메뉴 건너뛰기




Volumn 65, Issue 9, 1999, Pages 3867-3872

Enzymatic formation of G-group aflatoxins and biosynthetic relationship between G- and B-group aflatoxins

Author keywords

[No Author keywords available]

Indexed keywords

AFLATOXIN B; AFLATOXIN B1; AFLATOXIN B2; AFLATOXIN G1; AFLATOXIN G2; CYTOCHROME P450; ETHOXYQUIN; FUNGAL PROTEIN; GENE PRODUCT; IMIDAZOLE; METYRAPONE; MICROSOME ENZYME; PROADIFEN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; STERIGMATOCYSTIN; UNSPECIFIC MONOOXYGENASE;

EID: 0032875828     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/aem.65.9.3867-3872.1999     Document Type: Article
Times cited : (47)

References (39)
  • 1
    • 84985226093 scopus 로고
    • Regulation of aflatoxin biosynthesis: Induction of aflatoxin by various carbohydrates
    • Abdollahi, A., and R. L. Buchanan. 1981. Regulation of aflatoxin biosynthesis: induction of aflatoxin by various carbohydrates. J Food Sci. 46:633-635.
    • (1981) J Food Sci. , vol.46 , pp. 633-635
    • Abdollahi, A.1    Buchanan, R.L.2
  • 3
    • 84907134099 scopus 로고
    • The isolation of mutants of Aspergillus flavus and A. parasiticus with altered aflatoxin producing ability
    • Bennett, J. W. and L. A. Goldblatt. 1973. The isolation of mutants of Aspergillus flavus and A. parasiticus with altered aflatoxin producing ability. Sabouraudia 11:235-241.
    • (1973) Sabouraudia , vol.11 , pp. 235-241
    • Bennett, J.W.1    Goldblatt, L.A.2
  • 5
    • 0000286404 scopus 로고
    • Oxidation-reduction reactions in biosynthesis of secondary metabolites
    • D. Bhatnagar, E. B. Lillehoj, and D. K. Arora (ed.), Marcel Dekker, Inc., New York, N.Y.
    • Bhatnagar, D., K. C. Erlich, and T. E. Cleveland. 1992. Oxidation-reduction reactions in biosynthesis of secondary metabolites, p. 255-286. In D. Bhatnagar, E. B. Lillehoj, and D. K. Arora (ed.), Handbook of applied mycology, vol. 5. Marcel Dekker, Inc., New York, N.Y.
    • (1992) Handbook of Applied Mycology , vol.5 , pp. 255-286
    • Bhatnagar, D.1    Erlich, K.C.2    Cleveland, T.E.3
  • 7
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 9
    • 0023903976 scopus 로고
    • Enzymes and aflatoxin biosynthesis
    • Dutton, M. F. 1988. Enzymes and aflatoxin biosynthesis. Microbiol. Rev. 52:274-295.
    • (1988) Microbiol. Rev. , vol.52 , pp. 274-295
    • Dutton, M.F.1
  • 11
    • 51249180096 scopus 로고
    • 14C labeled aflatoxins and incorporation of unlabelled aflatoxin in a blocked versicolorin a accumulating mutant of Aspergillus parasiticus
    • 14C labeled aflatoxins and incorporation of unlabelled aflatoxin in a blocked versicolorin A accumulating mutant of Aspergillus parasiticus. J. Am. Oil Chem. Soc. 58:956A-959A.
    • (1981) J. Am. Oil Chem. Soc. , vol.58
    • Floyd, J.C.1    Bennett, J.W.2
  • 12
    • 84985161371 scopus 로고
    • Effects of ethoxyquin on aflatoxin-producing strains of Aspergillus parasiticus and A. flavus
    • Foudin, A. S., L. L. Leaich, and J. C. Ayres. 1978. Effects of ethoxyquin on aflatoxin-producing strains of Aspergillus parasiticus and A. flavus. J. Food Sci. 43:731-734.
    • (1978) J. Food Sci. , vol.43 , pp. 731-734
    • Foudin, A.S.1    Leaich, L.L.2    Ayres, J.C.3
  • 14
    • 0017379332 scopus 로고
    • 5,6-Dimethyoxysterigmatocystin, a new metabolite from Aspergillus multicolor
    • Hamasaki, T., T. Nakagomi, Y. Hatsuda, K. Fukuyama, and Y. Katsube. 1977. 5,6-Dimethyoxysterigmatocystin, a new metabolite from Aspergillus multicolor. Tetrahedron Lett. 1977:2765-2766.
    • (1977) Tetrahedron Lett. , vol.1977 , pp. 2765-2766
    • Hamasaki, T.1    Nakagomi, T.2    Hatsuda, Y.3    Fukuyama, K.4    Katsube, Y.5
  • 16
    • 0006668210 scopus 로고
    • Biosynthesis of aflatoxins. part II
    • London
    • Heathcote, J. G., M. F. Dutton, and J. R. Hibbert. 1976. Biosynthesis of aflatoxins. part II. Chem. Ind. (London) 20:270-272.
    • (1976) Chem. Ind. , vol.20 , pp. 270-272
    • Heathcote, J.G.1    Dutton, M.F.2    Hibbert, J.R.3
  • 18
    • 0014720177 scopus 로고
    • Taxonomic studies of the aflatoxin producing strains in the Aspergillus flavus group
    • Hesseltine, C. W., W. G. Sorenson, and M. Smith. 1970. Taxonomic studies of the aflatoxin producing strains in the Aspergillus flavus group. Mycologia 62:123-132.
    • (1970) Mycologia , vol.62 , pp. 123-132
    • Hesseltine, C.W.1    Sorenson, W.G.2    Smith, M.3
  • 19
    • 0014196737 scopus 로고
    • Reconversion of detergent- And sulfhydryl reagent-produced P-420 to P-450 by polyols and glutathione
    • Ichikawa, Y., and T. Yamamoto. 1967. Reconversion of detergent- and sulfhydryl reagent-produced P-420 to P-450 by polyols and glutathione. Biochim. Biophys. Acta 131:490.
    • (1967) Biochim. Biophys. Acta , vol.131 , pp. 490
    • Ichikawa, Y.1    Yamamoto, T.2
  • 20
    • 0023770812 scopus 로고
    • Constitutive testosterone 6b-hydroxylase in rat liver
    • Imaoka, S., Y. Terano, and Y. Funane. 1988. Constitutive testosterone 6b-hydroxylase in rat liver. J. Biochem. 104:481-487.
    • (1988) J. Biochem. , vol.104 , pp. 481-487
    • Imaoka, S.1    Terano, Y.2    Funane, Y.3
  • 21
    • 0016367332 scopus 로고
    • Permeability properties of liposomes prepared from dipalmitoyllecithin, dimyristoyllecithin, egg lecithin, rat liver lecithin and beef brain sphingomyelin
    • Inoue, K. 1974. Permeability properties of liposomes prepared from dipalmitoyllecithin, dimyristoyllecithin, egg lecithin, rat liver lecithin and beef brain sphingomyelin. Biochim. Biophys. Acta 339:390-402.
    • (1974) Biochim. Biophys. Acta , vol.339 , pp. 390-402
    • Inoue, K.1
  • 23
    • 0028290192 scopus 로고
    • Purification and characterization of two versiconal hemiacetal acetate reductases involved in aflatoxin biosynthesis
    • Matsushima, K., Y. Ando, T. Hamasaki, and K. Yabe. 1994. Purification and characterization of two versiconal hemiacetal acetate reductases involved in aflatoxin biosynthesis. Appl. Environ. Microbiol. 60:2561-2567.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 2561-2567
    • Matsushima, K.1    Ando, Y.2    Hamasaki, T.3    Yabe, K.4
  • 24
    • 0030946049 scopus 로고    scopus 로고
    • Ord1, an oxidoreductase gene responsible for the conversion of O-methylsterigmatocystin to aflatoxin in Aspergillus flavus
    • Prieto, R., and C. P. Woloshuk. 1997. ord1, an oxidoreductase gene responsible for the conversion of O-methylsterigmatocystin to aflatoxin in Aspergillus flavus. Appl. Environ. Microbiol. 63:1661-1666.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 1661-1666
    • Prieto, R.1    Woloshuk, C.P.2
  • 25
    • 0001783791 scopus 로고
    • The biosynthesis of aflatoxin and its congeners
    • P. S. Steyn (ed.), Academic Press, New York, N.Y.
    • Steyn, P. S., R. Vleggaar, and P. L. Wessels. 1980. The biosynthesis of aflatoxin and its congeners, p. 105-155. In P. S. Steyn (ed.), The biosynthesis of mycotoxins. Academic Press, New York, N.Y.
    • (1980) The Biosynthesis of Mycotoxins , pp. 105-155
    • Steyn, P.S.1    Vleggaar, R.2    Wessels, P.L.3
  • 26
    • 0029006805 scopus 로고
    • Molecular biology of aflatoxin biosynthesis
    • Trail, F., N. Mahanti, and J. Linz. 1995. Molecular biology of aflatoxin biosynthesis. Microbiology 141:755-765.
    • (1995) Microbiology , vol.141 , pp. 755-765
    • Trail, F.1    Mahanti, N.2    Linz, J.3
  • 28
    • 0032521312 scopus 로고    scopus 로고
    • Genetic organization and function of the aflatoxin B1 biosynthetic genes
    • Woloshuk, C. P., and R. Prieto. 1998. Genetic organization and function of the aflatoxin B1 biosynthetic genes. FEMS Microbiol. Lett. 160:169-176.
    • (1998) FEMS Microbiol. Lett. , vol.160 , pp. 169-176
    • Woloshuk, C.P.1    Prieto, R.2
  • 29
    • 0017093791 scopus 로고
    • Metabolism of benzo[a]pyrene and benzo-[a]pyrenederivatives to mutagenic products by highly purified hepatic microsomal enzymes
    • Wood, A. W., W. Levin, A. Y. H. Lu, H. Yagi, O. Hernandez, D. M. Jerina, and A. H. Conney. 1976. Metabolism of benzo[a]pyrene and benzo-[a]pyrenederivatives to mutagenic products by highly purified hepatic microsomal enzymes. J. Biol. Chem. 251:4882-4890.
    • (1976) J. Biol. Chem. , vol.251 , pp. 4882-4890
    • Wood, A.W.1    Levin, W.2    Lu, A.Y.H.3    Yagi, H.4    Hernandez, O.5    Jerina, D.M.6    Conney, A.H.7
  • 30
    • 0345183516 scopus 로고    scopus 로고
    • Unpublished data
    • Yabe, K. Unpublished data.
    • Yabe, K.1
  • 33
    • 0025953938 scopus 로고
    • A metabolic grid among versiconal hemiacetal acetate, versiconol acetate, versiconol, and versiconal during aflatoxin biosynthesis
    • Yabe, K., Y. Ando, and T. Hamasaki. 1991. A metabolic grid among versiconal hemiacetal acetate, versiconol acetate, versiconol, and versiconal during aflatoxin biosynthesis. J. Gen. Microbiol. 137:2469-2475.
    • (1991) J. Gen. Microbiol. , vol.137 , pp. 2469-2475
    • Yabe, K.1    Ando, Y.2    Hamasaki, T.3
  • 35
    • 0027202731 scopus 로고
    • Stereochemistry during aflatoxin biosynthesis. II. Cyclase reaction in the conversion of versiconal to versicolorin B and racemization of versiconal hemiacetal acetate
    • Yabe, K., and T. Hamasaki. 1993. Stereochemistry during aflatoxin biosynthesis. II. Cyclase reaction in the conversion of versiconal to versicolorin B and racemization of versiconal hemiacetal acetate. Appl. Environ. Microbiol. 59:2493-2500.
    • (1993) Appl. Environ. Microbiol. , vol.59 , pp. 2493-2500
    • Yabe, K.1    Hamasaki, T.2
  • 36
    • 0027304898 scopus 로고
    • Stereochemistry during aflatoxin biosynthesis: Conversion of norsolorinic acid to averufin
    • Yabe, K., Y. Matsuyama, Y. Ando, H. Nakajima, and T. Hamasaki. 1993. Stereochemistry during aflatoxin biosynthesis: conversion of norsolorinic acid to averufin. Appl. Environ. Microbiol. 59:2486-2492.
    • (1993) Appl. Environ. Microbiol. , vol.59 , pp. 2486-2492
    • Yabe, K.1    Matsuyama, Y.2    Ando, Y.3    Nakajima, H.4    Hamasaki, T.5
  • 37
    • 0023806863 scopus 로고
    • Isolation and characterization of Aspergillus parasiticus mutants with impaired aflatoxin production by a novel tip culture method
    • Yabe, K., H. Nakamura, Y. Ando, N. Terakado, H. Nakajima, and T. Hamasaki. 1988. Isolation and characterization of Aspergillus parasiticus mutants with impaired aflatoxin production by a novel tip culture method. Appl. Environ. Microbiol. 54:2096-2100.
    • (1988) Appl. Environ. Microbiol. , vol.54 , pp. 2096-2100
    • Yabe, K.1    Nakamura, H.2    Ando, Y.3    Terakado, N.4    Nakajima, H.5    Hamasaki, T.6
  • 38
    • 0025876250 scopus 로고
    • Enzymatic conversion of norsolorinic acid to averufin in aflatoxin biosynthesis
    • Yabe, K., N. Nakamura, H. Nakajima, Y. Ando, and T. Hamasaki. 1991. Enzymatic conversion of norsolorinic acid to averufin in aflatoxin biosynthesis. Appl. Environ. Microbiol. 57:1340-1345.
    • (1991) Appl. Environ. Microbiol. , vol.57 , pp. 1340-1345
    • Yabe, K.1    Nakamura, N.2    Nakajima, H.3    Ando, Y.4    Hamasaki, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.