메뉴 건너뛰기




Volumn 72, Issue 12, 2006, Pages 7652-7660

Engineered cyanophycin synthetase (CphA) from Nostoc ellipsosporum confers enhanced CphA activity and cyanophycin accumulation to Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BACTERIA; CELLS; ENZYME KINETICS; HYDROPHOBICITY;

EID: 33845547991     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.01132-06     Document Type: Article
Times cited : (29)

References (52)
  • 1
    • 0033714944 scopus 로고    scopus 로고
    • Molecular characterization of the cyanophycin synthetase from Synechocystis sp. strain PCC6308
    • Aboulmagd, E., F. B. Oppermann-Sanio, and A. Steinbüchel. 2000. Molecular characterization of the cyanophycin synthetase from Synechocystis sp. strain PCC6308. Arch. Microbiol. 174:297-306.
    • (2000) Arch. Microbiol. , vol.174 , pp. 297-306
    • Aboulmagd, E.1    Oppermann-Sanio, F.B.2    Steinbüchel, A.3
  • 2
    • 0035668788 scopus 로고    scopus 로고
    • Heterologous expression of cyanophycin synthetase and cyanophycin synthesis in the industrial relevant bacteria Corynebacterium glutamicum and Ralstonia eutropha and in Pseudomonas putida
    • Aboulmagd, E., I. Voss, F. B. Oppermann-Sanio, and A. Steinbüchel. 2001. Heterologous expression of cyanophycin synthetase and cyanophycin synthesis in the industrial relevant bacteria Corynebacterium glutamicum and Ralstonia eutropha and in Pseudomonas putida. Biomacromolecules 2:338-1342.
    • (2001) Biomacromolecules , vol.2 , pp. 338-1342
    • Aboulmagd, E.1    Voss, I.2    Oppermann-Sanio, F.B.3    Steinbüchel, A.4
  • 4
    • 0020622147 scopus 로고
    • Protein degradation and synthesis of cyanophycin granule polypeptide in Aphanocapsa sp
    • Allen, M. M., and M. A. Hawley. 1983. Protein degradation and synthesis of cyanophycin granule polypeptide in Aphanocapsa sp. J. Bacteriol. 154:1480-1484.
    • (1983) J. Bacteriol. , vol.154 , pp. 1480-1484
    • Allen, M.M.1    Hawley, M.A.2
  • 5
    • 0036038421 scopus 로고    scopus 로고
    • In vivo evolution of the Aeromonas punctata polyhydroxyalkanoate (PHA) synthase: Isolation and characterization of modified PHA synthases with enhanced activity
    • Amara, A. A., A. Steinbüchel, and B. H. A. Rehm. 2002. In vivo evolution of the Aeromonas punctata polyhydroxyalkanoate (PHA) synthase: isolation and characterization of modified PHA synthases with enhanced activity. Appl. Microbiol. Biotechnol. 59:477-482.
    • (2002) Appl. Microbiol. Biotechnol. , vol.59 , pp. 477-482
    • Amara, A.A.1    Steinbüchel, A.2    Rehm, B.H.A.3
  • 8
    • 0033850973 scopus 로고    scopus 로고
    • Biosynthesis of the cyanobacterial reserve polymer multi-L-arginyl-poly- L-aspartic acid (cyanophycin): Mechanism of the cyanophycin synthetase reaction studied with synthetic primers
    • Berg, H., K. Ziegler, K. Piotukh, K. Baier, W. Lockau, and R. Volkmer-Engert. 2000. Biosynthesis of the cyanobacterial reserve polymer multi-L-arginyl-poly-L-aspartic acid (cyanophycin): mechanism of the cyanophycin synthetase reaction studied with synthetic primers. Eur. J. Biochem. 267:5561-5570.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 5561-5570
    • Berg, H.1    Ziegler, K.2    Piotukh, K.3    Baier, K.4    Lockau, W.5    Volkmer-Engert, R.6
  • 9
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for 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
  • 10
    • 0033929214 scopus 로고    scopus 로고
    • Deletion of various carboxy-terminal domains of Lactococcus lactis SK11 proteinase: Effects on activity, specificity, and stability of the truncated enzyme
    • Bruinenberg, P. G., W. E. De Vos, and R. J. Siezen. 2000. Deletion of various carboxy-terminal domains of Lactococcus lactis SK11 proteinase: effects on activity, specificity, and stability of the truncated enzyme. Appl. Environ. Microbiol. 66:2859-2865.
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 2859-2865
    • Bruinenberg, P.G.1    De Vos, W.E.2    Siezen, R.J.3
  • 13
    • 13544249631 scopus 로고    scopus 로고
    • Physiological conditions conductive to high cyanophycin content in biomass of Acinetobacter calcoaceticus strain ADP1
    • Elbahloul, Y., M. Krehenbrink, R. Reichelt, and A. Steinbüchel. 2005. Physiological conditions conductive to high cyanophycin content in biomass of Acinetobacter calcoaceticus strain ADP1. Appl. Environ. Microbiol. 71:858-866.
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 858-866
    • Elbahloul, Y.1    Krehenbrink, M.2    Reichelt, R.3    Steinbüchel, A.4
  • 14
    • 29144497375 scopus 로고    scopus 로고
    • Protamylasse, a residual compound of industrial starch production, provides a suitable medium for large-scale cyanophycin production
    • Elbahloul, Y., K. Frey, J. Sanders, and A. Steinbüchel. 2005. Protamylasse, a residual compound of industrial starch production, provides a suitable medium for large-scale cyanophycin production. Appl. Environ. Microbiol. 71:7759-7767.
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 7759-7767
    • Elbahloul, Y.1    Frey, K.2    Sanders, J.3    Steinbüchel, A.4
  • 15
    • 33144470936 scopus 로고    scopus 로고
    • Engineering the genotype of Acinetobacter sp. strain ADP1 to enhance biosynthesis of cyanophycin
    • Elbahloul, Y., and A. Steinbüchel. 2006. Engineering the genotype of Acinetobacter sp. strain ADP1 to enhance biosynthesis of cyanophycin. Appl. Environ. Microbiol. 72:1410-1419.
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 1410-1419
    • Elbahloul, Y.1    Steinbüchel, A.2
  • 16
    • 0036304471 scopus 로고    scopus 로고
    • Technical scale production of cyanophycin with recombinant strains of Escherichia coli
    • Frey, K. M., F. B. Oppermann-Sanio, H. Schmidt, and A. Steinbüchel. 2002. Technical scale production of cyanophycin with recombinant strains of Escherichia coli. Appl. Environ. Microbiol. 68:3377-3384.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 3377-3384
    • Frey, K.M.1    Oppermann-Sanio, F.B.2    Schmidt, H.3    Steinbüchel, A.4
  • 17
    • 0034009799 scopus 로고    scopus 로고
    • Axenic cultivation of anoxygenic phototrophic bacteria, cyanobacteria, and microalgae in a new closed tubular glass photobioreactor
    • Hai, T., H. Ahlers, V. Gorenflo, and A. Steinbüchel. 2000. Axenic cultivation of anoxygenic phototrophic bacteria, cyanobacteria, and microalgae in a new closed tubular glass photobioreactor. Appl. Microbiol. Biotechnol. 53:383-389.
    • (2000) Appl. Microbiol. Biotechnol. , vol.53 , pp. 383-389
    • Hai, T.1    Ahlers, H.2    Gorenflo, V.3    Steinbüchel, A.4
  • 18
    • 0036135278 scopus 로고    scopus 로고
    • Molecular characterization of a thermostable cyanophycin synthetase from the thermophilic cyanobacterium Synechococcus sp. strain MA19 and in vitro synthesis of cyanophycin and related polyamides
    • Hai, T., F. B. Oppermann-Sanio, and A. Steinbüchel. 2002. Molecular characterization of a thermostable cyanophycin synthetase from the thermophilic cyanobacterium Synechococcus sp. strain MA19 and in vitro synthesis of cyanophycin and related polyamides. Appl. Environ. Microbiol. 68:93-101.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 93-101
    • Hai, T.1    Oppermann-Sanio, F.B.2    Steinbüchel, A.3
  • 19
    • 0003037055 scopus 로고
    • Chemical composition
    • P. Gerhardt (ed.). American Society for Microbiology, Washington, D.C.
    • Hanson, R. S., and J. A. Phillips. 1981. Chemical composition, p. 328-364. In P. Gerhardt (ed.), Manual of methods for general bacteriology. American Society for Microbiology, Washington, D.C.
    • (1981) Manual of Methods for General Bacteriology , pp. 328-364
    • Hanson, R.S.1    Phillips, J.A.2
  • 20
    • 0031686669 scopus 로고    scopus 로고
    • Synechocystis sp. PCC6803 possesses a two-component polyhydroxyalkanoic acid synthase similar to that of anoxygenic purple sulfur bacteria
    • Hein, S., T. Hai, and A. Steinbüchel. 1998. Synechocystis sp. PCC6803 possesses a two-component polyhydroxyalkanoic acid synthase similar to that of anoxygenic purple sulfur bacteria. Arch. Microbiol. 170:162-170.
    • (1998) Arch. Microbiol. , vol.170 , pp. 162-170
    • Hein, S.1    Hai, T.2    Steinbüchel, A.3
  • 21
    • 34248342121 scopus 로고    scopus 로고
    • Polyaspartic acid homopolymers and copolymers: Biotechnological production and use thereof
    • 11 September. International patent application WO 98/39090
    • Joentgen, W., T. Groth, A. Steinbüchel, T. Hai, and F. B. Oppermann. 11 September 1998. Polyaspartic acid homopolymers and copolymers: biotechnological production and use thereof. International patent application WO 98/39090.
    • (1998)
    • Joentgen, W.1    Groth, T.2    Steinbüchel, A.3    Hai, T.4    Oppermann, F.B.5
  • 25
    • 0036244738 scopus 로고    scopus 로고
    • Enhanced accumulation and changed monomer composition in polyhydroxyalkanoate (PHA) copolyester by in vitro evolution of Aeromonas caviae PHA synthase
    • Kichise, T., S. Taguchi, and Y. Doi. 2002. Enhanced accumulation and changed monomer composition in polyhydroxyalkanoate (PHA) copolyester by in vitro evolution of Aeromonas caviae PHA synthase. Appl. Environ. Microbiol. 68:2411-2419.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 2411-2419
    • Kichise, T.1    Taguchi, S.2    Doi, Y.3
  • 26
    • 0036236197 scopus 로고    scopus 로고
    • Evaluation of non-cyanobacterial genome sequences for occurrence of genes encoding proteins homologous to cyanophycin synthetase and cloning of an active cyanophycin synthetase from Acinetobacter sp. strain DSM 587
    • Krehenbrink, M., F. B. Oppermann-Sanio, and A. Steinbüchel. 2002. Evaluation of non-cyanobacterial genome sequences for occurrence of genes encoding proteins homologous to cyanophycin synthetase and cloning of an active cyanophycin synthetase from Acinetobacter sp. strain DSM 587. Arch. Microbiol. 177:371-380.
    • (2002) Arch. Microbiol. , vol.177 , pp. 371-380
    • Krehenbrink, M.1    Oppermann-Sanio, F.B.2    Steinbüchel, A.3
  • 27
    • 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
  • 28
    • 0032052136 scopus 로고    scopus 로고
    • N- and C-terminal peptide sequences are essential for enzyme assembly, allosteric, and/or catalytic properties of ADP-glucose pyrophosphorylase
    • Laughlin, M. J., S. E. Chantler, and T. W. Okita. 1998. N- and C-terminal peptide sequences are essential for enzyme assembly, allosteric, and/or catalytic properties of ADP-glucose pyrophosphorylase. Plant J. 14:159-168.
    • (1998) Plant J. , vol.14 , pp. 159-168
    • Laughlin, M.J.1    Chantler, S.E.2    Okita, T.W.3
  • 29
    • 84985268195 scopus 로고
    • The normal and induced occurrence of cyanophycin inclusion bodies in several blue green-algae
    • Lawry, N. H., and R. D. Simon. 1982. The normal and induced occurrence of cyanophycin inclusion bodies in several blue green-algae. J. Phycol. 18:391-399.
    • (1982) J. Phycol. , vol.18 , pp. 391-399
    • Lawry, N.H.1    Simon, R.D.2
  • 30
    • 0031873421 scopus 로고    scopus 로고
    • A transposition-induced mutant of Nostoc ellipsosporum implicates an arginine-biosynthetic gene in the formation of cyanophycin granules and of functional heterocysts and akinetes
    • Leganés, F., F. Fernandez-Pinas, and C. P. Wolk. 1998. A transposition-induced mutant of Nostoc ellipsosporum implicates an arginine-biosynthetic gene in the formation of cyanophycin granules and of functional heterocysts and akinetes. Microbiology 144:1799-1805.
    • (1998) Microbiology , vol.144 , pp. 1799-1805
    • Leganés, F.1    Fernandez-Pinas, F.2    Wolk, C.P.3
  • 31
    • 0029555330 scopus 로고
    • In vivo pharmacokinetics study for the assessment of poly(L-aspartic acid) as a drug carrier for colon-specific drug delivery
    • Leopold, C. S., and D. R. Friend. 1995. In vivo pharmacokinetics study for the assessment of poly(L-aspartic acid) as a drug carrier for colon-specific drug delivery. J. Pharmacokinet. Biopharm. 4:397-406.
    • (1995) J. Pharmacokinet. Biopharm. , vol.4 , pp. 397-406
    • Leopold, C.S.1    Friend, D.R.2
  • 32
    • 0025054141 scopus 로고
    • Transient accumulation of cyanophycin in Anabaena cylindrica and Synechocystis 6308
    • Mackerras, A. H., N. M. de Chazal, and G. D. Smith. 1990. Transient accumulation of cyanophycin in Anabaena cylindrica and Synechocystis 6308. J. Gen. Microbiol. 136:2057-2065.
    • (1990) J. Gen. Microbiol. , vol.136 , pp. 2057-2065
    • Mackerras, A.H.1    De Chazal, N.M.2    Smith, G.D.3
  • 33
    • 0026322834 scopus 로고
    • Sequential truncation of the lactose permease over a three-amino acid sequence near the carboxyl terminus leads to progressive loss of activity and stability
    • McKenna, E., D. Hardy, J. C. Pastore, and H. R. Kaback. 1991. Sequential truncation of the lactose permease over a three-amino acid sequence near the carboxyl terminus leads to progressive loss of activity and stability. Proc. Natl. Acad. Sci. USA 88:2969-2973.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 2969-2973
    • McKenna, E.1    Hardy, D.2    Pastore, J.C.3    Kaback, H.R.4
  • 34
    • 0038492584 scopus 로고    scopus 로고
    • Crystal structures of active fully assembled substrate- and product-bound complexes of UDP-N-acetylmuramic acid:L-alanine ligase (MurC) from Haemophilus influenzae
    • Mol, C. D., A. Brooun, D. R. Dougan, M. T. Hilgers, L. W. Tari, R. A. Wijnands, M. W. Knuth, D. E. McRee, and R. V. Swanson. 2003. Crystal structures of active fully assembled substrate- and product-bound complexes of UDP-N-acetylmuramic acid:L-alanine ligase (MurC) from Haemophilus influenzae. J. Bacteriol. 185:4152-4162.
    • (2003) J. Bacteriol. , vol.185 , pp. 4152-4162
    • Mol, C.D.1    Brooun, A.2    Dougan, D.R.3    Hilgers, M.T.4    Tari, L.W.5    Wijnands, R.A.6    Knuth, M.W.7    McRee, D.E.8    Swanson, R.V.9
  • 37
    • 0036164128 scopus 로고    scopus 로고
    • Occurrence, functions and biosynthesis of polyamides in microorganisms and biotechnological production
    • Oppermann-Sanio, F. B., and A. Steinbüchel. 2002. Occurrence, functions and biosynthesis of polyamides in microorganisms and biotechnological production. Naturwissenschaften 89:11-22.
    • (2002) Naturwissenschaften , vol.89 , pp. 11-22
    • Oppermann-Sanio, F.B.1    Steinbüchel, A.2
  • 39
    • 0018409915 scopus 로고
    • Generic assignments, strain histories and properties of pure cultures of cyanobacteria
    • Rippka, R., J. Deruelles, J. B. Waterbury, M. Herdman, and R. Y. Stanier. 1979. Generic assignments, strain histories and properties of pure cultures of cyanobacteria. J. Gen. Microbiol. 111:1-61.
    • (1979) J. Gen. Microbiol. , vol.111 , pp. 1-61
    • Rippka, R.1    Deruelles, J.2    Waterbury, J.B.3    Herdman, M.4    Stanier, R.Y.5
  • 41
    • 0025958714 scopus 로고
    • Molecular analysis of the Alcaligenes eutrophus poly(3-hydroxybutyrate) (PHB)-biosynthetic operon: Identification of the N terminus of PHB-synthase and identification of the promotor
    • Schubert, P., N. Krüger, and A. Steinbüchel. 1991. Molecular analysis of the Alcaligenes eutrophus poly(3-hydroxybutyrate) (PHB)-biosynthetic operon: identification of the N terminus of PHB-synthase and identification of the promotor. J. Bacteriol. 173:168-175.
    • (1991) J. Bacteriol. , vol.173 , pp. 168-175
    • Schubert, P.1    Krüger, N.2    Steinbüchel, A.3
  • 42
    • 0031599328 scopus 로고    scopus 로고
    • Chemical synthesis of polyaspartates: A biodegradable alternative to currently used polycarboxylate homo- and copolymers
    • Schwamborn, M. 1998. Chemical synthesis of polyaspartates: a biodegradable alternative to currently used polycarboxylate homo- and copolymers. Polym. Degrad. Stabil. 59:39-45.
    • (1998) Polym. Degrad. Stabil. , vol.59 , pp. 39-45
    • Schwamborn, M.1
  • 43
    • 0015783334 scopus 로고
    • The effect of chloramphenicol on the production of cyanophycin granule polypeptide in the blue-green alga Anabaena cylindrica
    • Simon, R. 1973. The effect of chloramphenicol on the production of cyanophycin granule polypeptide in the blue-green alga Anabaena cylindrica. Arch. Mikrobiol. 92:115-122.
    • (1973) Arch. Mikrobiol. , vol.92 , pp. 115-122
    • Simon, R.1
  • 44
    • 0017263448 scopus 로고
    • The biosynthesis of multi-L-arginyl-poly(L-aspartic acid) in the filamentous cyanobacterium Anabaena cylindrica
    • Simon, R. D. 1976. The biosynthesis of multi-L-arginyl-poly(L-aspartic acid) in the filamentous cyanobacterium Anabaena cylindrica. Biochim. Biophys. Acta 422:407-418.
    • (1976) Biochim. Biophys. Acta , vol.422 , pp. 407-418
    • Simon, R.D.1
  • 45
    • 0016881981 scopus 로고
    • Determination of the structure of the novel polypeptide containing aspartic acid and arginine which is found in cyanobacteria
    • Simon, R. D., and P. Weathers. 1976. Determination of the structure of the novel polypeptide containing aspartic acid and arginine which is found in cyanobacteria. Biochim. Biophys. Acta 420:165-176.
    • (1976) Biochim. Biophys. Acta , vol.420 , pp. 165-176
    • Simon, R.D.1    Weathers, P.2
  • 46
    • 4143079287 scopus 로고    scopus 로고
    • Identification of the Anabaena sp. strain PCC7120 cyanophycin synthetase as suitable enzyme for production of cyanophycin in Gram-negative bacteria like Pseudomonas putida and Ralstonia eutropha
    • Voss, I., S. C. Diniz, E. Aboulmagd, and A. Steinbüchel. 2004. Identification of the Anabaena sp. strain PCC7120 cyanophycin synthetase as suitable enzyme for production of cyanophycin in Gram-negative bacteria like Pseudomonas putida and Ralstonia eutropha. Biomacromolecules 5:1588-1595.
    • (2004) Biomacromolecules , vol.5 , pp. 1588-1595
    • Voss, I.1    Diniz, S.C.2    Aboulmagd, E.3    Steinbüchel, A.4
  • 47
    • 29544440779 scopus 로고    scopus 로고
    • Application of a KDPG-aldolase gene-dependent addiction system for enhanced production of cyanophycin in Ralstonia eutropha strain H16
    • Voss, I., and A. Steinbüchel. 2006. Application of a KDPG-aldolase gene-dependent addiction system for enhanced production of cyanophycin in Ralstonia eutropha strain H16. Metabol. Eng. 8:66-78.
    • (2006) Metabol. Eng. , vol.8 , pp. 66-78
    • Voss, I.1    Steinbüchel, A.2
  • 48
    • 0000745994 scopus 로고
    • Isolierung und kristallisierung des gärungsferments enolase
    • Warburg, O., and W. Christian. 1941. Isolierung und Kristallisierung des Gärungsferments Enolase. Biochem. Z. 310:384-421.
    • (1941) Biochem. Z. , vol.310 , pp. 384-421
    • Warburg, O.1    Christian, W.2
  • 49
    • 32344449996 scopus 로고    scopus 로고
    • Biochemical properties of UspG, a universal stress protein of Escherichia coli
    • Weber, A., and K. Jung. 2006. Biochemical properties of UspG, a universal stress protein of Escherichia coli. Biochemistry 45:1620-1628.
    • (2006) Biochemistry , vol.45 , pp. 1620-1628
    • Weber, A.1    Jung, K.2
  • 50
    • 0025343062 scopus 로고
    • Characterization and anticancer activity of the micelle forming polymeric anticancer drug adriamycin-conjugated poly(ethylene glycol)-poly(aspartic acid) block copolymer
    • Yokoyama, M., M. Miyauchi, N. Yamada, T. Okano, Y. Sakurai, K. Kataoka, and S. Inoue. 1990. Characterization and anticancer activity of the micelle forming polymeric anticancer drug adriamycin-conjugated poly(ethylene glycol)-poly(aspartic acid) block copolymer. Cancer Res. 6:1693-1700.
    • (1990) Cancer Res. , vol.6 , pp. 1693-1700
    • Yokoyama, M.1    Miyauchi, M.2    Yamada, N.3    Okano, T.4    Sakurai, Y.5    Kataoka, K.6    Inoue, S.7
  • 51
    • 0032523821 scopus 로고    scopus 로고
    • Molecular characterization of cyanophycin synthetase, the enzyme catalyzing the biosynthesis of the cyanobacterial reserve material multi-L-arginyl-poly-L-aspartate (cyanophycin)
    • Ziegler, K., A. Diener, C. Herpin, R. Richter, R. Deutzmann, and W. Lockau. 1998. Molecular characterization of cyanophycin synthetase, the enzyme catalyzing the biosynthesis of the cyanobacterial reserve material multi-L-arginyl-poly-L-aspartate (cyanophycin). Eur. J. Biochem. 254:154-159.
    • (1998) Eur. J. Biochem. , vol.254 , pp. 154-159
    • Ziegler, K.1    Diener, A.2    Herpin, C.3    Richter, R.4    Deutzmann, R.5    Lockau, W.6
  • 52
    • 0036560886 scopus 로고    scopus 로고
    • Cyanophycin synthetase-like enzymes of non-cyanobacterial eubacteria: Characterization of the polymer produced by a recombinant synthetase of Desulfitobacterium hafniense
    • Ziegler, K., R. Deutzmann, and W. Lockau. 2002. Cyanophycin synthetase-like enzymes of non-cyanobacterial eubacteria: characterization of the polymer produced by a recombinant synthetase of Desulfitobacterium hafniense. Z. Naturforsch. 57:522-529.
    • (2002) Z. Naturforsch. , vol.57 , pp. 522-529
    • Ziegler, K.1    Deutzmann, R.2    Lockau, W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.