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Volumn 43, Issue 4, 2003, Pages 287-300

Does the detoxification of penicillin side-chain precursors depend on microsomal monooxygenase and glutathione S-transferase in Penicillium chrysogenum?

Author keywords

[No Author keywords available]

Indexed keywords

ARYL HYDROCARBON HYDROXYLASES; GLUTATHIONE; GLUTATHIONE TRANSFERASE; HYDROGEN-ION CONCENTRATION; METABOLIC DETOXICATION, DRUG; PENICILLINS; PENICILLIUM CHRYSOGENUM;

EID: 0042429006     PISSN: 0233111X     EISSN: None     Source Type: Journal    
DOI: 10.1002/jobm.200390032     Document Type: Article
Times cited : (8)

References (53)
  • 1
    • 0022272493 scopus 로고
    • Determination of glutathione and glutathione disulphide in biological samples
    • ANDERSON, M. E., 1985. Determination of glutathione and glutathione disulphide in biological samples. Methods Enzymol., 113, 548-555.
    • (1985) Methods Enzymol. , vol.113 , pp. 548-555
    • Anderson, M.E.1
  • 2
    • 0009546294 scopus 로고
    • The gel-filtration behaviour of proteins related to their molecular weights over a wide range
    • ANDREWS, P., 1965. The gel-filtration behaviour of proteins related to their molecular weights over a wide range. Biochem. J., 96, 222-223.
    • (1965) Biochem. J. , vol.96 , pp. 222-223
    • Andrews, P.1
  • 3
    • 0030464821 scopus 로고    scopus 로고
    • NADP- specific glutamate dehydrogenase of Penicillium chrysogenum has a homohexamer structure
    • BOGÁTI, M. SZ., PÓCSI, I., MATICSEK, J., BOROSS, P., TOZSÉR, J. and SZENTIRMAI, A., 1996. NADP- specific glutamate dehydrogenase of Penicillium chrysogenum has a homohexamer structure. J. Basic Microbiol., 36, 371-375.
    • (1996) J. Basic Microbiol. , vol.36 , pp. 371-375
    • Bogáti, M.Sz.1    Pócsi, I.2    Maticsek, J.3    Boross, P.4    Tozsér, J.5    Szentirmai, A.6
  • 4
    • 0035949436 scopus 로고    scopus 로고
    • Purification and characterization of a glutathione S-transferase from the fungus Cunninghamella elegans
    • CHA, C. J., COLES, B. F. and CERNIGLIA, C. E., 2001. Purification and characterization of a glutathione S-transferase from the fungus Cunninghamella elegans. FEMS Microbiol. Lett., 203, 257-261.
    • (2001) FEMS Microbiol. Lett. , vol.203 , pp. 257-261
    • Cha, C.J.1    Coles, B.F.2    Cerniglia, C.E.3
  • 5
    • 0028223220 scopus 로고
    • Metabolism and cytotoxicity of naphthalene and its metabolites in isolated murine Clara cells
    • CHICHESTER, C. H., BUCKPITT, A. R., CHANG, A. and PLOPPER, C. G., 1994. Metabolism and cytotoxicity of naphthalene and its metabolites in isolated murine Clara cells. Mol. Pharmacol., 45, 664-672.
    • (1994) Mol. Pharmacol. , vol.45 , pp. 664-672
    • Chichester, C.H.1    Buckpitt, A.R.2    Chang, A.3    Plopper, C.G.4
  • 6
    • 0028137113 scopus 로고
    • A robust liquid chromatographic method for measurement of medium components during penicillin fermentations
    • CHRISTENSEN, L. H., MANDRUP, G., NIELSEN, J. and VILLADSEN, J., 1994. A robust liquid chromatographic method for measurement of medium components during penicillin fermentations. Anal. Chim. Acta, 296, 51-62.
    • (1994) Anal. Chim. Acta , vol.296 , pp. 51-62
    • Christensen, L.H.1    Mandrup, G.2    Nielsen, J.3    Villadsen, J.4
  • 7
    • 0027089896 scopus 로고
    • Characterisation of a novel microsomal glutathione S-transferase produced by Aspergillus ochraceus TS
    • DATTA, J. and SAMANTA, T. B., 1992. Characterisation of a novel microsomal glutathione S-transferase produced by Aspergillus ochraceus TS. Mol. Cell Biochem., 118, 31-38.
    • (1992) Mol. Cell Biochem. , vol.118 , pp. 31-38
    • Datta, J.1    Samanta, T.B.2
  • 8
    • 0028033751 scopus 로고
    • Microsomal glutathione S-transferase (GST) isoenzymes in Aspergillus ochraceus TS: Induction by 3-methylcholanthrene
    • DATTA, J., DUTTA, T. K. and SAMATA, T. B., 1994. Microsomal glutathione S-transferase (GST) isoenzymes in Aspergillus ochraceus TS: induction by 3-methylcholanthrene. Biochem. Biophys. Res. Commun., 203, 1508-1514.
    • (1994) Biochem. Biophys. Res. Commun. , vol.203 , pp. 1508-1514
    • Datta, J.1    Dutta, T.K.2    Samata, T.B.3
  • 10
    • 0031007706 scopus 로고    scopus 로고
    • Glutathione S-transferases from the white-rot fungus Phanerochaete chrysosporium
    • DOWD, C. A., BUCKLEY, C. M. and SHEEHAN, D., 1997. Glutathione S-transferases from the white-rot fungus Phanerochaete chrysosporium. Biochem. J., 324, 243-248.
    • (1997) Biochem. J. , vol.324 , pp. 243-248
    • Dowd, C.A.1    Buckley, C.M.2    Sheehan, D.3
  • 11
    • 0032922387 scopus 로고    scopus 로고
    • Variable expression of glutathione S-transferase isoenzymes in the fungus Mucor circinelloides
    • DOWD, C. A. and SHEEHAN, D., 1999. Variable expression of glutathione S-transferase isoenzymes in the fungus Mucor circinelloides. FEMS Microbiol. Lett., 170, 13-17.
    • (1999) FEMS Microbiol. Lett. , vol.170 , pp. 13-17
    • Dowd, C.A.1    Sheehan, D.2
  • 12
    • 0028223899 scopus 로고
    • Regulation of specific activity of glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase in Penicillium chrysogenum
    • EMRI, T., BARTÓK, G. and SZENTIRMAI, A., 1994. Regulation of specific activity of glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase in Penicillium chrysogenum. FEMS Microbiol. Lett., 117, 67-70.
    • (1994) FEMS Microbiol. Lett. , vol.117 , pp. 67-70
    • Emri, T.1    Bartók, G.2    Szentirmai, A.3
  • 13
    • 0030750021 scopus 로고    scopus 로고
    • Phenoxyacetic acid induces glutathione-dependent detoxification and depletes the glutathione pool in Penicillium chrysogenum
    • EMRI, T., PÓCSI, I. and SZENTIRMAI, A., 1997. Phenoxyacetic acid induces glutathione-dependent detoxification and depletes the glutathione pool in Penicillium chrysogenum. J. Basic Microbiol., 37, 181-186.
    • (1997) J. Basic Microbiol. , vol.37 , pp. 181-186
    • Emri, T.1    Pócsi, I.2    Szentirmai, A.3
  • 14
    • 2642595054 scopus 로고    scopus 로고
    • Changes in the glutathione (GSH) metabolism of Penicillium chrysogenum grown on different nitrogen sulphur and carbon sources
    • EMRI, T., PÓCSI, I. and SZENTIRMAI, A., 1998. Changes in the glutathione (GSH) metabolism of Penicillium chrysogenum grown on different nitrogen sulphur and carbon sources. J. Basic Microbiol., 38, 3-8.
    • (1998) J. Basic Microbiol. , vol.38 , pp. 3-8
    • Emri, T.1    Pócsi, I.2    Szentirmai, A.3
  • 15
    • 0345561613 scopus 로고    scopus 로고
    • Analysis of the oxidative stress response of Penicillium chrysogenum to menadione
    • EMRI, T., PÓCSI, I. and SZENTIRMAI, A., 1999a. Analysis of the oxidative stress response of Penicillium chrysogenum to menadione. Free Rad. Res., 26, 125-132.
    • (1999) Free Rad. Res. , vol.26 , pp. 125-132
    • Emri, T.1    Pócsi, I.2    Szentirmai, A.3
  • 16
    • 0344654733 scopus 로고    scopus 로고
    • Co-ordination of the nitrate and nitrite assimilation, the glutathione and free radical metabolism, and the pentose phosphate pathway in Penicillium chrysogenum
    • EMRI, T., SÁMI, L., SZENTIRMAI, A. and PÓCSI, I., 1999b. Co-ordination of the nitrate and nitrite assimilation, the glutathione and free radical metabolism, and the pentose phosphate pathway in Penicillium chrysogenum. J. Basic Microbiol., 39, 109-115.
    • (1999) J. Basic Microbiol. , vol.39 , pp. 109-115
    • Emri, T.1    Sámi, L.2    Szentirmai, A.3    Pócsi, I.4
  • 17
    • 0034077786 scopus 로고    scopus 로고
    • Effect of phenoxyacetic acid on the glutathione metabolism of Penicillium chrysogenum
    • EMRI, T., LEITER, É. and PÓCSI, I., 2000. Effect of phenoxyacetic acid on the glutathione metabolism of Penicillium chrysogenum. J. Basic Microbiol., 40, 93-104.
    • (2000) J. Basic Microbiol. , vol.40 , pp. 93-104
    • Emri, T.1    Leiter, É.2    Pócsi, I.3
  • 18
    • 0034964917 scopus 로고    scopus 로고
    • Penicillin productivity and glutathione-dependent detoxification of phenylacetic and phenoxyacetic acids in Penicillium chrysogenum
    • EMRI, T., LEITER, É., FARKAS, E. and PÓCSI, I., 2001. Penicillin productivity and glutathione-dependent detoxification of phenylacetic and phenoxyacetic acids in Penicillium chrysogenum. J. Basic Microbiol., 41, 67-73.
    • (2001) J. Basic Microbiol. , vol.41 , pp. 67-73
    • Emri, T.1    Leiter, É.2    Farkas, E.3    Pócsi, I.4
  • 19
    • 0028331325 scopus 로고
    • Utilization of side-chain precursors for penicillin biosynthesis in a high-producing strain of P. chrysogenum
    • ERIKSEN, S. H., JENSEN, B., SCHNEIDER, I., KAASGAARD, S. and OLSEN, J., 1994. Utilization of side-chain precursors for penicillin biosynthesis in a high-producing strain of P. chrysogenum. Appl. Microbiol. Biotechnol., 40, 883-887.
    • (1994) Appl. Microbiol. Biotechnol. , vol.40 , pp. 883-887
    • Eriksen, S.H.1    Jensen, B.2    Schneider, I.3    Kaasgaard, S.4    Olsen, J.5
  • 20
    • 0001522673 scopus 로고
    • Starch gel electrophoresis - Application to the classification of pituitary proteins and polypeptides
    • FERGUSON, K. A., 1964. Starch gel electrophoresis - application to the classification of pituitary proteins and polypeptides. Metabolism, 13, 985-1004.
    • (1964) Metabolism , vol.13 , pp. 985-1004
    • Ferguson, K.A.1
  • 21
    • 0029976725 scopus 로고    scopus 로고
    • Involvement of cytochrome P450, glutathione S-transferase, and epoxide hydrolase in the metabolism of aflatoxin B1 and relevance to risk of human liver cancer
    • GUENGERICH, F. P., JOHNSON, W. W., UENG, Y. F., YAMAZAKI, H. and SHIMADA, T., 1996. Involvement of cytochrome P450, glutathione S-transferase, and epoxide hydrolase in the metabolism of aflatoxin B1 and relevance to risk of human liver cancer. Environ. Health Perspect., 104 Suppl. 3, 557-562.
    • (1996) Environ. Health Perspect. , vol.104 , Issue.3 SUPPL. , pp. 557-562
    • Guengerich, F.P.1    Johnson, W.W.2    Ueng, Y.F.3    Yamazaki, H.4    Shimada, T.5
  • 22
    • 0019741605 scopus 로고
    • Assays for differentiation of glutathione S-transferases
    • HABIG, W. H. and JACOBY, W. B., 1981. Assays for differentiation of glutathione S-transferases. Methods Enzymol., 77, 389-405.
    • (1981) Methods Enzymol. , vol.77 , pp. 389-405
    • Habig, W.H.1    Jacoby, W.B.2
  • 23
    • 0032553852 scopus 로고    scopus 로고
    • Modelling of the protonophoric uncoupling by phenoxyacetic acid of the plasma membrane potential of Penicillium chrysogenum
    • HENRIKSEN, C. M., NIELSEN, J. and VILLADSEN, J., 1998a. Modelling of the protonophoric uncoupling by phenoxyacetic acid of the plasma membrane potential of Penicillium chrysogenum. Biotechnol. Bioeng., 60, 761-767.
    • (1998) Biotechnol. Bioeng. , vol.60 , pp. 761-767
    • Henriksen, C.M.1    Nielsen, J.2    Villadsen, J.3
  • 24
    • 0031825078 scopus 로고    scopus 로고
    • High exogenous concentration of phenoxyacetic acid are crucial for a high penicillin V productivity in Penicillium chrysogenum
    • HENRIKSEN, C. M., NIELSEN, J. and VILLADSEN, J., 1998b. High exogenous concentration of phenoxyacetic acid are crucial for a high penicillin V productivity in Penicillium chrysogenum. Microbiology, 144, 2001-2006.
    • (1998) Microbiology , vol.144 , pp. 2001-2006
    • Henriksen, C.M.1    Nielsen, J.2    Villadsen, J.3
  • 25
    • 0026459859 scopus 로고
    • The ATP-dependent glutathione S-conjugate export pump
    • ISHIKAWA, T., 1992. The ATP-dependent glutathione S-conjugate export pump. Trends Biochem. Sci., 17, 463-468.
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 463-468
    • Ishikawa, T.1
  • 26
    • 0033011878 scopus 로고    scopus 로고
    • Common structural features of MAPEG - A widespread superfamily of membrane associated proteins with highly divergent functions in eicosanoid and glutathione metabolism
    • JAKOBSSON, P. J., MORGENSTERN, R., MANCINI, J., FORD-HUTCHINSON, A. and PERSSON, B., 1999. Common structural features of MAPEG - a widespread superfamily of membrane associated proteins with highly divergent functions in eicosanoid and glutathione metabolism. Protein Sci., 8, 689-692.
    • (1999) Protein Sci. , vol.8 , pp. 689-692
    • Jakobsson, P.J.1    Morgenstern, R.2    Mancini, J.3    Ford-Hutchinson, A.4    Persson, B.5
  • 28
    • 0017447640 scopus 로고
    • Meiotic and mitotic recombination in Aspergillus and its chromosomal aberrations
    • KÄFER, E., 1977. Meiotic and mitotic recombination in Aspergillus and its chromosomal aberrations. Adv. Genet., 19, 33-131.
    • (1977) Adv. Genet. , vol.19 , pp. 33-131
    • Käfer, E.1
  • 29
    • 0030605127 scopus 로고    scopus 로고
    • Effects of the structure of a toxicokinetic model of butadiene inhalation exposure on computed production of carcinogenic intermediates
    • KOHN, M. C. and MELNICK, R. L., 1996. Effects of the structure of a toxicokinetic model of butadiene inhalation exposure on computed production of carcinogenic intermediates. Toxicology, 113, 31-39.
    • (1996) Toxicology , vol.113 , pp. 31-39
    • Kohn, M.C.1    Melnick, R.L.2
  • 30
    • 0018878263 scopus 로고
    • Resolution, purification and some properties of three glutathione transferases from rat liver mitochondria
    • KRAUS, P., 1980. Resolution, purification and some properties of three glutathione transferases from rat liver mitochondria. Hoppe Seylers Z. Physiol. Chem., 361, 9-15.
    • (1980) Hoppe Seylers Z. Physiol. Chem. , vol.361 , pp. 9-15
    • Kraus, P.1
  • 31
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • LAEMMLI, U. K., 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 32
    • 0023517606 scopus 로고
    • Identification of multiple glutathione S-transferases from Daphnia magna
    • LEBLANC, G. A. and COCHRANE, B. J., 1987. Identification of multiple glutathione S-transferases from Daphnia magna. Comp. Biochem. Physiol., 88B, 39-45.
    • (1987) Comp. Biochem. Physiol. , vol.88 B , pp. 39-45
    • Leblanc, G.A.1    Cochrane, B.J.2
  • 33
    • 0035504267 scopus 로고    scopus 로고
    • γ-glutamyl transpeptidase in the yeast Saccharomyces cerevisiae and its role in the vacuolar transport and metabolism of glutathione
    • MEHDI, K., THIERE, J. and PENNINCKX, M. J., 2001. γ-Glutamyl transpeptidase in the yeast Saccharomyces cerevisiae and its role in the vacuolar transport and metabolism of glutathione. Biochem. J., 359, 631-637.
    • (2001) Biochem. J. , vol.359 , pp. 631-637
    • Mehdi, K.1    Thiere, J.2    Penninckx, M.J.3
  • 34
    • 0040559975 scopus 로고    scopus 로고
    • Disruption of phacA, an Aspergillus nidulans gene encoding a novel cytochrome p450 monooxygenase catalyzing phenylacetate 2-hydroxylation, results in penicillin overproduction
    • MINGOT, J. M., PEÑALVA, M. A. and FERNÁNDEZ-CAÑON, J. M., 1999. Disruption of phacA, an Aspergillus nidulans gene encoding a novel cytochrome p450 monooxygenase catalyzing phenylacetate 2-hydroxylation, results in penicillin overproduction. J. Biol. Chem., 274, 14545-14550.
    • (1999) J. Biol. Chem. , vol.274 , pp. 14545-14550
    • Mingot, J.M.1    Peñalva, M.A.2    Fernández-Cañon, J.M.3
  • 37
    • 0034951909 scopus 로고    scopus 로고
    • β-galactosidase of Penicillium chrysogenum: Production, purification, and characterization of the enzyme
    • NAGY, Z., KISS, T., SZENTIRMAI, A. and BIRO, S., 2001. β-Galactosidase of Penicillium chrysogenum: production, purification, and characterization of the enzyme. Protein Expr. Purif., 21, 24-29.
    • (2001) Protein Expr. Purif. , vol.21 , pp. 24-29
    • Nagy, Z.1    Kiss, T.2    Szentirmai, A.3    Biro, S.4
  • 38
    • 0027412924 scopus 로고
    • Metabolism and functions of glutathione in microorganisms
    • PENNINCKX, M. J. and ELSKENS, M. T., 1993. Metabolism and functions of glutathione in microorganisms. Adv. Microbial. Physiol., 34, 239-301.
    • (1993) Adv. Microbial. Physiol. , vol.34 , pp. 239-301
    • Penninckx, M.J.1    Elskens, M.T.2
  • 39
    • 0020669405 scopus 로고
    • Determination of total protein
    • PETERSON, G. L., 1983. Determination of total protein. Methods Enzymol., 91, 86-105.
    • (1983) Methods Enzymol. , vol.91 , pp. 86-105
    • Peterson, G.L.1
  • 40
    • 0023761561 scopus 로고
    • Kinetic studies on the broad-specificity β-D-glucosidase from pig kidney
    • PÓCSI, I. and KISS, L., 1988. Kinetic studies on the broad-specificity β-D-glucosidase from pig kidney. Biochem. J., 256, 139-146.
    • (1988) Biochem. J. , vol.256 , pp. 139-146
    • Pócsi, I.1    Kiss, L.2
  • 41
    • 84985200222 scopus 로고
    • The formation of N-acetyl-β-D-hexosaminidase is repressed by glucose in Penicillium chrysogenum
    • PÓCSI, I., PUSZTAHELYI, T., BOGÁTI, M. SZ. and SZENTIRMAI, A., 1993. The formation of N-acetyl-β-D-hexosaminidase is repressed by glucose in Penicillium chrysogenum. J. Basic Microbiol., 33, 259-267.
    • (1993) J. Basic Microbiol. , vol.33 , pp. 259-267
    • Pócsi, I.1    Pusztahelyi, T.2    Bogáti, M.Sz.3    Szentirmai, A.4
  • 42
    • 0035752048 scopus 로고    scopus 로고
    • The glutathione metabolism of the β-lactam producer filamentous fungus Penicillium chrysogenum
    • PÓCSI, I., EMRI, T., SÁMI, L., LEITER, É. and SZENTIRMAI, A., 2001. The glutathione metabolism of the β-lactam producer filamentous fungus Penicillium chrysogenum. Acta Microbiol. Immunol. Hung., 48, 393-411.
    • (2001) Acta Microbiol. Immunol. Hung. , vol.48 , pp. 393-411
    • Pócsi, I.1    Emri, T.2    Sámi, L.3    Leiter, É.4    Szentirmai, A.5
  • 43
    • 0034836582 scopus 로고    scopus 로고
    • Reduced function of a phenylacetate-oxidizing cytochrome P450 caused strong genetic improvement in early phylogeny of penicillin-producing strains
    • RODRÍGUEZ-SÁIZ, M., BARREDO, J. L., MORENO, M. A., FERNÁNDEZ-CAÑON, J. M., PEÑALVA, M. A. and DÍEZ, B., 2001. Reduced function of a phenylacetate-oxidizing cytochrome P450 caused strong genetic improvement in early phylogeny of penicillin-producing strains. J. Bacteriol., 183, 5465-5471.
    • (2001) J. Bacteriol. , vol.183 , pp. 5465-5471
    • Rodríguez-Sáiz, M.1    Barredo, J.L.2    Moreno, M.A.3    Fernández-Cañon, J.M.4    Peñalva, M.A.5    Díez, B.6
  • 44
    • 0035207154 scopus 로고    scopus 로고
    • Autolysis and aging of Penicillium chrysogenum cultures under carbon starvation: Chitinase production and antifungal effect of allosamidin
    • SÁMI, L., PUSZTAHELYI, T., EMRI, T., VARECZA, Z., FEKETE, A., GRALLERT, Á, KARANYI, Z., KISS, L. and PÓCSI, I., 2001. Autolysis and aging of Penicillium chrysogenum cultures under carbon starvation: Chitinase production and antifungal effect of allosamidin. J. Gen. Appl. Microbiol., 47, 201-211.
    • (2001) J. Gen. Appl. Microbiol. , vol.47 , pp. 201-211
    • Sámi, L.1    Pusztahelyi, T.2    Emri, T.3    Varecza, Z.4    Fekete, A.5    Grallert, Á.6    Karanyi, Z.7    Kiss, L.8    Pócsi, I.9
  • 45
    • 0023791460 scopus 로고
    • Positive correlation exists between glutathione S-transferase activity and aflatoxin formation in Aspergillus flavus
    • SAXENA, M., MUKERJI, K. G. and RAJ, H. G., 1988. Positive correlation exists between glutathione S-transferase activity and aflatoxin formation in Aspergillus flavus. Biochem. J., 254, 567-570.
    • (1988) Biochem. J. , vol.254 , pp. 567-570
    • Saxena, M.1    Mukerji, K.G.2    Raj, H.G.3
  • 46
    • 0025924285 scopus 로고
    • Epoxidation of aflatoxin B1 by Aspergillus flavus microsomes in vitro: Interaction with DNA and formation of aflatoxin B1-glutathione conjugate
    • SAXENA, M., ALLAMEH, A., MUKERJI, K. G. and RAJ, H. G., 1991. Epoxidation of aflatoxin B1 by Aspergillus flavus microsomes in vitro: interaction with DNA and formation of aflatoxin B1-glutathione conjugate. Chem. Biol. Interact., 78, 13-22.
    • (1991) Chem. Biol. Interact. , vol.78 , pp. 13-22
    • Saxena, M.1    Allameh, A.2    Mukerji, K.G.3    Raj, H.G.4
  • 47
    • 0027439463 scopus 로고
    • Microbial glutathione S-transferases
    • SHEEHAN, D. and CASEY, J. P., 1993. Microbial glutathione S-transferases. Comp. Biochem. Physiol., 104B, 1-6.
    • (1993) Comp. Biochem. Physiol. , vol.104 B , pp. 1-6
    • Sheehan, D.1    Casey, J.P.2
  • 48
    • 0035890484 scopus 로고    scopus 로고
    • Structure, function and evaluation of glutathione transferases: Implications for classification of non-mammalian members of an ancient enzyme superfamily
    • SHEEHAN, D., MEADE, G., FOLEY, V. M. and DOWD, C. A., 2001. Structure, function and evaluation of glutathione transferases: implications for classification of non-mammalian members of an ancient enzyme superfamily. Biochem. J., 360, 1-16.
    • (2001) Biochem. J. , vol.360 , pp. 1-16
    • Sheehan, D.1    Meade, G.2    Foley, V.M.3    Dowd, C.A.4
  • 49
    • 0019760046 scopus 로고
    • Purification of glutathione S-transferases by glutathione-affinity chromatography
    • SIMONS, P. and VAN DER JAGT, D. L., 1981. Purification of glutathione S-transferases by glutathione-affinity chromatography. Methods Enzymol., 77, 235-237.
    • (1981) Methods Enzymol. , vol.77 , pp. 235-237
    • Simons, P.1    Van Der Jagt, D.L.2
  • 50
    • 0024015336 scopus 로고
    • Glutathione formation in Penicillium chrysogenum: Stimulatory effect of ammonium
    • SCHWARTZ, R., LUCAS, M. T., ESCALANTE, L., VÁZQUEZ, G. and SÁNCHEZ, S., 1988. Glutathione formation in Penicillium chrysogenum: Stimulatory effect of ammonium. J. Gen. Microbiol., 134, 1117-1121.
    • (1988) J. Gen. Microbiol. , vol.134 , pp. 1117-1121
    • Schwartz, R.1    Lucas, M.T.2    Escalante, L.3    Vázquez, G.4    Sánchez, S.5
  • 51
    • 0032958467 scopus 로고    scopus 로고
    • Expression of two glutathione S-transferase genes in the yeast Issatchenkia orientalis is induced by o-dinitrobenzene during cell growth arrest
    • TAMAKI, H., YAMAMOTO, K. and KUMAGAI, H., 1999. Expression of two glutathione S-transferase genes in the yeast Issatchenkia orientalis is induced by o-dinitrobenzene during cell growth arrest. J. Bacteriol., 181, 2958-2962.
    • (1999) J. Bacteriol. , vol.181 , pp. 2958-2962
    • Tamaki, H.1    Yamamoto, K.2    Kumagai, H.3
  • 52
    • 0033019615 scopus 로고    scopus 로고
    • Metabolic control analysis of the penicillin biosynthetic pathway: The influence of the LLD-ACV:bisACV ratio on the flux control
    • THEILGAARD, H. A. and NIELSEN, J., 1999. Metabolic control analysis of the penicillin biosynthetic pathway: the influence of the LLD-ACV:bisACV ratio on the flux control. Antonie van Leeuwenhoek, 75, 145-154.
    • (1999) Antonie van Leeuwenhoek , vol.75 , pp. 145-154
    • Theilgaard, H.A.1    Nielsen, J.2
  • 53
    • 0033020288 scopus 로고    scopus 로고
    • Compartmentalization and transport in β-lactam antibiotic biosynthesis by filamentous fungi
    • VAN DE KAMP, M., DRIESSEN, A. J. M. and KONINGS, W. N., 1999. Compartmentalization and transport in β-lactam antibiotic biosynthesis by filamentous fungi. Antonie van Leeuwenhoek, 75, 41-78.
    • (1999) Antonie van Leeuwenhoek , vol.75 , pp. 41-78
    • Van De Kamp, M.1    Driessen, A.J.M.2    Konings, W.N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.