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Volumn 9, Issue 7, 2000, Pages 1265-1273

Structural requirements of pyrroloquinoline quinone dependent enzymatic reactions

Author keywords

Catalytic mechanism; Electron transfer; Glucose dehydrogenase; Methanol dehydrogenase; PQQ; Quinoprotein; X ray structure

Indexed keywords

ARGININE; ASPARTIC ACID; CALCIUM ION; GLUCOSE DEHYDROGENASE; HISTIDINE; PYRROLOQUINOLINEQUINONE; QUINONE DERIVATIVE;

EID: 0033858629     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.9.7.1265     Document Type: Review
Times cited : (46)

References (41)
  • 1
    • 0010466676 scopus 로고
    • Calcium in quinoprotein methanol dehydrogenase can be replaced by strontium
    • Adachi O, Matsushita K, Shinagawa E, Ameyama M. 1990. Calcium in quinoprotein methanol dehydrogenase can be replaced by strontium. Agric Biol Chem 54:2833-2837.
    • (1990) Agric Biol Chem , vol.54 , pp. 2833-2837
    • Adachi, O.1    Matsushita, K.2    Shinagawa, E.3    Ameyama, M.4
  • 2
    • 0002788957 scopus 로고
    • Methanol dehydrogenase in Gram-negative bacteria
    • Davidson VL, ed. New York: Marcel Dekker
    • Anthony C. 1993. Methanol dehydrogenase in Gram-negative bacteria. In: Davidson VL, ed. Principles and applications of quinoproteins. New York: Marcel Dekker. pp 17-45.
    • (1993) Principles and Applications of Quinoproteins , pp. 17-45
    • Anthony, C.1
  • 3
    • 0030442943 scopus 로고    scopus 로고
    • Quinoprotein-catalyzed reactions
    • Anthony C. 1996. Quinoprotein-catalyzed reactions. Biochem J 320:697-711.
    • (1996) Biochem J , vol.320 , pp. 697-711
    • Anthony, C.1
  • 4
    • 0028584412 scopus 로고
    • The structure and function of methanol dehydrogenase and related quinoproteins containing pyrrolo-quinoline quinone
    • Anthony C, Ghosh M, Blake CC. 1994. The structure and function of methanol dehydrogenase and related quinoproteins containing pyrrolo-quinoline quinone. Biochem J 304:665-674.
    • (1994) Biochem J , vol.304 , pp. 665-674
    • Anthony, C.1    Ghosh, M.2    Blake, C.C.3
  • 5
    • 0029023298 scopus 로고
    • The role of the novel disulphide ring in the active site of the quinoprotein methanol dehydrogenase from Methylobacterium extorquem
    • Avezoux A, Goodwin MG, Anthony C. 1995. The role of the novel disulphide ring in the active site of the quinoprotein methanol dehydrogenase from Methylobacterium extorquem. Biochem J 307:735-741.
    • (1995) Biochem J , vol.307 , pp. 735-741
    • Avezoux, A.1    Goodwin, M.G.2    Anthony, C.3
  • 6
    • 0025188604 scopus 로고
    • Cloning, mapping, and sequencing of the gene encoding Escherichia coli quinoprotein glucose dehydrogenase
    • Cleton-Jansen A-M, Goosen N, Fayet O, van de Putte P. 1990. Cloning, mapping, and sequencing of the gene encoding Escherichia coli quinoprotein glucose dehydrogenase. J Bacteriol 172:6308-6315.
    • (1990) J Bacteriol , vol.172 , pp. 6308-6315
    • Cleton-Jansen, A.-M.1    Goosen, N.2    Fayet, O.3    Van De Putte, P.4
  • 7
    • 0023874871 scopus 로고
    • Cloning of the gene encoding quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus: Evidence for the presence of a second enzyme
    • Cleton-Jansen A-M, Goosen N, Wenzel TJ, van de Putte P. 1988. Cloning of the gene encoding quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus: Evidence for the presence of a second enzyme. J Bacteriol 170:2121-2125.
    • (1988) J Bacteriol , vol.170 , pp. 2121-2125
    • Cleton-Jansen, A.-M.1    Goosen, N.2    Wenzel, T.J.3    Van De Putte, P.4
  • 8
    • 0029609904 scopus 로고
    • Structure of the quinoprotein glucose dehydrogenase of Escherichia coli modelled on that of methanol dehydrogenase from Methylobacterium extorquens
    • Cozier GE, Anthony C. 1995. Structure of the quinoprotein glucose dehydrogenase of Escherichia coli modelled on that of methanol dehydrogenase from Methylobacterium extorquens. Biochem J 312:679-685.
    • (1995) Biochem J , vol.312 , pp. 679-685
    • Cozier, G.E.1    Anthony, C.2
  • 9
    • 0029043812 scopus 로고
    • The structure of the quinoprotein alcohol dehydrogenase of Acetobacter aceti modeled on that of methanol dehydrogenase from Mathylobacterium extorquens
    • Cozier GE, Giles IG, Anthony C. 1995. The structure of the quinoprotein alcohol dehydrogenase of Acetobacter aceti modeled on that of methanol dehydrogenase from Mathylobacterium extorquens. Biochem J 308:375-379.
    • (1995) Biochem J , vol.308 , pp. 375-379
    • Cozier, G.E.1    Giles, I.G.2    Anthony, C.3
  • 12
    • 0032168569 scopus 로고    scopus 로고
    • Catalytic triads and their relatives
    • Dodson G, Wlodawer A. 1998. Catalytic triads and their relatives. Trends Biochem Sci 23:347-352.
    • (1998) Trends Biochem Sci , vol.23 , pp. 347-352
    • Dodson, G.1    Wlodawer, A.2
  • 13
    • 0022979007 scopus 로고
    • Purification and characterization of quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus L.M.D. 79.41
    • Dokter P, Frank Jzn J, Duine JA. 1986. Purification and characterization of quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus L.M.D. 79.41. Biochem J 239:163-167.
    • (1986) Biochem J , vol.239 , pp. 163-167
    • Dokter, P.1    Frank Jzn, J.2    Duine, J.A.3
  • 14
    • 0024288393 scopus 로고
    • Cytochrome b-562 from Acinetobacter calcoaceticus L.M.D. 79.41. Its characteristics and role as electron acceptor for quinoprotein glucose dehydrogenase
    • Dokter P, van Wielink JE, van Kleef MA, Duine JA. 1988. Cytochrome b-562 from Acinetobacter calcoaceticus L.M.D. 79.41. Its characteristics and role as electron acceptor for quinoprotein glucose dehydrogenase. Biochem J 254:131-138.
    • (1988) Biochem J , vol.254 , pp. 131-138
    • Dokter, P.1    Van Wielink, J.E.2    Van Kleef, M.A.3    Duine, J.A.4
  • 15
    • 0025830659 scopus 로고
    • Quinoproteins: Enzymes containing the quinonoid cofactor pyrroloquinoline quinone, topaquinone, or tryptophan-tryptophan quinone
    • Duine JA. 1991. Quinoproteins: Enzymes containing the quinonoid cofactor pyrroloquinoline quinone, topaquinone, or tryptophan-tryptophan quinone. Eur J Biochem 200:271-84.
    • (1991) Eur J Biochem , vol.200 , pp. 271-284
    • Duine, J.A.1
  • 16
    • 0019003966 scopus 로고
    • Studies on methanol dehydrogenase from Hyphomicrobium X. Isolation of an oxidized form of the enzyme
    • Duine JA, Frank Jxn J. 1980. Studies on methanol dehydrogenase from Hyphomicrobium X. Isolation of an oxidized form of the enzyme. Biochem J 187:213-219.
    • (1980) Biochem J , vol.187 , pp. 213-219
    • Duine, J.A.1    Frank Jxn, J.2
  • 18
    • 0023906632 scopus 로고
    • Kinetic and spectral studies on the redox forms of methanol dehydrogenase from Hyphomicrobium X
    • Frank Jzn J, Dijkstra M, Duine JA, Balny C. 1988. Kinetic and spectral studies on the redox forms of methanol dehydrogenase from Hyphomicrobium X. Eur J Biochem 174:331-338.
    • (1988) Eur J Biochem , vol.174 , pp. 331-338
    • Frank Jzn, J.1    Dijkstra, M.2    Duine, J.A.3    Balny, C.4
  • 19
    • 0029643953 scopus 로고
    • The refined structure of the quinoprotein methanol dehydrogenase from Methylobacterium extorquens at 1.94 Å
    • Ghosh M, Anthony C, Harlos K, Goodwin MG, Blake C. 1995. The refined structure of the quinoprotein methanol dehydrogenase from Methylobacterium extorquens at 1.94 Å. Structure 3:177-187.
    • (1995) Structure , vol.3 , pp. 177-187
    • Ghosh, M.1    Anthony, C.2    Harlos, K.3    Goodwin, M.G.4    Blake, C.5
  • 22
    • 0028334063 scopus 로고
    • Replacement of enzyme-bound calcium with strontium alters the kinetic properties of methanol dehydrogenase
    • Harris TK, Davidson VL. 1994. Replacement of enzyme-bound calcium with strontium alters the kinetic properties of methanol dehydrogenase. Biochem J 300:175-182.
    • (1994) Biochem J , vol.300 , pp. 175-182
    • Harris, T.K.1    Davidson, V.L.2
  • 23
    • 0032485844 scopus 로고    scopus 로고
    • 2+ for the oxidation of alcohols by coenzyme PQQ (4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylic acid)
    • 2+ for the oxidation of alcohols by coenzyme PQQ (4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylic acid). Biochemistry 37:6562-6571.
    • (1998) Biochemistry , vol.37 , pp. 6562-6571
    • Itoh, S.1    Fukuzumi, S.2
  • 24
    • 0031054851 scopus 로고    scopus 로고
    • Modeling of the chemistry of quinoprotein methanol dehydrogenase. Oxidation of methanol by calcium complex of coenzyme PQQ via addition-elimination mechanism
    • Itoh S, Kawakami H, Fukuzumi S. 1997. Modeling of the chemistry of quinoprotein methanol dehydrogenase. Oxidation of methanol by calcium complex of coenzyme PQQ via addition-elimination mechanism. J Am Chem Soc 119:439-440.
    • (1997) J Am Chem Soc , vol.119 , pp. 439-440
    • Itoh, S.1    Kawakami, H.2    Fukuzumi, S.3
  • 25
    • 0000561126 scopus 로고
    • C-4 and C-5 adducts of cofactor PQQ (pyrroloquinoline-quinone). Model studies directed toward the action of quinoprotein methanol dehydrogenase
    • Itoh S, Ogino M, Fukui Y, Murao H, Komatsu M, Ohshiro Y, Inoue T, Kai Y, Kasai N. 1993. C-4 and C-5 adducts of cofactor PQQ (pyrroloquinoline-quinone). Model studies directed toward the action of quinoprotein methanol dehydrogenase. J Am Chem Soc 115:9960-9967.
    • (1993) J Am Chem Soc , vol.115 , pp. 9960-9967
    • Itoh, S.1    Ogino, M.2    Fukui, Y.3    Murao, H.4    Komatsu, M.5    Ohshiro, Y.6    Inoue, T.7    Kai, Y.8    Kasai, N.9
  • 26
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones TA, Zou J-Y, Cowan SW, Kjeldgaard M. 1991. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr A 47:110-119.
    • (1991) Acta Crystallogr A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 27
    • 0031942422 scopus 로고    scopus 로고
    • Homology model of the quinohaemoprotein alcohol dehydrogenase from Comamonas testosteroni
    • Jongejan A, Jongejan JA, Duine JA. 1998. Homology model of the quinohaemoprotein alcohol dehydrogenase from Comamonas testosteroni. Protein Eng 11:185-198.
    • (1998) Protein Eng , vol.11 , pp. 185-198
    • Jongejan, A.1    Jongejan, J.A.2    Duine, J.A.3
  • 28
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P. 1991. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J Appl Crystallogr 24:946-950.
    • (1991) J Appl Crystallogr , vol.24 , pp. 946-950
    • Kraulis, P.1
  • 30
    • 0030478428 scopus 로고    scopus 로고
    • Production, characterization, and reconstitution of recombinant quinoprotein glucose dehydrogenase (soluble type; EC 1.1.99.17) apoenzyme of Acinetobacter calcoaceticus
    • Olsthoorn AJJ, Duine JA. 1996. Production, characterization, and reconstitution of recombinant quinoprotein glucose dehydrogenase (soluble type; EC 1.1.99.17) apoenzyme of Acinetobacter calcoaceticus. Arch Biochem Biophys 336-42-48.
    • (1996) Arch Biochem Biophys , vol.336 , pp. 42-48
    • Olsthoorn, A.J.J.1    Duine, J.A.2
  • 31
    • 0032578493 scopus 로고    scopus 로고
    • On the mechanism and specificity of the soluble, quinoprotein glucose dehydrogenase in the oxidation of aldose sugars
    • Olsthoorn AJJ, Duine JA. 1998. On the mechanism and specificity of the soluble, quinoprotein glucose dehydrogenase in the oxidation of aldose sugars, Biochemistry 37:13854-13861.
    • (1998) Biochemistry , vol.37 , pp. 13854-13861
    • Olsthoorn, A.J.J.1    Duine, J.A.2
  • 32
    • 0030612120 scopus 로고    scopus 로고
    • 2+ and its substitutes have two different binding sites and roles in soluble, quinoprotein (pyrroloquinoline-quinone-containing) glucose dehydrogenase
    • 2+ and its substitutes have two different binding sites and roles in soluble, quinoprotein (pyrroloquinoline-quinone-containing) glucose dehydrogenase. Eur J Biochem 247:659-665.
    • (1997) Eur J Biochem , vol.247 , pp. 659-665
    • Olsthoorn, A.J.J.1    Otsuki, T.2    Duine, J.A.3
  • 33
    • 0032742692 scopus 로고    scopus 로고
    • Active-site structure of the soluble quinoprotein glucose dehydrogenase complexed with methylhydrazine: A covalent cofactor-inhibitor complex
    • Oubrie A, Rozeboom HJ, Dijkstra BW. 1999a. Active-site structure of the soluble quinoprotein glucose dehydrogenase complexed with methylhydrazine: A covalent cofactor-inhibitor complex. Proc Natl Acad Sci USA 96:11787-11791.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 11787-11791
    • Oubrie, A.1    Rozeboom, H.J.2    Dijkstra, B.W.3
  • 34
    • 0033522648 scopus 로고    scopus 로고
    • The 1.7 Å crystal structure of the apo form of the soluble quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus reveals a novel internal conserved sequence repeat
    • Oubrie A, Rozeboom HJ, Kalk KH, Duine JA, Dijkstra BW. 1999b. The 1.7 Å crystal structure of the apo form of the soluble quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus reveals a novel internal conserved sequence repeat. J Mol Biol 289:319-333.
    • (1999) J Mol Biol , vol.289 , pp. 319-333
    • Oubrie, A.1    Rozeboom, H.J.2    Kalk, K.H.3    Duine, J.A.4    Dijkstra, B.W.5
  • 36
    • 0026460168 scopus 로고
    • Characterization of mutant forms of the quinoprotein methanol dehydrogenase lacking an essential calcium ion
    • Richardson IW, Anthony C. 1992. Characterization of mutant forms of the quinoprotein methanol dehydrogenase lacking an essential calcium ion. Biochem J 287:709-715.
    • (1992) Biochem J , vol.287 , pp. 709-715
    • Richardson, I.W.1    Anthony, C.2
  • 38
    • 0030000290 scopus 로고    scopus 로고
    • Determination of the gene sequence and the three-dimensional structure at 2.4 angstroms resolution of methanol dehydrogenase from Methylophilus W3A1
    • Xia Z-X, Dai W-W, Zhang Y-E, White SA, Boyd GD, Mathews FS. 1996. Determination of the gene sequence and the three-dimensional structure at 2.4 angstroms resolution of methanol dehydrogenase from Methylophilus W3A1. J Mol Biol 259:480-501.
    • (1996) J Mol Biol , vol.259 , pp. 480-501
    • Xia, Z.-X.1    Dai, W.-W.2    Zhang, Y.-E.3    White, S.A.4    Boyd, G.D.5    Mathews, F.S.6
  • 39
    • 0033604837 scopus 로고    scopus 로고
    • Detailed active site configuration of a new crystal form of methanol dehydrogenase from Methylophilus W3A1 at 1.9 Å resolution
    • Xia Z-X, He Y-N, Dai W-W, White SA, Boyd GD, Mathews FS. 1999. Detailed active site configuration of a new crystal form of methanol dehydrogenase from Methylophilus W3A1 at 1.9 Å resolution. Biochemistry 38:1214-1220.
    • (1999) Biochemistry , vol.38 , pp. 1214-1220
    • Xia, Z.-X.1    He, Y.-N.2    Dai, W.-W.3    White, S.A.4    Boyd, G.D.5    Mathews, F.S.6
  • 41
    • 0030722730 scopus 로고    scopus 로고
    • 2+ in the catalytic mechanism of quinoprotein methanol dehydrogenase
    • 2+ in the catalytic mechanism of quinoprotein methanol dehydrogenase. Proc Natl Acad Sci USA 94:11881-11886.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 11881-11886
    • Zheng, Y.-J.1    Bruice, T.C.2


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