메뉴 건너뛰기




Volumn 24, Issue , 2014, Pages 160-172

Engineered, highly productive biosynthesis of artificial, lactonized statin side-chain building blocks: The hidden potential of Escherichia coli unleashed

Author keywords

Artificial biosynthetic pathway; DERA; Escherichia coli; Glucose dehydrogenase; Pathway engineering; PQQ; Respiratory chain; Super statins; Whole cell

Indexed keywords

BIOCHEMISTRY; BIOSYNTHESIS; CHAINS; ESCHERICHIA COLI; ESTERS; GLUCOSE; OXIDATION; REACTION INTERMEDIATES; REGIOSELECTIVITY; STEREOCHEMISTRY;

EID: 84902000106     PISSN: 10967176     EISSN: 10967184     Source Type: Journal    
DOI: 10.1016/j.ymben.2014.05.012     Document Type: Article
Times cited : (18)

References (82)
  • 1
    • 38549113256 scopus 로고    scopus 로고
    • Biooxidation with PQQ-and FAD-Dependent Dehydrogenases
    • Wiley Online Library, Weinheim, Germany, R.D. Schmid, V.B. Urlacher (Eds.)
    • Adachi O., Ano Y., Toyama H., Matsushita K. Biooxidation with PQQ-and FAD-Dependent Dehydrogenases. Modern Biooxidation: Enzymes, Reactions and Applications 2007, 1-41. Wiley Online Library, Weinheim, Germany. R.D. Schmid, V.B. Urlacher (Eds.).
    • (2007) Modern Biooxidation: Enzymes, Reactions and Applications , pp. 1-41
    • Adachi, O.1    Ano, Y.2    Toyama, H.3    Matsushita, K.4
  • 3
    • 0001843637 scopus 로고
    • Purification and characterization of the quinoprotein d-glucose dehydrogenase apoenzyme from escherichia coli.
    • Ameyama M., Nonobe M., Shinagawa E., Matsushita K., Takimoto K. Purification and characterization of the quinoprotein d-glucose dehydrogenase apoenzyme from escherichia coli. Agric. Biol. Chem. 1986, 50:49-57.
    • (1986) Agric. Biol. Chem. , vol.50 , pp. 49-57
    • Ameyama, M.1    Nonobe, M.2    Shinagawa, E.3    Matsushita, K.4    Takimoto, K.5
  • 4
    • 3042691747 scopus 로고    scopus 로고
    • The quinoprotein dehydrogenases for methanol and glucose
    • Anthony C. The quinoprotein dehydrogenases for methanol and glucose. Arch. Biochem. Biophys. 2004, 428:2-9.
    • (2004) Arch. Biochem. Biophys. , vol.428 , pp. 2-9
    • Anthony, C.1
  • 7
    • 0036152266 scopus 로고    scopus 로고
    • Electronic effects on the regio- and enantioselectivity of the asymmetric aminohydroxylation of O-substituted 4-hydroxy-2-butenoates
    • Chuang C.-Y., Vassar V.C., Ma Z., Geney R., Ojima I. Electronic effects on the regio- and enantioselectivity of the asymmetric aminohydroxylation of O-substituted 4-hydroxy-2-butenoates. Chirality 2002, 14:151-162.
    • (2002) Chirality , vol.14 , pp. 151-162
    • Chuang, C.-Y.1    Vassar, V.C.2    Ma, Z.3    Geney, R.4    Ojima, I.5
  • 9
    • 84902004537 scopus 로고    scopus 로고
    • ((2S, 4R)-4, 6-dihydroxytetrahydro-2H-pyran-2-yl) methyl carboxylate and process for the production thereof. WO2009092702.
    • Cluzeau, J., Časar, Z., Mrak, P., 2009. ((2S, 4R)-4, 6-dihydroxytetrahydro-2H-pyran-2-yl) methyl carboxylate and process for the production thereof. WO2009092702.
    • (2009)
    • Cluzeau, J.1    Časar, Z.2    Mrak, P.3
  • 10
    • 0033564725 scopus 로고    scopus 로고
    • Characterization of the membrane quinoprotein glucose dehydrogenase from Escherichia coli and characterization of a site-directed mutant in which histidine-262 has been changed to tyrosine
    • Cozier G.E., Salleh R.A., Anthony C. Characterization of the membrane quinoprotein glucose dehydrogenase from Escherichia coli and characterization of a site-directed mutant in which histidine-262 has been changed to tyrosine. Biochem. J. 1999, 340:639-647.
    • (1999) Biochem. J. , vol.340 , pp. 639-647
    • Cozier, G.E.1    Salleh, R.A.2    Anthony, C.3
  • 11
    • 49649100687 scopus 로고    scopus 로고
    • Straightforward and efficient synthesis of (4r,6s)-4-(tert-butyldimethylsiloxy)-6-(hydroxymethyl)tetrahydropyran-2-one
    • Časar Z. Straightforward and efficient synthesis of (4r,6s)-4-(tert-butyldimethylsiloxy)-6-(hydroxymethyl)tetrahydropyran-2-one. Synlett 2008, 2036-2040.
    • (2008) Synlett , pp. 2036-2040
    • Časar, Z.1
  • 12
    • 77954940183 scopus 로고    scopus 로고
    • Historic overview and recent advances in the synthesis of super-statins
    • Časar Z. Historic overview and recent advances in the synthesis of super-statins. Curr. Org. Chem. 2010, 14:816-845.
    • (2010) Curr. Org. Chem. , vol.14 , pp. 816-845
    • Časar, Z.1
  • 13
    • 84902004538 scopus 로고    scopus 로고
    • Processes for the preparation of statins, particularly rosuvastatin, and intermediates for the preparation thereof. WO2008119810.
    • Časar, Z., Kopitar, G., Mesar, T., Mrak, P., Ošlaj, M., 2008. Processes for the preparation of statins, particularly rosuvastatin, and intermediates for the preparation thereof. WO2008119810.
    • (2008)
    • Časar, Z.1    Kopitar, G.2    Mesar, T.3    Mrak, P.4    Ošlaj, M.5
  • 14
    • 67649388098 scopus 로고    scopus 로고
    • The First Convenient Entry to δ-Formyl-δ-valerolactone Precursor for the Synthesis of Statins via Lactonized Side Chain
    • Časar Z., Košmrlj J. The First Convenient Entry to δ-Formyl-δ-valerolactone Precursor for the Synthesis of Statins via Lactonized Side Chain. Synlett 2009, 1144-1148.
    • (2009) Synlett , pp. 1144-1148
    • Časar, Z.1    Košmrlj, J.2
  • 15
    • 77957123606 scopus 로고    scopus 로고
    • Lactone Pathway to statins utilizing the wittig reaction. the synthesis of rosuvastatin
    • Časar Z., Steinbucher M., Košmrlj J. Lactone Pathway to statins utilizing the wittig reaction. the synthesis of rosuvastatin. J. Org. Chem. 2010, 75:6681-6684.
    • (2010) J. Org. Chem. , vol.75 , pp. 6681-6684
    • Časar, Z.1    Steinbucher, M.2    Košmrlj, J.3
  • 16
    • 33846133002 scopus 로고    scopus 로고
    • Lipid-lowering effects of statins: a comparative review
    • Davidson M.H., Robinson J.G. Lipid-lowering effects of statins: a comparative review. Expert Opin. Pharmacother. 2006, 7:1701-1714.
    • (2006) Expert Opin. Pharmacother. , vol.7 , pp. 1701-1714
    • Davidson, M.H.1    Robinson, J.G.2
  • 17
    • 3042647300 scopus 로고    scopus 로고
    • Electron transfer in quinoproteins
    • Davidson V.L. Electron transfer in quinoproteins. Arch. Biochem. Biophys. 2004, 428:32-40.
    • (2004) Arch. Biochem. Biophys. , vol.428 , pp. 32-40
    • Davidson, V.L.1
  • 18
    • 0034622429 scopus 로고    scopus 로고
    • 2+-assisted, direct hydride transfer, and rate-determining tautomerization of c5-reduced PQQ to PQQH 2, in the oxidation of-d-glucose by soluble, quinoprotein glucose dehydrogenase
    • 2+-assisted, direct hydride transfer, and rate-determining tautomerization of c5-reduced PQQ to PQQH 2, in the oxidation of-d-glucose by soluble, quinoprotein glucose dehydrogenase. Biochemistry 2000, 39:9384-9392.
    • (2000) Biochemistry , vol.39 , pp. 9384-9392
    • Dewanti, A.R.1    Duine, J.A.2
  • 19
    • 1642453630 scopus 로고    scopus 로고
    • Occurrence of a bound ubiquinone and its function in Escherichia coli membrane-bound quinoprotein glucose dehydrogenase
    • Elias M.D., Nakamura S., Migita C.T., Miyoshi H., Toyama H., Matsushita K., Adachi O., Yamada M. Occurrence of a bound ubiquinone and its function in Escherichia coli membrane-bound quinoprotein glucose dehydrogenase. J. Biol. Chem. 2004, 279:3078-3083.
    • (2004) J. Biol. Chem. , vol.279 , pp. 3078-3083
    • Elias, M.D.1    Nakamura, S.2    Migita, C.T.3    Miyoshi, H.4    Toyama, H.5    Matsushita, K.6    Adachi, O.7    Yamada, M.8
  • 20
    • 84861341314 scopus 로고    scopus 로고
    • The Use of a Lactonized Statin Side-Chain Precursor in a Concise and Efficient Assembly of Pitavastatin
    • Fabris J., Časar Z., Smilović I. The Use of a Lactonized Statin Side-Chain Precursor in a Concise and Efficient Assembly of Pitavastatin. Synthesis (Stuttg) 2012, 44:1700-1710.
    • (2012) Synthesis (Stuttg) , vol.44 , pp. 1700-1710
    • Fabris, J.1    Časar, Z.2    Smilović, I.3
  • 21
    • 84857405775 scopus 로고    scopus 로고
    • Review of glucose oxidases and glucose dehydrogenases: a bird[U+05F3]s eye view of glucose sensing enzymes
    • Ferri S., Kojima K., Sode K. Review of glucose oxidases and glucose dehydrogenases: a bird[U+05F3]s eye view of glucose sensing enzymes. J. Diabetes Sci. Technol. 2011, 5:1068-1076.
    • (2011) J. Diabetes Sci. Technol. , vol.5 , pp. 1068-1076
    • Ferri, S.1    Kojima, K.2    Sode, K.3
  • 22
    • 0000305933 scopus 로고
    • Unprecedented asymmetric aldol reactions with three aldehyde substrates catalyzed by 2-deoxyribose-5-phosphate aldolase
    • Gijsen H.J.M., Wong C.-H. Unprecedented asymmetric aldol reactions with three aldehyde substrates catalyzed by 2-deoxyribose-5-phosphate aldolase. J. Am. Chem. Soc. 1994, 116:8422-8423.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 8422-8423
    • Gijsen, H.J.M.1    Wong, C.-H.2
  • 23
    • 0028854636 scopus 로고
    • Sequential three-and four-substrate aldol reactions catalyzed by aldolases
    • Gijsen H.J.M., Wong C.-H. Sequential three-and four-substrate aldol reactions catalyzed by aldolases. J. Am. Chem. Soc. 1995, 117:7585-7591.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 7585-7591
    • Gijsen, H.J.M.1    Wong, C.-H.2
  • 25
    • 0031733482 scopus 로고    scopus 로고
    • The Biochemistry, Physiology and Genetics of PQQ and PQQ-containing Enzymes
    • Academic Press, London, UK, R.K. Poole (Ed.)
    • Goodwin P.M., Anthony C. The Biochemistry, Physiology and Genetics of PQQ and PQQ-containing Enzymes. Advances in Microbial Physiology 1998, 1-80. Academic Press, London, UK. R.K. Poole (Ed.).
    • (1998) Advances in Microbial Physiology , pp. 1-80
    • Goodwin, P.M.1    Anthony, C.2
  • 26
    • 1942469509 scopus 로고    scopus 로고
    • Development of an efficient, scalable, aldolase-catalyzed process for enantioselective synthesis of statin intermediates
    • Greenberg W., Varvak A., Hanson S.R., Wong K., Huang H., Chen P., Burk M.J. Development of an efficient, scalable, aldolase-catalyzed process for enantioselective synthesis of statin intermediates. Proc. Natl. Acad. Sci. USA 2004, 101:5788.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 5788
    • Greenberg, W.1    Varvak, A.2    Hanson, S.R.3    Wong, K.4    Huang, H.5    Chen, P.6    Burk, M.J.7
  • 27
    • 84858009802 scopus 로고    scopus 로고
    • Chemoselective ruthenium-catalyzed reduction of acid chlorides to aldehydes with dimethylphenylsilane
    • Gutsulyak D.V., Nikonov G.I. Chemoselective ruthenium-catalyzed reduction of acid chlorides to aldehydes with dimethylphenylsilane. Adv. Synth. Catal. 2012, 354:607-611.
    • (2012) Adv. Synth. Catal. , vol.354 , pp. 607-611
    • Gutsulyak, D.V.1    Nikonov, G.I.2
  • 28
    • 79953052029 scopus 로고    scopus 로고
    • Genome-wide identification of the subcellular localization of the Escherichia coli B proteome using experimental and computational methods
    • Han M.-J., Yun H., Lee J.W., Lee Y.H., Lee S.Y., Yoo J.-S., Kim J.Y., Kim J.F., Hur C.-G. Genome-wide identification of the subcellular localization of the Escherichia coli B proteome using experimental and computational methods. Proteomics 2011, 11:1213-1227.
    • (2011) Proteomics , vol.11 , pp. 1213-1227
    • Han, M.-J.1    Yun, H.2    Lee, J.W.3    Lee, Y.H.4    Lee, S.Y.5    Yoo, J.-S.6    Kim, J.Y.7    Kim, J.F.8    Hur, C.-G.9
  • 29
    • 78651151958 scopus 로고
    • Glucose Dehydrogenase of Bacterium anitratum: an enzyme with a novel prosthetic group glucose dehydrogenase of bacterium with a novel prosthetic group
    • Hauge J.G. Glucose Dehydrogenase of Bacterium anitratum: an enzyme with a novel prosthetic group glucose dehydrogenase of bacterium with a novel prosthetic group. J. Biol. Chem. 1964, 239:3630-3639.
    • (1964) J. Biol. Chem. , vol.239 , pp. 3630-3639
    • Hauge, J.G.1
  • 31
    • 2042548037 scopus 로고    scopus 로고
    • Engineering PQQ glucose dehydrogenase with improved substrate specificity: Site-directed mutagenesis studies on the active center of PQQ glucose dehydrogenase
    • Igarashi S., Hirokawa T., Sode K. Engineering PQQ glucose dehydrogenase with improved substrate specificity: Site-directed mutagenesis studies on the active center of PQQ glucose dehydrogenase. Biomol. Eng. 2004, 21:81-89.
    • (2004) Biomol. Eng. , vol.21 , pp. 81-89
    • Igarashi, S.1    Hirokawa, T.2    Sode, K.3
  • 32
    • 0033517714 scopus 로고    scopus 로고
    • Construction and characterization of mutant water-soluble PQQ glucose dehydrogenases with altered Km values-site-directed mutagenesis studies on the putative active site
    • Igarashi S., Ohtera T., Yoshida H., Witarto A.B., Sode K. Construction and characterization of mutant water-soluble PQQ glucose dehydrogenases with altered Km values-site-directed mutagenesis studies on the putative active site. Biochem. Biophys. Res. Commun. 1999, 264:820-824.
    • (1999) Biochem. Biophys. Res. Commun. , vol.264 , pp. 820-824
    • Igarashi, S.1    Ohtera, T.2    Yoshida, H.3    Witarto, A.B.4    Sode, K.5
  • 34
    • 0035843962 scopus 로고    scopus 로고
    • Structural mechanism for statin inhibition of HMG-CoA reductase
    • Istvan E.S., Deisenhofer J. Structural mechanism for statin inhibition of HMG-CoA reductase. Science 2001, 292:1160-1164.
    • (2001) Science , vol.292 , pp. 1160-1164
    • Istvan, E.S.1    Deisenhofer, J.2
  • 35
    • 1242341191 scopus 로고    scopus 로고
    • The metal ion in the active site of the membrane glucose dehydrogenase of Escherichia coli
    • James P.L., Anthony C. The metal ion in the active site of the membrane glucose dehydrogenase of Escherichia coli. Biochim. Biophys. Acta-Proteins Proteomics 2003, 1647:200-205.
    • (2003) Biochim. Biophys. Acta-Proteins Proteomics , vol.1647 , pp. 200-205
    • James, P.L.1    Anthony, C.2
  • 36
    • 0030030737 scopus 로고    scopus 로고
    • Pyrroloquinoline quinone, a Chemotactic Attractant for Escherichia coli
    • Jonge R.D.e., Mattos M.J.T., De Stock J.B., Neijssel O.M. Pyrroloquinoline quinone, a Chemotactic Attractant for Escherichia coli. J. Bacteriol. 1996, 178:1224-1226.
    • (1996) J. Bacteriol. , vol.178 , pp. 1224-1226
    • Jonge, R.1    Mattos, M.J.T.2    De Stock, J.B.3    Neijssel, O.M.4
  • 37
    • 0000107461 scopus 로고
    • Specificity of glucose oxidase (notatin)
    • Keilin D., Hartree E.F. Specificity of glucose oxidase (notatin). Biochem. J. 1952, 50:331-341.
    • (1952) Biochem. J. , vol.50 , pp. 331-341
    • Keilin, D.1    Hartree, E.F.2
  • 38
    • 33749233854 scopus 로고    scopus 로고
    • Life after statin patent expiries
    • Kidd J. Life after statin patent expiries. Nat. Rev. Drug Discov. 2006, 5:813-814.
    • (2006) Nat. Rev. Drug Discov. , vol.5 , pp. 813-814
    • Kidd, J.1
  • 39
    • 0142245758 scopus 로고    scopus 로고
    • Surface charge engineering of PQQ glucose dehydrogenase for downstream processing
    • Koh H., Igarashi S., Sode K. Surface charge engineering of PQQ glucose dehydrogenase for downstream processing. Biotechnol. Lett. 2003, 25:1695-1701.
    • (2003) Biotechnol. Lett. , vol.25 , pp. 1695-1701
    • Koh, H.1    Igarashi, S.2    Sode, K.3
  • 41
    • 0022392499 scopus 로고
    • An expeditious chiral route to analogs of mevinolin and compactin
    • Lee T.-J. An expeditious chiral route to analogs of mevinolin and compactin. Tetrahedron Lett. 1985, 26:4995-4996.
    • (1985) Tetrahedron Lett. , vol.26 , pp. 4995-4996
    • Lee, T.-J.1
  • 42
    • 70349621610 scopus 로고    scopus 로고
    • Biocatalysis in the Preparation of the Statin Side Chain
    • Liljeblad A., Kallinen A., Kanerva L. Biocatalysis in the Preparation of the Statin Side Chain. Curr. Org. Synth. 2009, 6:362-379.
    • (2009) Curr. Org. Synth. , vol.6 , pp. 362-379
    • Liljeblad, A.1    Kallinen, A.2    Kanerva, L.3
  • 46
    • 0008954032 scopus 로고
    • Quinoprotein d-glucose dehydrogenase in Acinetobacter calcoaceticus LMD 79.41: the membrane-bound enzyme is distinct from the soluble enzyme
    • Matsushita K., Shinagawa E., Adachi O., Ameyama M. Quinoprotein d-glucose dehydrogenase in Acinetobacter calcoaceticus LMD 79.41: the membrane-bound enzyme is distinct from the soluble enzyme. FEMS Microbiol. Lett. 1988, 55:53-57.
    • (1988) FEMS Microbiol. Lett. , vol.55 , pp. 53-57
    • Matsushita, K.1    Shinagawa, E.2    Adachi, O.3    Ameyama, M.4
  • 47
    • 0024978389 scopus 로고
    • Quinoprotein d-glucose dehydrogenase of the Acinetobacter calcoaceticus respiratory chain: membrane-bound and soluble forms are different molecular species
    • Matsushita K., Shinagawa E., Adachi O., Ameyama M. Quinoprotein d-glucose dehydrogenase of the Acinetobacter calcoaceticus respiratory chain: membrane-bound and soluble forms are different molecular species. Biochemistry 1989, 28:6276-6280.
    • (1989) Biochemistry , vol.28 , pp. 6276-6280
    • Matsushita, K.1    Shinagawa, E.2    Adachi, O.3    Ameyama, M.4
  • 49
    • 37049088240 scopus 로고
    • Synthetic study on 1,3-polyols. An efficient enantioselective synthesis of tarchonanthuslactone
    • Mori Y., Suzuki M. Synthetic study on 1,3-polyols. An efficient enantioselective synthesis of tarchonanthuslactone. J. Chem. Soc. Perkin Trans. I 1990, 1809-1812.
    • (1990) J. Chem. Soc. Perkin Trans. I , pp. 1809-1812
    • Mori, Y.1    Suzuki, M.2
  • 50
    • 12344273661 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis of building blocks for statin side chains
    • Müller M. Chemoenzymatic synthesis of building blocks for statin side chains. Angew. Chem. Int. 2005, 44:362-365.
    • (2005) Angew. Chem. Int. , vol.44 , pp. 362-365
    • Müller, M.1
  • 51
    • 52049118563 scopus 로고    scopus 로고
    • Amino acid residues interacting with both the bound quinone and coenzyme, pyrroloquinoline quinone, in Escherichia coli membrane-bound glucose dehydrogenase
    • Mustafa G., Ishikawa Y., Kobayashi K., Migita C.T., Elias M.D., Nakamura S., Tagawa S., Yamada M. Amino acid residues interacting with both the bound quinone and coenzyme, pyrroloquinoline quinone, in Escherichia coli membrane-bound glucose dehydrogenase. J. Biol. Chem. 2008, 283:22215-22221.
    • (2008) J. Biol. Chem. , vol.283 , pp. 22215-22221
    • Mustafa, G.1    Ishikawa, Y.2    Kobayashi, K.3    Migita, C.T.4    Elias, M.D.5    Nakamura, S.6    Tagawa, S.7    Yamada, M.8
  • 52
    • 57649129415 scopus 로고    scopus 로고
    • Menaquinone as well as ubiquinone as a bound quinone crucial for catalytic activity and intramolecular electron transfer in Escherichia coli membrane-bound glucose dehydrogenase
    • Mustafa G., Migita C.T., Ishikawa Y., Kobayashi K., Tagawa S., Yamada M. Menaquinone as well as ubiquinone as a bound quinone crucial for catalytic activity and intramolecular electron transfer in Escherichia coli membrane-bound glucose dehydrogenase. J. Biol. Chem. 2008, 283:28169-28175.
    • (2008) J. Biol. Chem. , vol.283 , pp. 28169-28175
    • Mustafa, G.1    Migita, C.T.2    Ishikawa, Y.3    Kobayashi, K.4    Tagawa, S.5    Yamada, M.6
  • 53
    • 0026638114 scopus 로고
    • Cloning, nucleotide sequences, and enzymatic properties of glucose dehydrogenase isozymes from Bacillus megaterium IAM1030
    • Nagao T., Mitamura T., Wang X.H., Negoro S., Yomo T., Urabe I., Okada H. Cloning, nucleotide sequences, and enzymatic properties of glucose dehydrogenase isozymes from Bacillus megaterium IAM1030. J. Bacteriol. 1992, 174:5013-5020.
    • (1992) J. Bacteriol. , vol.174 , pp. 5013-5020
    • Nagao, T.1    Mitamura, T.2    Wang, X.H.3    Negoro, S.4    Yomo, T.5    Urabe, I.6    Okada, H.7
  • 54
    • 84877139699 scopus 로고    scopus 로고
    • A highly productive, whole-cell dera chemoenzymatic process for production of key lactonized side-chain intermediates in statin synthesis
    • Ošlaj M., Cluzeau J., Orkić D., Kopitar G., Mrak P., Časar Z. A highly productive, whole-cell dera chemoenzymatic process for production of key lactonized side-chain intermediates in statin synthesis. PLoS One 2013, 8:e62250.
    • (2013) PLoS One , vol.8
    • Ošlaj, M.1    Cluzeau, J.2    Orkić, D.3    Kopitar, G.4    Mrak, P.5    Časar, Z.6
  • 55
    • 1242296082 scopus 로고    scopus 로고
    • Structure and mechanism of soluble glucose dehydrogenase and other PQQ-dependent enzymes
    • Oubrie Arthur Structure and mechanism of soluble glucose dehydrogenase and other PQQ-dependent enzymes. Biochim.t Biophys. Acta (BBA)-Proteins Proteomics 2003, 1647(1-2):143-151.
    • (2003) Biochim.t Biophys. Acta (BBA)-Proteins Proteomics , vol.1647 , Issue.1-2 , pp. 143-151
    • Oubrie, A.1
  • 56
    • 0015139551 scopus 로고
    • The oxidation of 2-acetamido-2-deoxyaldoses with aqueous bromine. Two diastereoisomeric 2-acetamido-2,3-dideoxyhex-2-enono-1,4-lactones from 2-acetamido-2-deoxy-d-glucose, -mannose, and -galactose1
    • Pravdić N., Fletcher H.G.J. The oxidation of 2-acetamido-2-deoxyaldoses with aqueous bromine. Two diastereoisomeric 2-acetamido-2,3-dideoxyhex-2-enono-1,4-lactones from 2-acetamido-2-deoxy-d-glucose, -mannose, and -galactose1. Carbohydr. Res. 1971, 19:339-352.
    • (1971) Carbohydr. Res. , vol.19 , pp. 339-352
    • Pravdić, N.1    Fletcher, H.G.J.2
  • 58
    • 1542306905 scopus 로고    scopus 로고
    • Mechanism of glucose oxidation by quinoprotein soluble glucose dehydrogenase[U+202F]: insights from molecular dynamics studies
    • Reddy S.Y., Bruice T.C. Mechanism of glucose oxidation by quinoprotein soluble glucose dehydrogenase[U+202F]: insights from molecular dynamics studies. J. Am. Chem. Soc. 2004, 126:2431-2438.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 2431-2438
    • Reddy, S.Y.1    Bruice, T.C.2
  • 61
    • 84869020402 scopus 로고    scopus 로고
    • Engineering of l-tyrosine oxidation in Escherichia coli and microbial production of hydroxytyrosol
    • Satoh Y., Tajima K., Munekata M., Keasling J.D., Lee T.S. Engineering of l-tyrosine oxidation in Escherichia coli and microbial production of hydroxytyrosol. Metab. Eng. 2012, 14:603-610.
    • (2012) Metab. Eng. , vol.14 , pp. 603-610
    • Satoh, Y.1    Tajima, K.2    Munekata, M.3    Keasling, J.D.4    Lee, T.S.5
  • 62
    • 0027996364 scopus 로고
    • Identification of a novel quinone-binding site in the cytochrome bo complex from Escherichia coli
    • Sato-Watanabe M., Mogi T., Ogura T., Kitagawa T., Miyoshi H., Iwamura H., Anraku Y. Identification of a novel quinone-binding site in the cytochrome bo complex from Escherichia coli. J. Biol. Chem. 1994, 269:28908-28912.
    • (1994) J. Biol. Chem. , vol.269 , pp. 28908-28912
    • Sato-Watanabe, M.1    Mogi, T.2    Ogura, T.3    Kitagawa, T.4    Miyoshi, H.5    Iwamura, H.6    Anraku, Y.7
  • 63
    • 13444251203 scopus 로고    scopus 로고
    • Chemical, pharmacokinetic and pharmacodynamic properties of statins: an update
    • Schachter M. Chemical, pharmacokinetic and pharmacodynamic properties of statins: an update. Fundam. Clin. Pharmacol. 2005, 19:117-125.
    • (2005) Fundam. Clin. Pharmacol. , vol.19 , pp. 117-125
    • Schachter, M.1
  • 64
    • 0025425199 scopus 로고
    • Fluorinated carbohydrates as potential plasma membrane modifiers. Synthesis of 4- and 6-fluoro derivatives of 2-acetamido-2-deoxy-d-hexopyranoses
    • Sharma M., Bernacki R.J., Paul B., Korytnyk W. Fluorinated carbohydrates as potential plasma membrane modifiers. Synthesis of 4- and 6-fluoro derivatives of 2-acetamido-2-deoxy-d-hexopyranoses. Carbohydr. Res. 1990, 198:205-221.
    • (1990) Carbohydr. Res. , vol.198 , pp. 205-221
    • Sharma, M.1    Bernacki, R.J.2    Paul, B.3    Korytnyk, W.4
  • 65
    • 0026705218 scopus 로고
    • Active site similarities of glucose dehydrogenase, glucose oxidase, and glucoamylase probed by deoxygenated substrates
    • Sierks M.R., Bock K., Refn S., Svensson B. Active site similarities of glucose dehydrogenase, glucose oxidase, and glucoamylase probed by deoxygenated substrates. Biochemistry 1992, 31:8972-8977.
    • (1992) Biochemistry , vol.31 , pp. 8972-8977
    • Sierks, M.R.1    Bock, K.2    Refn, S.3    Svensson, B.4
  • 66
    • 34547433650 scopus 로고    scopus 로고
    • Biotechnological production of gluconic acid: future implications
    • Singh O.V., Kumar R. Biotechnological production of gluconic acid: future implications. Appl. Microbiol. Biotechnol. 2007, 75:713-722.
    • (2007) Appl. Microbiol. Biotechnol. , vol.75 , pp. 713-722
    • Singh, O.V.1    Kumar, R.2
  • 67
    • 0030595043 scopus 로고    scopus 로고
    • Increased production of recombinant pyrroloquinoline quinone (PQQ) glucose dehydrogenase by metabolically engineered Escherichia coli strain capable of PQQ biosynthesis
    • Sode K., Ito K., Witarto A.B., Watanabe K., Yoshida H., Postma P.W. Increased production of recombinant pyrroloquinoline quinone (PQQ) glucose dehydrogenase by metabolically engineered Escherichia coli strain capable of PQQ biosynthesis. J. Biotechnol. 1996, 49:239-243.
    • (1996) J. Biotechnol. , vol.49 , pp. 239-243
    • Sode, K.1    Ito, K.2    Witarto, A.B.3    Watanabe, K.4    Yoshida, H.5    Postma, P.W.6
  • 68
    • 0034079533 scopus 로고    scopus 로고
    • Increasing the thermal stability of the water-soluble pyrroloquinoline quinone glucose dehydrogenase by single amino acid replacement
    • Sode K., Ootera T., Shirahane M., Witarto A.B., Igarashi S., Yoshida H. Increasing the thermal stability of the water-soluble pyrroloquinoline quinone glucose dehydrogenase by single amino acid replacement. Enzyme Microb. Technol. 2000, 26:491-496.
    • (2000) Enzyme Microb. Technol. , vol.26 , pp. 491-496
    • Sode, K.1    Ootera, T.2    Shirahane, M.3    Witarto, A.B.4    Igarashi, S.5    Yoshida, H.6
  • 70
    • 0028587627 scopus 로고
    • Over expression of PQQ glucose dehydrogenase in Esherichia coli under holo enzyme forming conditions
    • Sode K., Witarto A.B., Watanabe K., Noda K., Ito S., Tsugawa W. Over expression of PQQ glucose dehydrogenase in Esherichia coli under holo enzyme forming conditions. Biotechnol. Lett. 1994, 16:1265-1268.
    • (1994) Biotechnol. Lett. , vol.16 , pp. 1265-1268
    • Sode, K.1    Witarto, A.B.2    Watanabe, K.3    Noda, K.4    Ito, S.5    Tsugawa, W.6
  • 71
    • 33750075455 scopus 로고    scopus 로고
    • Soluble aldose sugar dehydrogenase from Escherichia coli: a highly exposed active site conferring broad substrate specificity
    • Southall S.M., Doel J.J., Richardson D.J., Oubrie A. Soluble aldose sugar dehydrogenase from Escherichia coli: a highly exposed active site conferring broad substrate specificity. J. Biol. Chem. 2006, 281:30650-30659.
    • (2006) J. Biol. Chem. , vol.281 , pp. 30650-30659
    • Southall, S.M.1    Doel, J.J.2    Richardson, D.J.3    Oubrie, A.4
  • 72
    • 84885184123 scopus 로고    scopus 로고
    • Monitoring of pqq-dependent glucose dehydrogenase substrate specificity for its potential use in biocatalysis and bioanalysis
    • Stred[U+05F3]anský M., Monošík R., Mastihuba V., Sturdík E. Monitoring of pqq-dependent glucose dehydrogenase substrate specificity for its potential use in biocatalysis and bioanalysis. Appl. Biochem. Biotechnol 2013.
    • (2013) Appl. Biochem. Biotechnol
    • Stred'anský, M.1    Monošík, R.2    Mastihuba, V.3    Sturdík, E.4
  • 73
    • 79952698902 scopus 로고    scopus 로고
    • Probing reactivity of pqq-dependent carbohydrate dehydrogenases using artificial electron acceptor
    • Tetianec L., Bratkovskaja I., Kulys J., Casaie V., Meskys R. Probing reactivity of pqq-dependent carbohydrate dehydrogenases using artificial electron acceptor. Appl. Biochem. Biotechnol. 2011, 163:404-414.
    • (2011) Appl. Biochem. Biotechnol. , vol.163 , pp. 404-414
    • Tetianec, L.1    Bratkovskaja, I.2    Kulys, J.3    Casaie, V.4    Meskys, R.5
  • 74
    • 78649833943 scopus 로고    scopus 로고
    • Efficient subfractionation of gram-negative bacteria for proteomics studies research articles
    • Thein M., Sauer G., Paramasivam N., Grin I., Linke D. Efficient subfractionation of gram-negative bacteria for proteomics studies research articles. J. Proteome Res. 2010, 9:6135-6147.
    • (2010) J. Proteome Res. , vol.9 , pp. 6135-6147
    • Thein, M.1    Sauer, G.2    Paramasivam, N.3    Grin, I.4    Linke, D.5
  • 75
    • 0038004785 scopus 로고    scopus 로고
    • Lovastatin and beyond: the history of the HMG-CoA reductase inhibitors
    • Tobert J.A. Lovastatin and beyond: the history of the HMG-CoA reductase inhibitors. Nat. Rev. Drug Discov. 2003, 2:517-526.
    • (2003) Nat. Rev. Drug Discov. , vol.2 , pp. 517-526
    • Tobert, J.A.1
  • 77
    • 34547634728 scopus 로고    scopus 로고
    • PH of the cytoplasm and periplasm of Escherichia coli: rapid measurement by green fluorescent protein fluorimetry
    • Wilks J.C., Slonczewski J.L. pH of the cytoplasm and periplasm of Escherichia coli: rapid measurement by green fluorescent protein fluorimetry. J. Bacteriol. 2007, 189:5601-5607.
    • (2007) J. Bacteriol. , vol.189 , pp. 5601-5607
    • Wilks, J.C.1    Slonczewski, J.L.2
  • 78
    • 43549095197 scopus 로고    scopus 로고
    • Glucose oxidase: natural occurrence, function, properties and industrial applications
    • Wong C.M., Wong K.H., Chen X.D. Glucose oxidase: natural occurrence, function, properties and industrial applications. Appl. Microbiol. Biotechnol. 2008, 78:927-938.
    • (2008) Appl. Microbiol. Biotechnol. , vol.78 , pp. 927-938
    • Wong, C.M.1    Wong, K.H.2    Chen, X.D.3
  • 79
    • 0038312036 scopus 로고    scopus 로고
    • Escherichia coli PQQ-containing quinoprotein glucose dehydrogenase: its structure comparison with other quinoproteins
    • Yamada M., Elias M., Matsushita K., Migita C., Adachi O. Escherichia coli PQQ-containing quinoprotein glucose dehydrogenase: its structure comparison with other quinoproteins. Biochim. Biophys. Acta (BBA)-Proteins Proteomics 2003, 1647:185-192.
    • (2003) Biochim. Biophys. Acta (BBA)-Proteins Proteomics , vol.1647 , pp. 185-192
    • Yamada, M.1    Elias, M.2    Matsushita, K.3    Migita, C.4    Adachi, O.5
  • 80
    • 77954688986 scopus 로고    scopus 로고
    • Pyrroloquinoline quinone biosynthesis in Escherichia coli through expression of the Gluconobacter oxydans pqqABCDE gene cluster
    • Yang X.-P., Zhong G.-F., Lin J.-P., Mao D.-B., Wei D.-Z. Pyrroloquinoline quinone biosynthesis in Escherichia coli through expression of the Gluconobacter oxydans pqqABCDE gene cluster. J. Microbiol. Biotechnol. 2010, 37:575-580.
    • (2010) J. Microbiol. Biotechnol. , vol.37 , pp. 575-580
    • Yang, X.-P.1    Zhong, G.-F.2    Lin, J.-P.3    Mao, D.-B.4    Wei, D.-Z.5
  • 81
    • 84880677911 scopus 로고    scopus 로고
    • Metabolic engineering of Escherichia coli for production of salvianic acid A via an artificial biosynthetic pathway
    • Yao Y.-F., Wang C.-S., Qiao J., Zhao G.-R. Metabolic engineering of Escherichia coli for production of salvianic acid A via an artificial biosynthetic pathway. Metab. Eng. 2013, 19C:79-87.
    • (2013) Metab. Eng. , vol.19 C , pp. 79-87
    • Yao, Y.-F.1    Wang, C.-S.2    Qiao, J.3    Zhao, G.-R.4
  • 82
    • 84858706476 scopus 로고    scopus 로고
    • Characterization of different FAD-dependent glucose dehydrogenases for possible use in glucose-based biosensors and biofuel cells
    • Zafar M.N., Beden N., Leech D., Sygmund C., Ludwig R., Gorton L. Characterization of different FAD-dependent glucose dehydrogenases for possible use in glucose-based biosensors and biofuel cells. Anal. Bioanal. Chem. 2012, 402:2069-2077.
    • (2012) Anal. Bioanal. Chem. , vol.402 , pp. 2069-2077
    • Zafar, M.N.1    Beden, N.2    Leech, D.3    Sygmund, C.4    Ludwig, R.5    Gorton, L.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.