메뉴 건너뛰기




Volumn 287, Issue 21, 2012, Pages 17662-17671

Characterization of a novel Agrobacterium tumefaciens galactarolactone cycloisomerase enzyme for direct conversion of D-galactarolactone to 3-deoxy-2-keto-L-threo-hexarate

Author keywords

[No Author keywords available]

Indexed keywords

AGROBACTERIUM TUMEFACIENS; AGROBACTERIUM TUMEFACIENS STRAIN; DIRECT CONVERSION; ENOLASE; KETOGLUTARATE; MANDELATE RACEMASE; OXIDATIVE PATHWAYS; PURIFIED ENZYME; REACTION MECHANISM; TUMEFACIENS;

EID: 84861209586     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.335240     Document Type: Article
Times cited : (29)

References (23)
  • 1
    • 61449166642 scopus 로고    scopus 로고
    • D-Galacturonic acid catabolism in microorganisms and its biotechnological relevance
    • Richard, P., and Hilditch, S. (2009) D-Galacturonic acid catabolism in microorganisms and its biotechnological relevance. Appl. Microbiol. Biotechnol. 82, 597-604
    • (2009) Appl. Microbiol. Biotechnol. , vol.82 , pp. 597-604
    • Richard, P.1    Hilditch, S.2
  • 2
    • 36949067313 scopus 로고
    • Uronate oxidation by phytopathogenic pseudomonads
    • Kilgore, W. W., and Starr, M. P. (1959) Uronate oxidation by phytopathogenic pseudomonads. Nature 183, 1412-1413
    • (1959) Nature , vol.183 , pp. 1412-1413
    • Kilgore, W.W.1    Starr, M.P.2
  • 3
    • 61449189947 scopus 로고
    • Hexuronic dehydrogenase of Agrobacterium tumefaciens
    • Zajic, J. E. (1959) Hexuronic dehydrogenase of Agrobacterium tumefaciens. J. Bacteriol. 78, 734-735
    • (1959) J. Bacteriol. , vol.78 , pp. 734-735
    • Zajic, J.E.1
  • 4
    • 0014570787 scopus 로고
    • Hexuronic acid dehydrogenase of Agrobacterium tumefaciens
    • Chang, Y. F, and Feingold, D. S. (1969) Hexuronic acid dehydrogenase of Agrobacterium tumefaciens. J. Bacteriol. 99, 667-673
    • (1969) J. Bacteriol. , vol.99 , pp. 667-673
    • Chang, Y.F.1    Feingold, D.S.2
  • 5
    • 0014766559 scopus 로고
    • D-Glucaric acid and galactaric acid catabolism by Agrobacterium tumefaciens
    • Chang, Y. F, and Feingold, D. S. (1970) D-Glucaric acid and galactaric acid catabolism by Agrobacterium tumefaciens. J. Bacteriol. 102, 85-96
    • (1970) J. Bacteriol. , vol.102 , pp. 85-96
    • Chang, Y.F.1    Feingold, D.S.2
  • 6
    • 0014634643 scopus 로고
    • Purification and properties of D-4-deoxy-5-oxoglucarate hydro-lyase (decarboxylating)
    • Jeffcoat, R., Hassall, H., and Dagley, S. (1969) Purification and properties of D-4-deoxy-5-oxoglucarate hydro-lyase (decarboxylating). Biochem. J. 115, 977-983
    • (1969) Biochem. J. , vol.115 , pp. 977-983
    • Jeffcoat, R.1    Hassall, H.2    Dagley, S.3
  • 7
    • 77950629780 scopus 로고    scopus 로고
    • Identification in Agrobacterium tumefaciens of the D-galacturonic acid dehydrogenase gene
    • Boer, H., Maaheimo, H., Koivula, A., Penttilä, M., and Richard, P. (2010) Identification in Agrobacterium tumefaciens of the D-galacturonic acid dehydrogenase gene. Appl. Microbiol. Biotechnol. 86, 901-909
    • (2010) Appl. Microbiol. Biotechnol. , vol.86 , pp. 901-909
    • Boer, H.1    Maaheimo, H.2    Koivula, A.3    Penttilä, M.4    Richard, P.5
  • 9
    • 9744279773 scopus 로고    scopus 로고
    • Divergent evolution in the enolase superfamily: The interplay of mechanism and specificity
    • DOI 10.1016/j.abb.2004.07.034, PII S0003986104004059
    • Gerlt, J. A., Babbitt, P. C., and Rayment, I. (2005) Divergent evolution in the enolase superfamily: the interplay of mechanism and specificity. Arch. Biochem. Biophys. 433, 59-70 (Pubitemid 39586583)
    • (2005) Archives of Biochemistry and Biophysics , vol.433 , Issue.1 , pp. 59-70
    • Gerlt, J.A.1    Babbitt, P.C.2    Rayment, I.3
  • 10
    • 0032514651 scopus 로고    scopus 로고
    • Evolution of enzymatic activities in the enolase superfamily: Characterization of the (D)-glucarate/galactarate catabolic pathway in Escherichia coli
    • DOI 10.1021/bi981124f
    • Hubbard, B. K., Koch, M., Palmer, D. R., Babbitt, P. C., and Gerlt, J. A. (1998) Evolution of enzymatic activities in the enolase superfamily: characterization of the (D)-glucarate/galactarate catabolic pathway in Escherichia coli. Biochemistry 37, 14369-14375 (Pubitemid 28489042)
    • (1998) Biochemistry , vol.37 , Issue.41 , pp. 14369-14375
    • Hubbard, B.K.1    Koch, M.2    Palmer, D.R.J.3    Babbitt, P.C.4    Gerlt, J.A.5
  • 11
    • 0033229936 scopus 로고    scopus 로고
    • An extremely thermostable aldolase from Sulfolobus solfataricus with specificity for non-phosphorylated substrates
    • DOI 10.1042/0264-6021:3430563
    • Buchanan, C. L., Connaris, H., Danson, M. J., Reeve, C. D., and Hough, D. W. (1999) An extremely thermostable aldolase from Sulfolobus solfataricus with specificity for non-phosphorylated substrates. Biochem. J. 343, 563-570 (Pubitemid 29537367)
    • (1999) Biochemical Journal , vol.343 , Issue.3 , pp. 563-570
    • Buchanan, C.L.1    Connaris, H.2    Danson, M.J.3    Reeve, C.D.4    Hough, D.W.5
  • 12
    • 0005349244 scopus 로고
    • Anew phosphorylated intermediate in glucose oxidation
    • MacGee, J., and Doudoroff, M. (1954)Anew phosphorylated intermediate in glucose oxidation. J. Biol. Chem. 210, 617-626
    • (1954) J. Biol. Chem. , vol.210 , pp. 617-626
    • MacGee, J.1    Doudoroff, M.2
  • 13
    • 0029983371 scopus 로고    scopus 로고
    • T7 vectors with modified T7lac promoter for expression of proteins in Escherichia coli
    • Peränen, J., Rikkonen, M., Hyvönen, M., and Kääriäinen, L. (1996) T7 vectors with modified T7lac promoter for expression of proteins in Escherichia coli. Anal. Biochem. 236, 371-373
    • (1996) Anal. Biochem. , vol.236 , pp. 371-373
    • Peränen, J.1    Rikkonen, M.2    Hyvönen, M.3    Kääriäinen, L.4
  • 14
    • 84873799110 scopus 로고
    • Studies on lysogenesis. I. The mode of phage liberation by lysogenic Escherichia coli
    • Bertani, G., and Nice, S. J. (1951) Studies on lysogenesis. I. The mode of phage liberation by lysogenic Escherichia coli. J. Bacteriol. 62, 293-300
    • (1951) J. Bacteriol. , vol.62 , pp. 293-300
    • Bertani, G.1    Nice, S.J.2
  • 15
    • 34548094602 scopus 로고    scopus 로고
    • Evolution of enzymatic activities in the enolase superfamily: L-talarate/galactarate dehydratase from Salmonella typhimurium LT2
    • DOI 10.1021/bi7008882
    • Yew, W. S., Fedorov, A. A., Fedorov, E. V., Almo, S. C., and Gerlt, J. A. (2007) Evolution of enzymatic activities in the enolase superfamily: Ltalarate/ galactarate dehydratase from Salmonella typhimurium LT2. Biochemistry 46, 9564-9577 (Pubitemid 47291963)
    • (2007) Biochemistry , vol.46 , Issue.33 , pp. 9564-9577
    • Wen, S.Y.1    Fedorov, A.A.2    Fedorov, E.V.3    Almo, S.C.4    Gerlt, J.A.5
  • 17
    • 0034254465 scopus 로고    scopus 로고
    • Crystal structures of the metal-dependent 2-dehydro-3-deoxy-galactarate aldolase suggest a novel reaction mechanism
    • Izard, T., and Blackwell, N. C. (2000) Crystal structures of the metal-dependent 2-dehydro-3-deoxy-galactarate aldolase suggest a novel reaction mechanism. EMBO J. 19, 3849-3856 (Pubitemid 30608525)
    • (2000) EMBO Journal , vol.19 , Issue.15 , pp. 3849-3856
    • Izard, T.1    Blackwell, N.C.2
  • 19
    • 80055052940 scopus 로고    scopus 로고
    • An NMR study of the equilibration of D-glucaric acid with lactone forms in aquenous acid solutions
    • Brown, J. M., Manley-Harris, M., Field, R. J., and Kiely, D. E. (2007) An NMR study of the equilibration of D-glucaric acid with lactone forms in aquenous acid solutions. J. Carbohydr. Chem. 26, 455-467
    • (2007) J. Carbohydr. Chem. , vol.26 , pp. 455-467
    • Brown, J.M.1    Manley-Harris, M.2    Field, R.J.3    Kiely, D.E.4
  • 20
    • 0030002507 scopus 로고    scopus 로고
    • Mechanism of the reaction catalyzed by mandelate racemase: Structure and mechanistic properties of the D270N mutant
    • DOI 10.1021/bi960174m
    • Schafer, S. L., Barrett, W. C., Kallarakal, A. T., Mitra, B., Kozarich, J. W., Gerlt, J. A., Clifton, J. G., Petsko, G. A., and Kenyon, G. L. (1996) Mechanism of the reaction catalyzed by mandelate racemase: structure and mechanistic properties of the D270N mutant. Biochemistry 35, 5662-5669 (Pubitemid 26143661)
    • (1996) Biochemistry , vol.35 , Issue.18 , pp. 5662-5669
    • Schafer, S.L.1    Barrett, W.C.2    Kallarakal, A.T.3    Mitra, B.4    Kozarich, J.W.5    Gerlt, J.A.6    Clifton, J.G.7    Petsko, G.A.8    Kenyon, G.L.9
  • 21
    • 0028957901 scopus 로고
    • Mechanism of the reaction catalyzed by mandelate racemase: Importance of electrophilic catalysis by glutamic acid 317
    • Mitra, B., Kallarakal, A. T., Kozarich, J. W., Gerlt, J. A., Clifton, J. G., Petsko, G. A., and Kenyon, G. L. (1995) Mechanism of the reaction catalyzed by mandelate racemase: importance of electrophilic catalysis by glutamic acid 317. Biochemistry 34, 2777-2787
    • (1995) Biochemistry , vol.34 , pp. 2777-2787
    • Mitra, B.1    Kallarakal, A.T.2    Kozarich, J.W.3    Gerlt, J.A.4    Clifton, J.G.5    Petsko, G.A.6    Kenyon, G.L.7
  • 22
    • 33845401627 scopus 로고    scopus 로고
    • Evolution of enzymatic activities in the enolase superfamily: L-fuconate dehydratase from Xanthomonas campestris
    • DOI 10.1021/bi061687o
    • Yew, W. S., Fedorov, A. A., Fedorov, E. V., Rakus, J. F., Pierce, R. W., Almo, S. C., and Gerlt, J. A. (2006) Evolution of enzymatic activities in the enolase superfamily: L-fuconate dehydratase from Xanthomonas campestris. Biochemistry 45, 14582-14597 (Pubitemid 44906975)
    • (2006) Biochemistry , vol.45 , Issue.49 , pp. 14582-14597
    • Yew, W.S.1    Fedorov, A.A.2    Fedorov, E.V.3    Rakus, J.F.4    Pierce, R.W.5    Almo, S.C.6    Gerlt, J.A.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.