 0001515246 scopus 로고
    • Regulation of Escherichia coli methylglyoxal synthase: New control site in glycolysis?
    • Hopper, D. J., and R. A. Cooper. 1971. Regulation of Escherichia coli methylglyoxal synthase: new control site in glycolysis? FEBS Lett. 13:213-216.
    • (1971) FEBS Lett. , vol.13 , pp. 213-216
    • Hopper, D.J.1    Cooper, R.A.2
  • 20
    • 0025972739 scopus 로고
    • Pyruvate-formate-lyase-deactivase and acetyl-CoA reductase activities of Escherichia coli reside on a polymeric protein particle encoded by adhE
    • Kessler, D., I. Leibrecht, and J. Knappe. 1991. Pyruvate-formate-lyase- deactivase and acetyl-CoA reductase activities of Escherichia coli reside on a polymeric protein particle encoded by adhE. FEBS Lett. 281:59-63.
    • (1991) FEBS Lett. , vol.281 , pp. 59-63
    • Kessler, D.1    Leibrecht, I.2    Knappe, J.3
  • 21
    • 0015413830 scopus 로고
    • Purification and properties of the flavine-stimulated anaerobic l-α-glycerophosphate dehydrogenase of Escherichia coli
    • Kistler, W. S., and E. C. C. Lin. 1972. Purification and properties of the flavine-stimulated anaerobic l-α-glycerophosphate dehydrogenase of Escherichia coli. J. Bacteriol. 112:539-547.
    • (1972) J. Bacteriol. , vol.112 , pp. 539-547
    • Kistler, W.S.1    Lin, E.C.C.2
  • 22
    • 23644445048 scopus 로고    scopus 로고
    • Conversion of methylglyoxal to acetol by Escherichia coli aldo-keto reductases
    • Ko, J., I. Kim, S. Yoo, B. Min, K. Kim, and C. Park. 2005. Conversion of methylglyoxal to acetol by Escherichia coli aldo-keto reductases. J. Bacteriol. 187:5782-5789.
    • (2005) J. Bacteriol. , vol.187 , pp. 5782-5789
    • Ko, J.1    Kim, I.2    Yoo, S.3    Min, B.4    Kim, K.5    Park, C.6
  • 23
    • 0015377479 scopus 로고
    • Inducible phosphoenolpyruvate-dependent hexose phosphotransferase activities in Escherichia coli
    • Kornberg, H. L., and R. E. Reeves. 1972. Inducible phosphoenolpyruvate- dependent hexose phosphotransferase activities in Escherichia coli. Biochem. J. 128:1339-1344.
    • (1972) Biochem. J. , vol.128 , pp. 1339-1344
    • Kornberg, H.L.1    Reeves, R.E.2
  • 24
    • 0017243175 scopus 로고
    • Glycerol dissimilation and its regulation in bacteria
    • Lin, E. C. C. 1976. Glycerol dissimilation and its regulation in bacteria. Annu. Rev. Microbiol. 30:535-578.
    • (1976) Annu. Rev. Microbiol. , vol.30 , pp. 535-578
    • Lin, E.C.C.1
  • 25
    • 0029872670 scopus 로고    scopus 로고
    • Reduction of methylglyoxal in Escherichia coli K12 by an aldehyde reductase and alcohol dehydrogenase
    • Misra, K., A. B. Banerjee, S. Ray, and M. Ray. 1996. Reduction of methylglyoxal in Escherichia coli K12 by an aldehyde reductase and alcohol dehydrogenase. Mol. Cell. Biochem. 156:117-124.
    • (1996) Mol. Cell. Biochem. , vol.156 , pp. 117-124
    • Misra, K.1    Banerjee, A.B.2    Ray, S.3    Ray, M.4
  • 26
    • 39649103644 scopus 로고    scopus 로고
    • Fermentative utilization of glycerol by Escherichia coli and its implications for the production of fuels and chemicals
    • Murarka, A., Y. Dharmadi, S. S. Yazdani, and R. Gonzalez. 2008. Fermentative utilization of glycerol by Escherichia coli and its implications for the production of fuels and chemicals. Appl. Environ. Microbiol. 74:1124-1135.
    • (2008) Appl. Environ. Microbiol. , vol.74 , pp. 1124-1135
    • Murarka, A.1    Dharmadi, Y.2    Yazdani, S.S.3    Gonzalez, R.4
  • 27
    • 0030700663 scopus 로고    scopus 로고
    • Characterization of anaerobic fermentative growth of Bacillus subtilis: Identification of fermentation end products and genes required for growth
    • Nakano, M. M., Y. P. Dailly, P. Zuber, and D. P. Clark. 1997. Characterization of anaerobic fermentative growth of Bacillus subtilis: identification of fermentation end products and genes required for growth. J. Bacteriol. 179:6749-6755.
    • (1997) J. Bacteriol. , vol.179 , pp. 6749-6755
    • Nakano, M.M.1    Dailly, Y.P.2    Zuber, P.3    Clark, D.P.4
  • 29
    • 0025166757 scopus 로고
    • Nucleotide regulation of Escherichia coli glycerol kinase: Initial-velocity and substrate binding studies
    • Pettigrew, D. W., G. J. Yu, and Y. G. Liu. 1990. Nucleotide regulation of Escherichia coli glycerol kinase: initial-velocity and substrate binding studies. Biochemistry 29:8620-8627.
    • (1990) Biochemistry , vol.29 , pp. 8620-8627
    • Pettigrew, D.W.1    Yu, G.J.2    Liu, Y.G.3
  • 30
    • 0006554367 scopus 로고
    • Metabolism of 2-oxoaldehydes in bacteria: Purification and characterization of methylglyoxal reductase from Escherichia coli
    • Saikusa, T., H. Rhee, K. Watanabe, K. Murata, and A. Kimura. 1987. Metabolism of 2-oxoaldehydes in bacteria: purification and characterization of methylglyoxal reductase from Escherichia coli. Biosci. Biotechnol. Biochem. 51:1893-1899.
    • (1987) Biosci. Biotechnol. Biochem. , vol.51 , pp. 1893-1899
    • Saikusa, T.1    Rhee, H.2    Watanabe, K.3    Murata, K.4    Kimura, A.5
  • 31
    • 33747123465 scopus 로고    scopus 로고
    • Fermentative pyruvate and acetyl-coenzyme A metabolism
    • July posting date. Chapter 3.5.3, R. Curtiss III et al. (ed.), ASM Press, Washington, DC
    • Sawers, R. G., and D. P. Clark. July 2004, posting date. Chapter 3.5.3, Fermentative pyruvate and acetyl-coenzyme A metabolism. In R. Curtiss III et al. (ed.), EcoSal - Escherichia coli and Salmonella: cellular and molecular biology. ASM Press, Washington, DC. http://www.ecosal.org/.
    • (2004) EcoSal - Escherichia Coli and Salmonella: Cellular and Molecular Biology
    • Sawers, R.G.1    Clark, D.P.2
  • 32
    • 70149124825 scopus 로고    scopus 로고
    • Anaerobic formate and hydrogen metabolism
    • September posting date. Chapter 3.5.4, R. Curtiss III et al. (ed.), ASM Press, Washington, DC
    • Sawers, R. G., M. Blokesch, and A. Bock. September 2004, posting date. Chapter 3.5.4, Anaerobic formate and hydrogen metabolism. In R. Curtiss III et al. (ed.), EcoSal - Escherichia coli and Salmonella: cellular and molecular biology. ASM Press, Washington, DC. http://www.ecosal.org/.
    • (2004) EcoSal - Escherichia Coli and Salmonella: Cellular and Molecular Biology
    • Sawers, R.G.1    Blokesch, M.2    Bock, A.3
  • 33
    • 0342802270 scopus 로고
    • Fermentation of D-xylose to ethanol by Bacillus macerans
    • Schepers, H. J., S. Bringermeyer, and H. Sahm. 1987. Fermentation of D-xylose to ethanol by Bacillus macerans. Z. Naturforsch. 42c:401-407.
    • (1987) Z. Naturforsch. , vol.42 C , pp. 401-407
    • Schepers, H.J.1    Bringermeyer, S.2    Sahm, H.3
  • 34
    • 0028913541 scopus 로고
    • Anaerobic respiration of Bacillus macerans with fumarate, TMAO, nitrate and nitrite and regulation of the pathways by oxygen and nitrate
    • Schirawski, J., and G. Unden. 1995. Anaerobic respiration of Bacillus macerans with fumarate, TMAO, nitrate and nitrite and regulation of the pathways by oxygen and nitrate. Arch. Microbiol. 163:148-154.
    • (1995) Arch. Microbiol. , vol.163 , pp. 148-154
    • Schirawski, J.1    Unden, G.2
  • 35
    • 0020085934 scopus 로고
    • The anaerobic sn-glycerol-3-phosphate dehydrogenase: Cloning and expression of the glpA gene of Escherichia coli and identification of the glpA products
    • Schryvers, A., and J. H. Weiner. 1982. The anaerobic sn-glycerol-3- phosphate dehydrogenase: cloning and expression of the glpA gene of Escherichia coli and identification of the glpA products. Can. J. Biochem. 60:224-231.
    • (1982) Can. J. Biochem. , vol.60 , pp. 224-231
    • Schryvers, A.1    Weiner, J.H.2
  • 36
    • 0019785065 scopus 로고
    • Steady-state and pre-steady-state kinetics of coenzyme A-linked aldehyde dehydrogenase from Escherichia coli
    • Shone, C. C., and H. J. Fromm. 1981. Steady-state and pre-steady-state kinetics of coenzyme A-linked aldehyde dehydrogenase from Escherichia coli. Biochemistry 20:7494-7501.
    • (1981) Biochemistry , vol.20 , pp. 7494-7501
    • Shone, C.C.1    Fromm, H.J.2
  • 37
    • 0028348666 scopus 로고
    • Mapping and cloning of gldA, the structural gene of the Escherichia coli glycerol dehydrogenase
    • Truniger, V., and W. Boos. 1994. Mapping and cloning of gldA, the structural gene of the Escherichia coli glycerol dehydrogenase. J. Bacteriol. 176:1796-1800.
    • (1994) J. Bacteriol. , vol.176 , pp. 1796-1800
    • Truniger, V.1    Boos, W.2
  • 38
    • 0037101782 scopus 로고    scopus 로고
    • Aerobic sn-glycerol-3-phosphate dehydrogenase from Escherichia coli binds to the cytoplasmic membrane through an amphipathic α-helix
    • Walz, A. C., R. A. Demel, B. de Kruijff, and R. Mutzel. 2002. Aerobic sn-glycerol-3-phosphate dehydrogenase from Escherichia coli binds to the cytoplasmic membrane through an amphipathic α-helix. Biochem. J. 365:471-479.
    • (2002) Biochem. J. , vol.365 , pp. 471-479
    • Walz, A.C.1    Demel, R.A.2    De Kruijff, B.3    Mutzel, R.4
  • 39
    • 0021326948 scopus 로고
    • Control of product formation during glucose fermentation by Bacillus macerans
    • Weimer, P. J. 1984. Control of product formation during glucose fermentation by Bacillus macerans. J. Gen. Microbiol. 130:103-111.
    • (1984) J. Gen. Microbiol. , vol.130 , pp. 103-111
    • Weimer, P.J.1
  • 40
    • 0021328542 scopus 로고
    • Fermentation of 6-deoxyhexoses by Bacillus macerans
    • Weimer, P. J. 1984. Fermentation of 6-deoxyhexoses by Bacillus macerans. Appl. Environ. Microbiol. 47:263-267.
    • (1984) Appl. Environ. Microbiol. , vol.47 , pp. 263-267
    • Weimer, P.J.1
  • 41
    • 0022261925 scopus 로고
    • The production of hemicellulose-degrading enzymes by Bacillus macerans in anaerobic culture
    • Williams, A. G., and S. E. Withers. 1985. The production of hemicellulose-degrading enzymes by Bacillus macerans in anaerobic culture. Appl. Microbiol. Biotechnol. 22:318-324.
    • (1985) Appl. Microbiol. Biotechnol. , vol.22 , pp. 318-324
    • Williams, A.G.1    Withers, S.E.2
  • 42
    • 34249936957 scopus 로고    scopus 로고
    • Anaerobic fermentation of glycerol: A path to economic viability for the biofuels industry
    • Yazdani, S. S., and R. Gonzalez. 2007. Anaerobic fermentation of glycerol: a path to economic viability for the biofuels industry. Curr. Opin. Biotechnol. 18:213-219.
    • (2007) Curr. Opin. Biotechnol. , vol.18 , pp. 213-219
    • Yazdani, S.S.1    Gonzalez, R.2
  • 43
    • 57049188930 scopus 로고    scopus 로고
    • Engineering Escherichia coli for the efficient conversion of glycerol to ethanol and co-products
    • Yazdani, S. S., and R. Gonzalez. 2008. Engineering Escherichia coli for the efficient conversion of glycerol to ethanol and co-products. Metab. Eng. 10:340-351.
    • (2008) Metab. Eng. , vol.10 , pp. 340-351
    • Yazdani, S.S.1    Gonzalez, R.2
  • 44
    • 0034878313 scopus 로고    scopus 로고
    • Accumulation of methylglyoxal in anaerobically grown Escherichia coli and its detoxification by expression of the Pseudomonas putida glyoxalase I gene
    • Zhu, M. M., F. A. Skraly, and D. C. Cameron. 2001. Accumulation of methylglyoxal in anaerobically grown Escherichia coli and its detoxification by expression of the Pseudomonas putida glyoxalase I gene. Metab. Eng. 3:218-225.
    • (2001) Metab. Eng. , vol.3 , pp. 218-225
    • Zhu, M.M.1    Skraly, F.A.2    Cameron, D.C.3


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