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Volumn 142, Issue 12, 1996, Pages 3399-3406

Allophane increases the protein levels of several cephamycin biosynthetic enzymes in Nocardia lactamdurans

Author keywords

Allophane; Cephamycin; Nocardia lactamdurans; Phosphate control; Synthesis and degradation of enzymes

Indexed keywords

ANTIBODY; BACTERIAL ENZYME; CARBAMOYLTRANSFERASE; CEPHAMYCIN; ISOPENICILLIN N SYNTHETASE; LYSINE 6 AMINOTRANSFERASE; METHYLTRANSFERASE; OXYGENASE; PHOSPHATE; SYNTHETASE;

EID: 0030470447     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/13500872-142-12-3399     Document Type: Article
Times cited : (7)

References (34)
  • 1
    • 0018427698 scopus 로고
    • Nitrogen nutrition and regulation of cephalosporin production in Streptomyces clavuligerus
    • Aharonowitz, Y. & Demain, A. L. (1979). Nitrogen nutrition and regulation of cephalosporin production in Streptomyces clavuligerus. Can J Microbiol 25, 61-67.
    • (1979) Can J Microbiol , vol.25 , pp. 61-67
    • Aharonowitz, Y.1    Demain, A.L.2
  • 2
    • 0026800606 scopus 로고
    • Penicillin and cephalosporin biosynthetic genes: Structure, organization, regulation and evolution
    • Aharonowitz, Y., Cohen, G. & Martín, J. F. (1992). Penicillin and cephalosporin biosynthetic genes: structure, organization, regulation and evolution. Annu Rev Microbiol 46, 461-496.
    • (1992) Annu Rev Microbiol , vol.46 , pp. 461-496
    • Aharonowitz, Y.1    Cohen, G.2    Martín, J.F.3
  • 3
    • 0025195486 scopus 로고
    • Phosphate control of pabS gene transcription during candicidin biosynthesis
    • Asturias, J. A., Liras, P. & Martín, J. F. (1990). Phosphate control of pabS gene transcription during candicidin biosynthesis. Gene 93, 79-84.
    • (1990) Gene , vol.93 , pp. 79-84
    • Asturias, J.A.1    Liras, P.2    Martín, J.F.3
  • 4
    • 0025910809 scopus 로고
    • The cephamycin biosynthetic genes pcbAB, encoding a large multi-domain peptide synthase, and pcbC of Nocardia lactamdurans are clustered together in an organization different from the same genes in Acremonium chrysogenum and Penicillium chrysogenum
    • Coque, J. J. R., Martín, J. F., Calzada, J. G. & Liras, P. (1991a). The cephamycin biosynthetic genes pcbAB, encoding a large multi-domain peptide synthase, and pcbC of Nocardia lactamdurans are clustered together in an organization different from the same genes in Acremonium chrysogenum and Penicillium chrysogenum. Mol Microbiol 5, 1125-1133.
    • (1991) Mol Microbiol , vol.5 , pp. 1125-1133
    • Coque, J.J.R.1    Martín, J.F.2    Calzada, J.G.3    Liras, P.4
  • 5
    • 0025951613 scopus 로고
    • A gene encoding lysine 6-aminotransferase which forms α-aminoadipic acid, a precursor of β-lactam antibiotics, is located in the cluster of cephamycin biosynthetic genes in Nocardia lactamdurans
    • Coque, J. J. R., Liras, P., Láiz, L & Martín, J. F. (1991b). A gene encoding lysine 6-aminotransferase which forms α-aminoadipic acid, a precursor of β-lactam antibiotics, is located in the cluster of cephamycin biosynthetic genes in Nocardia lactamdurans. J Bacteriol 173, 6258-6264.
    • (1991) J Bacteriol , vol.173 , pp. 6258-6264
    • Coque, J.J.R.1    Liras, P.2    Láiz, L.3    Martín, J.F.4
  • 6
    • 0027525974 scopus 로고
    • Genes for a β-lactamase, a penicillin-binding protein and a transmembrane protein are clustered with the cephamycin biosynthetic genes in Nocardia lactamdurans
    • Coque, J. J. R., Liras, P. & Martín, J. F. (1993a). Genes for a β-lactamase, a penicillin-binding protein and a transmembrane protein are clustered with the cephamycin biosynthetic genes in Nocardia lactamdurans. EMBO J 12, 631-639.
    • (1993) EMBO J , vol.12 , pp. 631-639
    • Coque, J.J.R.1    Liras, P.2    Martín, J.F.3
  • 7
    • 0027402666 scopus 로고
    • Characterization and expression in Streptomyces linidans of cefD and cefE genes from Nocardia lactamdurans: The organization of the cephamycin gene cluster differs from that in Streptomyces clavuligerus
    • Coque, J. J. R., Martin, J. F. & Liras, P. (1993b). Characterization and expression in Streptomyces linidans of cefD and cefE genes from Nocardia lactamdurans: the organization of the cephamycin gene cluster differs from that in Streptomyces clavuligerus. Mol Gen Genet 236, 453-458.
    • (1993) Mol Gen Genet , vol.236 , pp. 453-458
    • Coque, J.J.R.1    Martin, J.F.2    Liras, P.3
  • 8
    • 0029126219 scopus 로고
    • Characterization of the cmcH genes of Nocardia lactamdurans and Streptomyces clavuligerus encoding a functional 3′-hydroxymethylcephem O-carbamoyltransferase from cephamycin biosynthesis
    • Coque, J. J. R., Pérez-Llarena, F. J., Enguita, F. J., de la Fuente, J. L., Martín, J. F. & Liras, P. (1995a). Characterization of the cmcH genes of Nocardia lactamdurans and Streptomyces clavuligerus encoding a functional 3′-hydroxymethylcephem O-carbamoyltransferase from cephamycin biosynthesis. Gene 162, 21-27.
    • (1995) Gene , vol.162 , pp. 21-27
    • Coque, J.J.R.1    Pérez-Llarena, F.J.2    Enguita, F.J.3    De La Fuente, J.L.4    Martín, J.F.5    Liras, P.6
  • 9
    • 0028986367 scopus 로고
    • A two-protein component 7α-cephem-methoxylase encoded by two genes of the cephamycin C cluster converts cephalosporin to 7-methoxycephalosporin C
    • Coque, J. J. R., Enguita, F. J., Martín, J. F. & Liras, P. (1995b). A two-protein component 7α-cephem-methoxylase encoded by two genes of the cephamycin C cluster converts cephalosporin to 7-methoxycephalosporin C. J Bacteriol 177, 2230-2235.
    • (1995) J Bacteriol , vol.177 , pp. 2230-2235
    • Coque, J.J.R.1    Enguita, F.J.2    Martín, J.F.3    Liras, P.4
  • 10
    • 0030019447 scopus 로고    scopus 로고
    • Characterization of the cefF gene of Nocardia lactamdurans encoding a 3′-methylcephem hydroxylase different from the 7-cephem hydroxylase
    • Coque, J. J. R., Enguita, F. J., Cardoza, R. E., Martín, J. F. & Liras, P. (1996a). Characterization of the cefF gene of Nocardia lactamdurans encoding a 3′-methylcephem hydroxylase different from the 7-cephem hydroxylase. Appl Microbiol Biotechnol 44, 605-609.
    • (1996) Appl Microbiol Biotechnol , vol.44 , pp. 605-609
    • Coque, J.J.R.1    Enguita, F.J.2    Cardoza, R.E.3    Martín, J.F.4    Liras, P.5
  • 11
    • 0029846299 scopus 로고    scopus 로고
    • Overexpression of the Nocardia lactamdurans α-aminoadipyl-cysteinyl-valine synthase in Streptomyces lividans. The purified multienzyme uses cystathione and 6-oxopiperidine-2-carboxylate as substrates for synthesis of the tripeptide
    • in press
    • Coque, J. J. R., de la Fuente, J. L., Liras, P. & Martín, J. F. (1996b). Overexpression of the Nocardia lactamdurans α-aminoadipyl-cysteinyl-valine synthase in Streptomyces lividans. The purified multienzyme uses cystathione and 6-oxopiperidine-2-carboxylate as substrates for synthesis of the tripeptide. Eur J Biochem (in press).
    • (1996) Eur J Biochem
    • Coque, J.J.R.1    De La Fuente, J.L.2    Liras, P.3    Martín, J.F.4
  • 12
    • 0022536213 scopus 로고
    • Glucose regulation of cephamycin biosynthesis in Streptomyces lactamdurans is exerted on the formation of α-aminoadipyl-cysteinyl-valine and deacetoxycephalosporin C synthase
    • Cortés, J., Liras, P., Castro, J. M. & Martín, J. F. (1986). Glucose regulation of cephamycin biosynthesis in Streptomyces lactamdurans is exerted on the formation of α-aminoadipyl-cysteinyl-valine and deacetoxycephalosporin C synthase. J Gen Microbiol 132, 1805-1814.
    • (1986) J Gen Microbiol , vol.132 , pp. 1805-1814
    • Cortés, J.1    Liras, P.2    Castro, J.M.3    Martín, J.F.4
  • 13
    • 0027483510 scopus 로고
    • The pab gene of Streptomyces griseus, encoding p-aminobenzoic acid synthase, is located between genes possibly involved in candicidin biosynthesis
    • Criado, L. M., Martín, J. F. & Gil, J. A. (1993). The pab gene of Streptomyces griseus, encoding p-aminobenzoic acid synthase, is located between genes possibly involved in candicidin biosynthesis. Gene 126, 135-139.
    • (1993) Gene , vol.126 , pp. 135-139
    • Criado, L.M.1    Martín, J.F.2    Gil, J.A.3
  • 14
    • 12644262482 scopus 로고    scopus 로고
    • Interaction of the two proteins of the methoxylation system involved in cephamycin C biosynthesis: Immunoaffinity, protein crosslinking and fluorescence spectroscopy studies
    • in press
    • Enguita, F. J., Liras, P., Leitão, A. L. & Martín, J. F. (1997). Interaction of the two proteins of the methoxylation system involved in cephamycin C biosynthesis: immunoaffinity, protein crosslinking and fluorescence spectroscopy studies. J Biol Chem (in press).
    • (1997) J Biol Chem
    • Enguita, F.J.1    Liras, P.2    Leitão, A.L.3    Martín, J.F.4
  • 15
    • 0024493257 scopus 로고
    • afsB stimulates transcription of the actinorhodin biosynthetic pathway in Streptomyces coelicolor A3(2) and Streptomyces lividans
    • Horinouchi, S., Malpartida, F., Hopwood, D. A. & Beppu, T. (1989). afsB stimulates transcription of the actinorhodin biosynthetic pathway in Streptomyces coelicolor A3(2) and Streptomyces lividans. Mol Gen Genet 215, 355-357.
    • (1989) Mol Gen Genet , vol.215 , pp. 355-357
    • Horinouchi, S.1    Malpartida, F.2    Hopwood, D.A.3    Beppu, T.4
  • 16
    • 0018909597 scopus 로고
    • L-Lysine ε-aminotransferase involved in cephamycin C synthesis in Streptomyces lactamdurans
    • Kern, B. A., Hendlin, D. & Inamine, E. (1980). L-Lysine ε-aminotransferase involved in cephamycin C synthesis in Streptomyces lactamdurans. Antimicrob Agents Chemother 17, 679-685.
    • (1980) Antimicrob Agents Chemother , vol.17 , pp. 679-685
    • Kern, B.A.1    Hendlin, D.2    Inamine, E.3
  • 17
    • 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
  • 18
    • 0025215769 scopus 로고
    • Purification and characterization of the isopenicillin N epimerase from Nocardia lactamduram
    • Láiz, L., Liras, P., Castro, J. M. & Martín, J. F. (1990). Purification and characterization of the isopenicillin N epimerase from Nocardia lactamduram. J Gen Microbiol 136, 663-671.
    • (1990) J Gen Microbiol , vol.136 , pp. 663-671
    • Láiz, L.1    Liras, P.2    Castro, J.M.3    Martín, J.F.4
  • 19
    • 0023848579 scopus 로고
    • Cloning and nucleotide sequence determination of the isopenicillin N synthetase gene from Streptomyces clavuligerus
    • Leskiw, B. K., Aharonowitz, Y., Mevarech, M., Wolfe, S., Vining, L. C., Westlake, D. W. S. & Jensen, S. E. (1988). Cloning and nucleotide sequence determination of the isopenicillin N synthetase gene from Streptomyces clavuligerus. Gene 62, 187-196.
    • (1988) Gene , vol.62 , pp. 187-196
    • Leskiw, B.K.1    Aharonowitz, Y.2    Mevarech, M.3    Wolfe, S.4    Vining, L.C.5    Westlake, D.W.S.6    Jensen, S.E.7
  • 20
    • 0025465341 scopus 로고
    • Phosphate control sequences involved in transcriptional regulation of antibiotic biosynthesis
    • Liras, P., Asturias, J. A. & Martín, J. F. (1990). Phosphate control sequences involved in transcriptional regulation of antibiotic biosynthesis. Trends Biotechnol 8, 184-189.
    • (1990) Trends Biotechnol , vol.8 , pp. 184-189
    • Liras, P.1    Asturias, J.A.2    Martín, J.F.3
  • 21
    • 0021707873 scopus 로고
    • Prevention of phosphate inhibition of cephalosporin synthetases by ferrous ion
    • Lübbe, C., Jensen, S. E. & Demain, A. L. (1984). Prevention of phosphate inhibition of cephalosporin synthetases by ferrous ion. FEMS Microbiol Lett 25, 75-79.
    • (1984) FEMS Microbiol Lett , vol.25 , pp. 75-79
    • Lübbe, C.1    Jensen, S.E.2    Demain, A.L.3
  • 22
    • 0021993624 scopus 로고
    • Repression and inhibition of cephalosporin synthetases in Streptomyces clavuligerus by inorganic phosphate
    • Lübbe, C., Wolfe, S. & Demain, A. L. (1985). Repression and inhibition of cephalosporin synthetases in Streptomyces clavuligerus by inorganic phosphate. Arch Microbiol 140, 317-320.
    • (1985) Arch Microbiol , vol.140 , pp. 317-320
    • Lübbe, C.1    Wolfe, S.2    Demain, A.L.3
  • 23
    • 0028886488 scopus 로고
    • Effects of enhanced lysine ε-aminotransferase activity on cephamycin biosynthesis in Streptomyces clavuligerus
    • Malmberg, L.-H., Hu, W.-S. & Sherman, D. H. (1995). Effects of enhanced lysine ε-aminotransferase activity on cephamycin biosynthesis in Streptomyces clavuligerus. Appl Microbiol Biotechnol 44, 198-205.
    • (1995) Appl Microbiol Biotechnol , vol.44 , pp. 198-205
    • Malmberg, L.-H.1    Hu, W.-S.2    Sherman, D.H.3
  • 24
    • 0003379440 scopus 로고
    • Molecular mechanisms for the control by phosphate of the biosynthesis of antibiotics and other secondary metabolites
    • Edited by S. Shapiro. Boca Raton, FL: CRC Press
    • Martín, J. F. (1989). Molecular mechanisms for the control by phosphate of the biosynthesis of antibiotics and other secondary metabolites. In Regulation of Secondary Metabolism in Actinomycetes, pp. 213-237. Edited by S. Shapiro. Boca Raton, FL: CRC Press.
    • (1989) Regulation of Secondary Metabolism in Actinomycetes , pp. 213-237
    • Martín, J.F.1
  • 25
    • 0017196141 scopus 로고
    • Control by phosphate of candicidin biosynthesis
    • Martín, J. F. & Demain, A. L. (1976). Control by phosphate of candicidin biosynthesis. Biochem Biophys Res Commun 71, 1103-1109.
    • (1976) Biochem Biophys Res Commun , vol.71 , pp. 1103-1109
    • Martín, J.F.1    Demain, A.L.2
  • 26
    • 0019292120 scopus 로고
    • Control of antibiotic synthesis
    • Martín, J. F. & Demain, A. L. (1980). Control of antibiotic synthesis. Microbiol Rev 44, 230-251.
    • (1980) Microbiol Rev , vol.44 , pp. 230-251
    • Martín, J.F.1    Demain, A.L.2
  • 27
    • 0024460765 scopus 로고
    • Organization and expression of genes involved in the biosynthesis of antibiotics and other secondary metabolites
    • Martín, J. F. & Liras, P. (1989). Organization and expression of genes involved in the biosynthesis of antibiotics and other secondary metabolites. Annu Rev Microbiol 43, 173-206.
    • (1989) Annu Rev Microbiol , vol.43 , pp. 173-206
    • Martín, J.F.1    Liras, P.2
  • 28
    • 0002064599 scopus 로고
    • Phosphate control of antibiotic biosynthesis at the transcriptional level
    • Edited by A. Torriani-Gorini, E. Yagil & S. Silver. Washington, DC: American Society for Microbiology
    • Martín, J. F., Marcos, A. T., Martín, A., Asturias, J. A. & Liras, P. (1994). Phosphate control of antibiotic biosynthesis at the transcriptional level. In Phosphate in Microorganisms: Cellular and Molecular Biology, pp. 140-147. Edited by A. Torriani-Gorini, E. Yagil & S. Silver. Washington, DC: American Society for Microbiology.
    • (1994) Phosphate in Microorganisms: Cellular and Molecular Biology , pp. 140-147
    • Martín, J.F.1    Marcos, A.T.2    Martín, A.3    Asturias, J.A.4    Liras, P.5
  • 29
    • 0022971190 scopus 로고
    • Production of nanaomycin and other antibiotics by phosphate-depressed fermentation using phosphate-trapping agents
    • Masuma, R., Tanaka, Y., Tanaka, H. & Omura, S. (1986). Production of nanaomycin and other antibiotics by phosphate-depressed fermentation using phosphate-trapping agents. J Antibiot 39, 1557-1564.
    • (1986) J Antibiot , vol.39 , pp. 1557-1564
    • Masuma, R.1    Tanaka, Y.2    Tanaka, H.3    Omura, S.4
  • 30
    • 0027980597 scopus 로고
    • Phosphorylation of the AfsR protein involved in secondary metabolism in Streptomyces species by a eukaryotic-type protein kinase
    • Matsumoto, A., Hong, S.-K., Ishizuka, H., Horinouchi, S. & Beppu, T. (1994). Phosphorylation of the AfsR protein involved in secondary metabolism in Streptomyces species by a eukaryotic-type protein kinase. Gene 146, 47-56.
    • (1994) Gene , vol.146 , pp. 47-56
    • Matsumoto, A.1    Hong, S.-K.2    Ishizuka, H.3    Horinouchi, S.4    Beppu, T.5
  • 31
    • 0343220923 scopus 로고
    • Biosynthesis of tylosin and its regulation by ammonium and phosphate
    • Edited by H. Kleinkauf, H. von Döhren, H. Dornauer & G. Nesemann. Germany: VCH Weinheim
    • Omura, S. & Tanaka, Y. (1986). Biosynthesis of tylosin and its regulation by ammonium and phosphate. In Regulation of Secondary Metabolite Formation, pp. 305-332. Edited by H. Kleinkauf, H. von Döhren, H. Dornauer & G. Nesemann. Germany: VCH Weinheim.
    • (1986) Regulation of Secondary Metabolite Formation , pp. 305-332
    • Omura, S.1    Tanaka, Y.2
  • 32
    • 0027234550 scopus 로고
    • Phthoxazolin A, a specific inhibitor of cellulose biosynthesis from microbial origin
    • Tanaka, Y., Kanaya, I., Takahashi, Y., Shinose, M., Tanaka, H. & Omura, S. (1993). Phthoxazolin A, a specific inhibitor of cellulose biosynthesis from microbial origin. J Antibiot 46, 1208-1213.
    • (1993) J Antibiot , vol.46 , pp. 1208-1213
    • Tanaka, Y.1    Kanaya, I.2    Takahashi, Y.3    Shinose, M.4    Tanaka, H.5    Omura, S.6
  • 33
    • 0001869753 scopus 로고
    • Regulation of phosphate metabolism and transport
    • Edited by A. M. Törriani-Gorini, E. Yagil & S. Silver. Washington, DC: American Society for Microbiology
    • Torriani-Gorini, A. M. (1994). Regulation of phosphate metabolism and transport. In Phosphate in Microorganisms: Cellular and Molecular Biology, pp. 1-4. Edited by A. M. Törriani-Gorini, E. Yagil & S. Silver. Washington, DC: American Society for Microbiology.
    • (1994) Phosphate in Microorganisms: Cellular and Molecular Biology , pp. 1-4
    • Torriani-Gorini, A.M.1
  • 34
    • 0024489265 scopus 로고
    • Phosphate regulation of ACV synthetase and cephalosporin biosynthesis in Streptomyces clavuligerus
    • Zhang, J. Y., Wolfe, S. & Demain, A. L. (1989). Phosphate regulation of ACV synthetase and cephalosporin biosynthesis in Streptomyces clavuligerus. FEMS Microbiol Lett 57, 145-150.
    • (1989) FEMS Microbiol Lett , vol.57 , pp. 145-150
    • Zhang, J.Y.1    Wolfe, S.2    Demain, A.L.3


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