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Volumn 8, Issue 4, 2013, Pages

Characterization of a Novel Metal-Dependent D-Psicose 3-Epimerase from Clostridium scindens 35704

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; DEXTRO PSICOSE 3 EPIMERASE; FRUCTOSE; MANGANESE; UNCLASSIFIED DRUG; EPIMERASE; METAL; PSICOSE; RECOMBINANT PROTEIN;

EID: 84876964338     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0062987     Document Type: Article
Times cited : (89)

References (26)
  • 1
    • 33750322796 scopus 로고    scopus 로고
    • Psicose contents in various food products and its origin
    • Oshima H, Kimura I, Izumori K, (2006) Psicose contents in various food products and its origin. Food Sci Technol Res 12: 137-143.
    • (2006) Food Sci Technol Res , vol.12 , pp. 137-143
    • Oshima, H.1    Kimura, I.2    Izumori, K.3
  • 2
    • 84867309135 scopus 로고    scopus 로고
    • Recent advances on applications and biotechnological production of D-psicose
    • Mu W, Zhang W, Feng Y, Jiang B, Zhou L, (2012) Recent advances on applications and biotechnological production of D-psicose. Appl Microbiol Biotechnol 94: 1461-1467.
    • (2012) Appl Microbiol Biotechnol , vol.94 , pp. 1461-1467
    • Mu, W.1    Zhang, W.2    Feng, Y.3    Jiang, B.4    Zhou, L.5
  • 3
    • 77950160792 scopus 로고    scopus 로고
    • Study on the postprandial blood glucose suppression effect of D-psicose in borderline diabetes and the safety of long-term ingestion by normal human subjects
    • Hayashi N, Iida T, Yamada T, Okuma K, Takehara I, et al. (2010) Study on the postprandial blood glucose suppression effect of D-psicose in borderline diabetes and the safety of long-term ingestion by normal human subjects. Biosci Biotechnol Biochem 74: 510-519.
    • (2010) Biosci Biotechnol Biochem , vol.74 , pp. 510-519
    • Hayashi, N.1    Iida, T.2    Yamada, T.3    Okuma, K.4    Takehara, I.5
  • 4
    • 64349119105 scopus 로고    scopus 로고
    • Acute D-psicose administration decreases the glycemic responses to an oral maltodextrin tolerance test in normal adults
    • Iida T, Kishimoto Y, Yoshikawa Y, Hayashi N, Okuma K, et al. (2008) Acute D-psicose administration decreases the glycemic responses to an oral maltodextrin tolerance test in normal adults. J Nutr Sci Vitaminol (Tokyo) 54: 511-514.
    • (2008) J Nutr Sci Vitaminol (Tokyo) , vol.54 , pp. 511-514
    • Iida, T.1    Kishimoto, Y.2    Yoshikawa, Y.3    Hayashi, N.4    Okuma, K.5
  • 5
    • 34548459712 scopus 로고    scopus 로고
    • Preventive effect of D-psicose, one of rare ketohexoses, on di-(2-ethylhexyl) phthalate (DEHP)-induced testicular injury in rat
    • Suna S, Yamaguchi F, Kimura S, Tokuda M, Jitsunari F, (2007) Preventive effect of D-psicose, one of rare ketohexoses, on di-(2-ethylhexyl) phthalate (DEHP)-induced testicular injury in rat. Toxicol Lett 173: 107-117.
    • (2007) Toxicol Lett , vol.173 , pp. 107-117
    • Suna, S.1    Yamaguchi, F.2    Kimura, S.3    Tokuda, M.4    Jitsunari, F.5
  • 6
    • 0042420473 scopus 로고    scopus 로고
    • A novel inhibitory effect of D-allose on production of reactive oxygen species from neutrophils
    • Murata A, Sekiya K, Watanabe Y, Yamaguchi F, Hatano N, et al. (2003) A novel inhibitory effect of D-allose on production of reactive oxygen species from neutrophils. J Biosci Bioeng 96: 89-91.
    • (2003) J Biosci Bioeng , vol.96 , pp. 89-91
    • Murata, A.1    Sekiya, K.2    Watanabe, Y.3    Yamaguchi, F.4    Hatano, N.5
  • 7
    • 31844437972 scopus 로고    scopus 로고
    • Neuroprotective effect of D-psicose on 6-hydroxydopamine-induced apoptosis in rat pheochromocytoma (PC12) cells
    • Takata MK, Yamaguchi F, Nakanose K, Watanabe Y, Hatano N, et al. (2005) Neuroprotective effect of D-psicose on 6-hydroxydopamine-induced apoptosis in rat pheochromocytoma (PC12) cells. J Biosci Bioeng 100: 511-516.
    • (2005) J Biosci Bioeng , vol.100 , pp. 511-516
    • Takata, M.K.1    Yamaguchi, F.2    Nakanose, K.3    Watanabe, Y.4    Hatano, N.5
  • 8
    • 30544446584 scopus 로고    scopus 로고
    • Evaluation of the site specific protein glycation and antioxidant capacity of rare sugar-protein/peptide conjugates
    • Sun Y, Hayakawa S, Ogawa M, Izumori K, (2005) Evaluation of the site specific protein glycation and antioxidant capacity of rare sugar-protein/peptide conjugates. J Agric Food Chem 53: 10205-10212.
    • (2005) J Agric Food Chem , vol.53 , pp. 10205-10212
    • Sun, Y.1    Hayakawa, S.2    Ogawa, M.3    Izumori, K.4
  • 9
    • 1542376970 scopus 로고    scopus 로고
    • Modification of ovalbumin with a rare ketohexose through the Maillard reaction: effect on protein structure and gel properties
    • Sun Y, Hayakawa S, Izumori K, (2004) Modification of ovalbumin with a rare ketohexose through the Maillard reaction: effect on protein structure and gel properties. J Agric Food Chem 52: 1293-1299.
    • (2004) J Agric Food Chem , vol.52 , pp. 1293-1299
    • Sun, Y.1    Hayakawa, S.2    Izumori, K.3
  • 10
    • 0005845640 scopus 로고
    • A new enzyme, D-ketohexose 3-epimerase, from Pseudomonas sp. ST-24
    • Izumori K, Khan AR, Okaya H, Tsumura T, (1993) A new enzyme, D-ketohexose 3-epimerase, from Pseudomonas sp. ST-24. Biosci Biotechnol Biochem 57: 1037-1039.
    • (1993) Biosci Biotechnol Biochem , vol.57 , pp. 1037-1039
    • Izumori, K.1    Khan, A.R.2    Okaya, H.3    Tsumura, T.4
  • 11
    • 0028984722 scopus 로고
    • Preparation of D-psicose from D-fructose by immobilized D-tagatose 3-epimerase
    • Itoh H, Sato T, Izumori K, (1995) Preparation of D-psicose from D-fructose by immobilized D-tagatose 3-epimerase. J Ferment Bioeng 80: 101-103.
    • (1995) J Ferment Bioeng , vol.80 , pp. 101-103
    • Itoh, H.1    Sato, T.2    Izumori, K.3
  • 12
    • 0034302040 scopus 로고    scopus 로고
    • Mass production of D-psicose from d-fructose by a continuous bioreactor system using immobilized D-tagatose 3-epimerase
    • Takeshita K, Suga A, Takada G, Izumori K, (2000) Mass production of D-psicose from d-fructose by a continuous bioreactor system using immobilized D-tagatose 3-epimerase. J Biosci Bioeng 90: 453-455.
    • (2000) J Biosci Bioeng , vol.90 , pp. 453-455
    • Takeshita, K.1    Suga, A.2    Takada, G.3    Izumori, K.4
  • 13
    • 33144484509 scopus 로고    scopus 로고
    • Characterization of an Agrobacterium tumefaciens D-psicose 3-epimerase that converts D-fructose to D-psicose
    • Kim HJ, Hyun EK, Kim YS, Lee YJ, Oh DK, (2006) Characterization of an Agrobacterium tumefaciens D-psicose 3-epimerase that converts D-fructose to D-psicose. Appl Environ Microbiol 72: 981-985.
    • (2006) Appl Environ Microbiol , vol.72 , pp. 981-985
    • Kim, H.J.1    Hyun, E.K.2    Kim, Y.S.3    Lee, Y.J.4    Oh, D.K.5
  • 14
    • 67349146995 scopus 로고    scopus 로고
    • Characterization of D-tagatose-3-epimerase from Rhodobacter sphaeroides that converts D-fructose into D-psicose
    • Zhang L, Mu W, Jiang B, Zhang T, (2009) Characterization of D-tagatose-3-epimerase from Rhodobacter sphaeroides that converts D-fructose into D-psicose. Biotechnol Lett 31: 857-862.
    • (2009) Biotechnol Lett , vol.31 , pp. 857-862
    • Zhang, L.1    Mu, W.2    Jiang, B.3    Zhang, T.4
  • 15
    • 79960573514 scopus 로고    scopus 로고
    • Cloning, expression, and characterization of a D-psicose 3-epimerase from Clostridium cellulolyticum H10
    • Mu W, Chu F, Xing Q, Yu S, Zhou L, et al. (2011) Cloning, expression, and characterization of a D-psicose 3-epimerase from Clostridium cellulolyticum H10. J Agric Food Chem 59: 7785-7792.
    • (2011) J Agric Food Chem , vol.59 , pp. 7785-7792
    • Mu, W.1    Chu, F.2    Xing, Q.3    Yu, S.4    Zhou, L.5
  • 16
    • 85027927300 scopus 로고    scopus 로고
    • Overexpression of D-psicose 3-epimerase from Ruminococcus sp. in Escherichia coli and its potential application in D-psicose production
    • Zhu Y, Men Y, Bai W, Li X, Zhang L, et al. (2012) Overexpression of D-psicose 3-epimerase from Ruminococcus sp. in Escherichia coli and its potential application in D-psicose production. Biotechnol Lett 34: 1901-1906.
    • (2012) Biotechnol Lett , vol.34 , pp. 1901-1906
    • Zhu, Y.1    Men, Y.2    Bai, W.3    Li, X.4    Zhang, L.5
  • 17
    • 33746929133 scopus 로고    scopus 로고
    • Crystal structure of D-psicose 3-epimerase from Agrobacterium tumefaciens and its complex with true substrate D-fructose: a pivotal role of metal in catalysis, an active site for the non-phosphorylated substrate, and its conformational changes
    • Kim K, Kim HJ, Oh DK, Cha SS, Rhee S, (2006) Crystal structure of D-psicose 3-epimerase from Agrobacterium tumefaciens and its complex with true substrate D-fructose: a pivotal role of metal in catalysis, an active site for the non-phosphorylated substrate, and its conformational changes. J Mol Biol 361: 920-931.
    • (2006) J Mol Biol , vol.361 , pp. 920-931
    • Kim, K.1    Kim, H.J.2    Oh, D.K.3    Cha, S.S.4    Rhee, S.5
  • 18
    • 35548990636 scopus 로고    scopus 로고
    • Crystal structures of D-tagatose 3-epimerase from Pseudomonas cichorii and its complexes with D-tagatose and D-fructose
    • Yoshida H, Yamada M, Nishitani T, Takada G, Izumori K, et al. (2007) Crystal structures of D-tagatose 3-epimerase from Pseudomonas cichorii and its complexes with D-tagatose and D-fructose. J Mol Biol 374: 443-453.
    • (2007) J Mol Biol , vol.374 , pp. 443-453
    • Yoshida, H.1    Yamada, M.2    Nishitani, T.3    Takada, G.4    Izumori, K.5
  • 19
    • 84862855717 scopus 로고    scopus 로고
    • Crystal structures of D-psicose 3-epimerase from Clostridium cellulolyticum H10 and its complex with ketohexose sugars
    • Chan HC, Zhu Y, Hu Y, Ko TP, Huang CH, et al. (2012) Crystal structures of D-psicose 3-epimerase from Clostridium cellulolyticum H10 and its complex with ketohexose sugars. Protein Cell 3: 123-131.
    • (2012) Protein Cell , vol.3 , pp. 123-131
    • Chan, H.C.1    Zhu, Y.2    Hu, Y.3    Ko, T.P.4    Huang, C.H.5
  • 20
    • 0028253982 scopus 로고
    • Purification and characterization of D-tagatose 3-epimerase from Pseudomonas sp. ST-24
    • Itoh H, Okaya H, Khan AR, Tajima S, Hayakawa S, et al. (1994) Purification and characterization of D-tagatose 3-epimerase from Pseudomonas sp. ST-24. Biosci Biotechnol Biochem 58: 2168-2171.
    • (1994) Biosci Biotechnol Biochem , vol.58 , pp. 2168-2171
    • Itoh, H.1    Okaya, H.2    Khan, A.R.3    Tajima, S.4    Hayakawa, S.5
  • 21
    • 0030749853 scopus 로고    scopus 로고
    • Cloning and characterization of the D-tagatose 3-epimerase gene from Pseudomonas cichorii ST-24
    • Ishida Y, Kamiya T, Itoh H, Kimura Y, Izumori K, (1997) Cloning and characterization of the D-tagatose 3-epimerase gene from Pseudomonas cichorii ST-24. J Ferment Bioeng 83: 529-534.
    • (1997) J Ferment Bioeng , vol.83 , pp. 529-534
    • Ishida, Y.1    Kamiya, T.2    Itoh, H.3    Kimura, Y.4    Izumori, K.5
  • 22
    • 82955240007 scopus 로고    scopus 로고
    • Improvement in the thermostability of D-psicose 3-epimerase from Agrobacterium tumefaciens by random and site-directed mutagenesis
    • Choi JG, Ju YH, Yeom SJ, Oh DK, (2011) Improvement in the thermostability of D-psicose 3-epimerase from Agrobacterium tumefaciens by random and site-directed mutagenesis. Appl Environ Microbiol 77: 7316-7320.
    • (2011) Appl Environ Microbiol , vol.77 , pp. 7316-7320
    • Choi, J.G.1    Ju, Y.H.2    Yeom, S.J.3    Oh, D.K.4
  • 23
    • 11444258321 scopus 로고    scopus 로고
    • Distinct metal dependence for catalytic and structural functions in the l-arabinose isomerases from the mesophilic Bacillus halodurans and the thermophilic Geobacillus stearothermophilus
    • Lee DW, Choe EA, Kim SB, Eom SH, Hong YH, et al. (2005) Distinct metal dependence for catalytic and structural functions in the l-arabinose isomerases from the mesophilic Bacillus halodurans and the thermophilic Geobacillus stearothermophilus. Arch Biochem Biophys 434: 333-343.
    • (2005) Arch Biochem Biophys , vol.434 , pp. 333-343
    • Lee, D.W.1    Choe, E.A.2    Kim, S.B.3    Eom, S.H.4    Hong, Y.H.5
  • 24
    • 78049306697 scopus 로고    scopus 로고
    • Characterization of a thermophilic L-rhamnose isomerase from Thermoanaerobacterium saccharolyticum NTOU1
    • Lin CJ, Tseng WC, Lin TH, Liu SM, Tzou WS, et al. (2010) Characterization of a thermophilic L-rhamnose isomerase from Thermoanaerobacterium saccharolyticum NTOU1. J Agric Food Chem 58: 10431-10436.
    • (2010) J Agric Food Chem , vol.58 , pp. 10431-10436
    • Lin, C.J.1    Tseng, W.C.2    Lin, T.H.3    Liu, S.M.4    Tzou, W.S.5
  • 25
    • 33644629689 scopus 로고    scopus 로고
    • Cloning, purification and biochemical characterization of metallic-ions independent and thermoactive l-arabinose isomerase from the Bacillus stearothermophilus US100 strain
    • Rhimi M, Bejar S, (2006) Cloning, purification and biochemical characterization of metallic-ions independent and thermoactive l-arabinose isomerase from the Bacillus stearothermophilus US100 strain. Biochim Biophys Acta 1760: 191-199.
    • (2006) Biochim Biophys Acta , vol.1760 , pp. 191-199
    • Rhimi, M.1    Bejar, S.2
  • 26
    • 34547615898 scopus 로고    scopus 로고
    • Characterization of ribose-5-phosphate isomerase of Clostridium thermocellum producing D-allose from D-psicose
    • Park CS, Yeom SJ, Kim HJ, Lee SH, Lee JK, et al. (2007) Characterization of ribose-5-phosphate isomerase of Clostridium thermocellum producing D-allose from D-psicose. Biotechnol Lett 29: 1387-1391.
    • (2007) Biotechnol Lett , vol.29 , pp. 1387-1391
    • Park, C.S.1    Yeom, S.J.2    Kim, H.J.3    Lee, S.H.4    Lee, J.K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.