메뉴 건너뛰기




Volumn 140, Issue 1-2, 2009, Pages 114-123

The gac-gene cluster for the production of acarbose from Streptomyces glaucescens GLA.O-Identification, isolation and characterization

Author keywords

glucosidase inhibitor; Acarbose; Actinomycetes; Carbophor; Diabetes treatment

Indexed keywords

ACARBOSE; ACTINOMYCETES; BIOSYNTHESIS PATHWAYS; CARBOPHOR; CYCLITOL; DIABETES TREATMENT; END-PRODUCTS; GENE BANKS; GENE CLUSTERS; ISOLATION AND CHARACTERIZATIONS; PCR APPROACHES; TYPE II;

EID: 61649104320     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2008.10.016     Document Type: Article
Times cited : (46)

References (51)
  • 1
    • 0024024077 scopus 로고
    • Cloning of DNA involved in sporulation of Streptomyces griseus
    • Babcock M.J., and Kendrick K.E. Cloning of DNA involved in sporulation of Streptomyces griseus. J. Bacteriol. 170 (1988) 2802-2808
    • (1988) J. Bacteriol. , vol.170 , pp. 2802-2808
    • Babcock, M.J.1    Kendrick, K.E.2
  • 2
    • 33646054552 scopus 로고    scopus 로고
    • Functional analysis of the validamycin biosynthetic gene cluster and engineered production of validoxylamine A
    • Bai L., Li L., Xu H., Minagawa K., Yu Y., Zhang Y., Zhou X., Floss H.G., Mahmud T., and Deng Z. Functional analysis of the validamycin biosynthetic gene cluster and engineered production of validoxylamine A. Chem. Biol. 13 (2006) 387-397
    • (2006) Chem. Biol. , vol.13 , pp. 387-397
    • Bai, L.1    Li, L.2    Xu, H.3    Minagawa, K.4    Yu, Y.5    Zhang, Y.6    Zhou, X.7    Floss, H.G.8    Mahmud, T.9    Deng, Z.10
  • 4
    • 0032522298 scopus 로고    scopus 로고
    • A gridded genomic library of the honeybee (Apis mellifera): a reference library system for basic and comparative genetic studies of a hymenopteran genome
    • Beye M., Poch A., Burgtorf C., Moritz R.F., and Lehrach H. A gridded genomic library of the honeybee (Apis mellifera): a reference library system for basic and comparative genetic studies of a hymenopteran genome. Genomics 49 (1998) 317-320
    • (1998) Genomics , vol.49 , pp. 317-320
    • Beye, M.1    Poch, A.2    Burgtorf, C.3    Moritz, R.F.4    Lehrach, H.5
  • 5
    • 0026645203 scopus 로고
    • Plasmid cloning vectors for the conjugal transfer of DNA from Escherichia coli to Streptomyces sp
    • Bierman M., Logan R., O'Brien K., Seno E.T., Rao R.N., and Schoner B.E. Plasmid cloning vectors for the conjugal transfer of DNA from Escherichia coli to Streptomyces sp. Gene 116 (1992) 43-49
    • (1992) Gene , vol.116 , pp. 43-49
    • Bierman, M.1    Logan, R.2    O'Brien, K.3    Seno, E.T.4    Rao, R.N.5    Schoner, B.E.6
  • 7
    • 16844365818 scopus 로고    scopus 로고
    • The acbH gene of Actinoplanes sp. encodes a solute receptor with binding activities for acarbose and longer homologs
    • Brunkhorst C., Wehmeier U.F., Piepersberg W., and Schneider E. The acbH gene of Actinoplanes sp. encodes a solute receptor with binding activities for acarbose and longer homologs. Res. Microbiol. 156 (2005) 322-327
    • (2005) Res. Microbiol. , vol.156 , pp. 322-327
    • Brunkhorst, C.1    Wehmeier, U.F.2    Piepersberg, W.3    Schneider, E.4
  • 8
    • 0032168134 scopus 로고    scopus 로고
    • Gridded genomic libraries of different chordate species: a reference library system for basic and comparative genetic studies of chordate genomes
    • Burgtorf C., Welzel K., Hasenbank R., Zehetner G., Weis S., and Lehrach H. Gridded genomic libraries of different chordate species: a reference library system for basic and comparative genetic studies of chordate genomes. Genomics 5 (1998) 230-232
    • (1998) Genomics , vol.5 , pp. 230-232
    • Burgtorf, C.1    Welzel, K.2    Hasenbank, R.3    Zehetner, G.4    Weis, S.5    Lehrach, H.6
  • 9
    • 0018413311 scopus 로고
    • Inhibition of human intestinal α-glucoside hydrolases by a new complex oligosaccharide
    • Caspary W.F., and Graf S. Inhibition of human intestinal α-glucoside hydrolases by a new complex oligosaccharide. Res. Exp. Med. 175 (1979) 1-6
    • (1979) Res. Exp. Med. , vol.175 , pp. 1-6
    • Caspary, W.F.1    Graf, S.2
  • 10
    • 61649114277 scopus 로고    scopus 로고
    • Isolation of the biosynthesis genes for pseudo-oligosaccharides from Streptomyces glaucescens GLA.O, and their use
    • German patent DE 19622783 US pat. 6,306,627
    • Decker, H., 1997. Isolation of the biosynthesis genes for pseudo-oligosaccharides from Streptomyces glaucescens GLA.O, and their use. German patent DE 19622783 (US pat. 6,306,627).
    • (1997)
    • Decker, H.1
  • 11
    • 0022404668 scopus 로고
    • Streptomycin biosynthesis in Streptomyces griseus. I. Characterizaton of streptomycin-idiotrophic mutants
    • Distler J., Klier K., Piendl W., Böck A., Kresze G., and Piepersberg W. Streptomycin biosynthesis in Streptomyces griseus. I. Characterizaton of streptomycin-idiotrophic mutants. FEMS Microbiol. Lett. 30 (1985) 145-150
    • (1985) FEMS Microbiol. Lett. , vol.30 , pp. 145-150
    • Distler, J.1    Klier, K.2    Piendl, W.3    Böck, A.4    Kresze, G.5    Piepersberg, W.6
  • 12
    • 0000431069 scopus 로고
    • Studies on transformation of Escherichia coli plasmids
    • Hanahan D. Studies on transformation of Escherichia coli plasmids. J. Mol. Biol. 127 (1983) 100-104
    • (1983) J. Mol. Biol. , vol.127 , pp. 100-104
    • Hanahan, D.1
  • 13
    • 0034938521 scopus 로고    scopus 로고
    • Identification, cloning, expression, and characterization of the extracellular acarbose-modifying glycosyltransferase, AcbD, from Actinoplanes sp. SE50/110 strain SE50
    • Hemker M., Stratmann A., Goeke K., Schröder W., Lenz J., Piepersberg W., and Pape H. Identification, cloning, expression, and characterization of the extracellular acarbose-modifying glycosyltransferase, AcbD, from Actinoplanes sp. SE50/110 strain SE50. J. Bacteriol. 183 (2001) 4484-4492
    • (2001) J. Bacteriol. , vol.183 , pp. 4484-4492
    • Hemker, M.1    Stratmann, A.2    Goeke, K.3    Schröder, W.4    Lenz, J.5    Piepersberg, W.6    Pape, H.7
  • 14
    • 0029111794 scopus 로고
    • A cellulase/xylanase-negative mutant of Streptomyces lividans 1326 defective in cellobiose and xylobiose uptake is mutated in a gene encoding a protein homologous to ATP-binding proteins
    • Hurtubise Y., Shareck F., Kluepfel D., and Morosoli R. A cellulase/xylanase-negative mutant of Streptomyces lividans 1326 defective in cellobiose and xylobiose uptake is mutated in a gene encoding a protein homologous to ATP-binding proteins. Mol. Microbiol. 17 (1995) 367-377
    • (1995) Mol. Microbiol. , vol.17 , pp. 367-377
    • Hurtubise, Y.1    Shareck, F.2    Kluepfel, D.3    Morosoli, R.4
  • 16
    • 0032942468 scopus 로고    scopus 로고
    • FramePlot: a new implementation of the frame analysis for predicting protein-coding regions in bacterial DNA with a high G + C content
    • Ishikawa J., and Hotta K. FramePlot: a new implementation of the frame analysis for predicting protein-coding regions in bacterial DNA with a high G + C content. FEMS Microbiol. Lett. 174 (1999) 251-253
    • (1999) FEMS Microbiol. Lett. , vol.174 , pp. 251-253
    • Ishikawa, J.1    Hotta, K.2
  • 17
    • 0033013283 scopus 로고    scopus 로고
    • Screening, nucleotide sequence, and biochemical characterization of an esterase from Pseudomonas fluorescens with high activity towards lactones
    • Khalameyzer V., Fischer I., Bornscheuer U.T., and Altenbuchner J. Screening, nucleotide sequence, and biochemical characterization of an esterase from Pseudomonas fluorescens with high activity towards lactones. Appl. Environ. Microbiol. 65 (1999) 477-482
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 477-482
    • Khalameyzer, V.1    Fischer, I.2    Bornscheuer, U.T.3    Altenbuchner, J.4
  • 19
    • 5444270335 scopus 로고    scopus 로고
    • A single mutation switches the reaction specificities of cyclodextrin glycosyltransferase and the acarbose modifying enzyme acarviosyl transferase
    • Leemhuis H., Wehmeier U.F., and Dijkhuizen L. A single mutation switches the reaction specificities of cyclodextrin glycosyltransferase and the acarbose modifying enzyme acarviosyl transferase. Biochemistry 43 (2004) 13204-13213
    • (2004) Biochemistry , vol.43 , pp. 13204-13213
    • Leemhuis, H.1    Wehmeier, U.F.2    Dijkhuizen, L.3
  • 20
    • 0028825809 scopus 로고
    • Nucleotide sequences of streptomycete 16S ribosomal DNA: towards a specific identification system for streptomycetes using PCR
    • Mehling A., Wehmeier U.F., and Piepersberg W. Nucleotide sequences of streptomycete 16S ribosomal DNA: towards a specific identification system for streptomycetes using PCR. Microbiology 141 (1995) 2139-2147
    • (1995) Microbiology , vol.141 , pp. 2139-2147
    • Mehling, A.1    Wehmeier, U.F.2    Piepersberg, W.3
  • 21
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory, Cold Spring Harbor p. 433
    • Miller J.H. Experiments in Molecular Genetics (1972), Cold Spring Harbor Laboratory, Cold Spring Harbor p. 433
    • (1972) Experiments in Molecular Genetics
    • Miller, J.H.1
  • 22
    • 0016617287 scopus 로고
    • New amylase inhibitor (S-AI) from Streptomyces diastaticus var. amylostaticus no. 2476
    • Muaro S., and Ohyama K. New amylase inhibitor (S-AI) from Streptomyces diastaticus var. amylostaticus no. 2476. Agr. Biol. Chem. 39 (1975) 2271-2273
    • (1975) Agr. Biol. Chem. , vol.39 , pp. 2271-2273
    • Muaro, S.1    Ohyama, K.2
  • 23
    • 0000143333 scopus 로고
    • Chemistry, biochemistry and therapeutic potential of microbial α-glucosidase inhibitors
    • Demain A.L., Somkuti G.A., Hunter-Creva J.C., and Rossmoore H.W. (Eds), Elsevier Science Publishers, Amsterdam
    • Mueller L. Chemistry, biochemistry and therapeutic potential of microbial α-glucosidase inhibitors. In: Demain A.L., Somkuti G.A., Hunter-Creva J.C., and Rossmoore H.W. (Eds). Novel Microbial Products for Medicine and Agriculture (1989), Elsevier Science Publishers, Amsterdam 109-116
    • (1989) Novel Microbial Products for Medicine and Agriculture , pp. 109-116
    • Mueller, L.1
  • 24
    • 0008558197 scopus 로고    scopus 로고
    • Crystal structures of human panceartic a-amylase in complex with carbohydrate and proteinaceous inhibitors
    • Nahoum V., Roux G., Anton V., Rouge P., Puigserver A., Bischoff H., Henrissat B., and Payan F. Crystal structures of human panceartic a-amylase in complex with carbohydrate and proteinaceous inhibitors. Biochem. J. 346 (2000) 201-208
    • (2000) Biochem. J. , vol.346 , pp. 201-208
    • Nahoum, V.1    Roux, G.2    Anton, V.3    Rouge, P.4    Puigserver, A.5    Bischoff, H.6    Henrissat, B.7    Payan, F.8
  • 25
    • 0020461811 scopus 로고
    • Studies on the α-glucoside hydrolase inhibitor adiposin. II. Taxonomic studies on the producing microorganism
    • Namiki S., Kangouri K., Nagate T., Hara H., Sugita K., and Omura S. Studies on the α-glucoside hydrolase inhibitor adiposin. II. Taxonomic studies on the producing microorganism. J. Antibiot. (Tokyo) 35 (1982) 1156-1159
    • (1982) J. Antibiot. (Tokyo) , vol.35 , pp. 1156-1159
    • Namiki, S.1    Kangouri, K.2    Nagate, T.3    Hara, H.4    Sugita, K.5    Omura, S.6
  • 26
    • 0026035996 scopus 로고
    • An improved bacterial colony lysis procedure enables direct DNA hybridisation using short (10, 11 bases) oligonucleotides to cosmids
    • Nizetic D., Drmanac R., and Lehrach H. An improved bacterial colony lysis procedure enables direct DNA hybridisation using short (10, 11 bases) oligonucleotides to cosmids. Nucleic Acids Res. 19 (1991) 182
    • (1991) Nucleic Acids Res. , vol.19 , pp. 182
    • Nizetic, D.1    Drmanac, R.2    Lehrach, H.3
  • 28
    • 0019806556 scopus 로고
    • Oligostatin, new antibiotics with amylase inhibitory activity. II. Structures of oligostatins C, D and E
    • Omoto S., Itoh J., Ogino H., and Iwamatsu K. Oligostatin, new antibiotics with amylase inhibitory activity. II. Structures of oligostatins C, D and E. J. Antibiot. (Tokyo) 34 (1981) 1429-1433
    • (1981) J. Antibiot. (Tokyo) , vol.34 , pp. 1429-1433
    • Omoto, S.1    Itoh, J.2    Ogino, H.3    Iwamatsu, K.4
  • 29
    • 0029450778 scopus 로고
    • Streptomycin and related aminoglycosides
    • Vining L., and Stuttard C. (Eds), Butterworth-Heinemann, Boston
    • Piepersberg W. Streptomycin and related aminoglycosides. In: Vining L., and Stuttard C. (Eds). Biochemistry and Genetics of Antibiotic Biosynthesis (1995), Butterworth-Heinemann, Boston 531-570
    • (1995) Biochemistry and Genetics of Antibiotic Biosynthesis , pp. 531-570
    • Piepersberg, W.1
  • 30
    • 84978696453 scopus 로고    scopus 로고
    • Aminoglycosides and sugar components in other secondary metabolites
    • Rehm H.-J., Reed G., Pühle r.A., and Stadler P. (Eds), VCH-Verlagsgesellschaft, Weinheim
    • Piepersberg W., and Distler J. Aminoglycosides and sugar components in other secondary metabolites. In: Rehm H.-J., Reed G., Pühle r.A., and Stadler P. (Eds). Biotechnology: products of secondary metabolism. 2nd ed. vol. 7 (1997), VCH-Verlagsgesellschaft, Weinheim 397-488
    • (1997) Biotechnology: products of secondary metabolism. 2nd ed. , vol.7 , pp. 397-488
    • Piepersberg, W.1    Distler, J.2
  • 32
    • 0026332251 scopus 로고
    • Genetics of streptomycin production in Streptomyces griseus. Molecular structure and putative function of genes strELMB2N
    • Pissowotzki K., Mansouri K., and Piepersberg W. Genetics of streptomycin production in Streptomyces griseus. Molecular structure and putative function of genes strELMB2N. Mol. Gen. Genet. 231 (1991) 113-123
    • (1991) Mol. Gen. Genet. , vol.231 , pp. 113-123
    • Pissowotzki, K.1    Mansouri, K.2    Piepersberg, W.3
  • 33
    • 0022432484 scopus 로고
    • Rapid transfer of DNA from agarose gels to nylon membranes
    • Reed K.C., and Mann D.A. Rapid transfer of DNA from agarose gels to nylon membranes. Nucleic Acids Res. 13 (1985) 7207-7221
    • (1985) Nucleic Acids Res. , vol.13 , pp. 7207-7221
    • Reed, K.C.1    Mann, D.A.2
  • 35
    • 0030896572 scopus 로고    scopus 로고
    • The Streptomyces ATP-binding component MsiK assists in cellobiose and maltose transport
    • Schlösser A., Kampers T., and Schrempf H. The Streptomyces ATP-binding component MsiK assists in cellobiose and maltose transport. J. Bacteriol. 179 (1997) 2092-2095
    • (1997) J. Bacteriol. , vol.179 , pp. 2092-2095
    • Schlösser, A.1    Kampers, T.2    Schrempf, H.3
  • 36
    • 0035282418 scopus 로고    scopus 로고
    • Synthesis of the Streptomyces lividans maltodextrin ABC transporter depends on the presence of the regulator MalR
    • Schlösser A., Weber A., and Schrempf H. Synthesis of the Streptomyces lividans maltodextrin ABC transporter depends on the presence of the regulator MalR. FEMS Microbiol. Lett. 196 (2001) 77-83
    • (2001) FEMS Microbiol. Lett. , vol.196 , pp. 77-83
    • Schlösser, A.1    Weber, A.2    Schrempf, H.3
  • 37
    • 33745134391 scopus 로고    scopus 로고
    • Genetic localization and heterologous expression of validamycin biosynthetic gene cluster isolated from Streptomyces hygroscopicus var. limoneus KCCM 11405 IFO 12704
    • Singh D., Seo M.J., Kwon H.J., Rajkarnikar A., Kim K.R., Kim S.O., and Suh J.W. Genetic localization and heterologous expression of validamycin biosynthetic gene cluster isolated from Streptomyces hygroscopicus var. limoneus KCCM 11405 IFO 12704. Gene 376 (2006) 13-23
    • (2006) Gene , vol.376 , pp. 13-23
    • Singh, D.1    Seo, M.J.2    Kwon, H.J.3    Rajkarnikar, A.4    Kim, K.R.5    Kim, S.O.6    Suh, J.W.7
  • 38
    • 0016774526 scopus 로고
    • A hydrophobic form of the small intestinal sucrose isomaltase complex
    • Sigrist H., Ronner P., and Semenza G. A hydrophobic form of the small intestinal sucrose isomaltase complex. Biochem. Biophys. Acta 406 (1975) 433-446
    • (1975) Biochem. Biophys. Acta , vol.406 , pp. 433-446
    • Sigrist, H.1    Ronner, P.2    Semenza, G.3
  • 39
    • 0026471501 scopus 로고
    • Gene probes for the detection of 6-deoxyhexose metabolism in secondary metabolite-producing streptomycetes
    • Stockmann M., and Piepersberg W. Gene probes for the detection of 6-deoxyhexose metabolism in secondary metabolite-producing streptomycetes. FEMS Microbiol. Lett. 90 (1992) 185-190
    • (1992) FEMS Microbiol. Lett. , vol.90 , pp. 185-190
    • Stockmann, M.1    Piepersberg, W.2
  • 40
    • 0033574676 scopus 로고    scopus 로고
    • 7-cyclitol synthase related to 3-dehydroquinate synthases and is involved in the biosynthesis of the α-glucosidase inhibitor acarbose
    • 7-cyclitol synthase related to 3-dehydroquinate synthases and is involved in the biosynthesis of the α-glucosidase inhibitor acarbose. J. Biol. Chem. 274 (1999) 10889-10896
    • (1999) J. Biol. Chem. , vol.274 , pp. 10889-10896
    • Stratmann, A.1    Mahmud, T.2    Lee, S.3    Distler, J.4    Floss, H.G.5    Piepersberg, W.6
  • 43
    • 0031018158 scopus 로고    scopus 로고
    • Substrate induction and glucose repression of maltose utilization by Streptomyces coelicolor A3(2) is controlled by MalR, a member of the Lacl-GalR family of regulatory genes
    • van Welzel G.P., White J., Young P., Postma P.W., and Bibb M.J. Substrate induction and glucose repression of maltose utilization by Streptomyces coelicolor A3(2) is controlled by MalR, a member of the Lacl-GalR family of regulatory genes. Mol. Microbiol. 23 (1997) 537-549
    • (1997) Mol. Microbiol. , vol.23 , pp. 537-549
    • van Welzel, G.P.1    White, J.2    Young, P.3    Postma, P.W.4    Bibb, M.J.5
  • 44
    • 0347337767 scopus 로고    scopus 로고
    • The biosynthesis and metabolism of acarbose in Actinoplanes SE50/110: a progress report
    • Wehmeier U.F. The biosynthesis and metabolism of acarbose in Actinoplanes SE50/110: a progress report. Biocat. Biotrans. 21 (2003) 279-285
    • (2003) Biocat. Biotrans. , vol.21 , pp. 279-285
    • Wehmeier, U.F.1
  • 45
    • 1542299147 scopus 로고    scopus 로고
    • Molecular biology and enzymology of the metabolism of the α-glucosidase inhibitor acarbose
    • Wehmeier U.F., and Piepersberg W. Molecular biology and enzymology of the metabolism of the α-glucosidase inhibitor acarbose. Appl. Microbiol. Biotechnol. 63 (2004) 613-625
    • (2004) Appl. Microbiol. Biotechnol. , vol.63 , pp. 613-625
    • Wehmeier, U.F.1    Piepersberg, W.2
  • 46
    • 33845318295 scopus 로고
    • Interaction of pyrophosphate moieties with α-helices in dinucleotide binding proteins
    • Wierenga R., De Maeyer M., and Hol W. Interaction of pyrophosphate moieties with α-helices in dinucleotide binding proteins. Biochemistry 24 (1985) 1346-1357
    • (1985) Biochemistry , vol.24 , pp. 1346-1357
    • Wierenga, R.1    De Maeyer, M.2    Hol, W.3
  • 47
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors
    • Yanisch-Perron C., Vieira J., and Messing J. Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 33 (1985) 103-119
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3
  • 48
    • 0021033037 scopus 로고
    • New α-amylase inhibitor, trestatins. II. Structure determination of trestatins A, B and C
    • Yokose K., Ogawa K., Sano T., Watanabe K., Maruyama H.B., and Suhara Y. New α-amylase inhibitor, trestatins. II. Structure determination of trestatins A, B and C. J. Antibiot. (Tokyo) 36 (1983) 1166-1175
    • (1983) J. Antibiot. (Tokyo) , vol.36 , pp. 1166-1175
    • Yokose, K.1    Ogawa, K.2    Sano, T.3    Watanabe, K.4    Maruyama, H.B.5    Suhara, Y.6
  • 49
    • 0345270037 scopus 로고    scopus 로고
    • The acarbose-biosynthetic enzyme AcbO from Actinoplanes sp. SE 50/110 is a 2-epi-5-epi-valiolone-7-phosphate 2-epimerase
    • Zhang C.S., Podeschwa M., Altenbach H.J., Piepersberg W., and Wehmeier U.F. The acarbose-biosynthetic enzyme AcbO from Actinoplanes sp. SE 50/110 is a 2-epi-5-epi-valiolone-7-phosphate 2-epimerase. FEBS Lett. 540 (2003) 47-52
    • (2003) FEBS Lett. , vol.540 , pp. 47-52
    • Zhang, C.S.1    Podeschwa, M.2    Altenbach, H.J.3    Piepersberg, W.4    Wehmeier, U.F.5
  • 50
    • 0344838677 scopus 로고    scopus 로고
    • Identification of a 1-epi-valienol 7-kinase activity in the producer of acarbose, Actinoplanes sp. SE50/110
    • Zhang C.S., Podeschwa M., Block O., Altenbach H.J., Piepersberg W., and Wehmeier U.F. Identification of a 1-epi-valienol 7-kinase activity in the producer of acarbose, Actinoplanes sp. SE50/110. FEBS Lett. 540 (2003) 53-57
    • (2003) FEBS Lett. , vol.540 , pp. 53-57
    • Zhang, C.S.1    Podeschwa, M.2    Block, O.3    Altenbach, H.J.4    Piepersberg, W.5    Wehmeier, U.F.6
  • 51
    • 0037151092 scopus 로고    scopus 로고
    • Biosynthesis of the C(7)-cyclitol moiety of acarbose in Actinoplanes species SE50/110. 7-O-phosphorylation of the initial cyclitol precursor leads to proposal of a new biosynthetic pathway
    • Zhang C.S., Stratmann A., Block O., Brueckner R., Podeschwa M., Altenbach H.J., Wehmeier U.F., and Piepersberg W. Biosynthesis of the C(7)-cyclitol moiety of acarbose in Actinoplanes species SE50/110. 7-O-phosphorylation of the initial cyclitol precursor leads to proposal of a new biosynthetic pathway. J. Biol. Chem. 277 (2002) 22853-22862
    • (2002) J. Biol. Chem. , vol.277 , pp. 22853-22862
    • Zhang, C.S.1    Stratmann, A.2    Block, O.3    Brueckner, R.4    Podeschwa, M.5    Altenbach, H.J.6    Wehmeier, U.F.7    Piepersberg, W.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.