메뉴 건너뛰기




Volumn 56, Issue 8, 2012, Pages 4175-4183

Different biosynthetic pathways to fosfomycin in Pseudomonas syringae and Streptomyces species

Author keywords

[No Author keywords available]

Indexed keywords

2 HYDROXYPROPYLPHOSPHONATE; 3 (N ACETYL N HYDROXYAMINO)PROPYLPHOSPHONIC ACID; ANTIBIOTIC AGENT; BACTERIAL ENZYME; CARBOXYLYASE; CITRATE SYNTHASE; FOSFOMYCIN; PHOSPHINOTHRICIN; PHOSPHOENOLPYRUVATE; PHOSPHONIC ACID DERIVATIVE; PHOSPHONOPYRUVATE; PSF2 PROTEIN; PYRUVIC ACID DERIVATIVE; UNCLASSIFIED DRUG;

EID: 84864389225     PISSN: 00664804     EISSN: 10986596     Source Type: Journal    
DOI: 10.1128/AAC.06478-11     Document Type: Article
Times cited : (56)

References (62)
  • 1
    • 0025632955 scopus 로고
    • Brief overview of single-dose therapy for uncomplicated urinary tract infections
    • Bailey RR. 1990. Brief overview of single-dose therapy for uncomplicated urinary tract infections. Chemotherapy 36(Suppl 1):27-30.
    • (1990) Chemotherapy , vol.36 , Issue.SUPPL. 1 , pp. 27-30
    • Bailey, R.R.1
  • 2
    • 0027328150 scopus 로고
    • Management of lower urinary tract infections
    • Bailey RR. 1993. Management of lower urinary tract infections. Drugs 45(Suppl 3):139-144. (Pubitemid 23242928)
    • (1993) Drugs , vol.46 , Issue.SUPPL. 3 , pp. 139-144
    • Bailey, R.R.1
  • 3
    • 84873799110 scopus 로고
    • Studies on lysogenesis. I. The mode of phage liberation by lysogenic Escherichia coli
    • Bertani G. 1951. Studies on lysogenesis. I. The mode of phage liberation by lysogenic Escherichia coli. J. Bacteriol. 62:293-300.
    • (1951) J. Bacteriol. , vol.62 , pp. 293-300
    • Bertani, G.1
  • 5
    • 11244354656 scopus 로고    scopus 로고
    • Molecular cloning, sequence analysis, and heterologous expression of the phosphinothricin tripeptide biosynthetic gene cluster from Streptomyces viridochromogenes DSM 40736
    • DOI 10.1128/AAC.49.1.230-240.2005
    • Blodgett JA, Zhang JK, Metcalf WW. 2005. Molecular cloning, sequence analysis, and heterologous expression of the phosphinothricin tripeptide biosynthetic gene cluster from Streptomyces viridochromogenes DSM 40736. Antimicrob. Agents Chemother. 49:230-240. (Pubitemid 40065797)
    • (2005) Antimicrobial Agents and Chemotherapy , vol.49 , Issue.1 , pp. 230-240
    • Blodgett, J.A.V.1    Zhang, J.K.2    Metcalf, W.W.3
  • 6
    • 75149160998 scopus 로고    scopus 로고
    • Biosynthesis of rhizocticins, antifungal phosphonate oligopeptides produced by Bacillus subtilis ATCC6633
    • Borisova SA, Circello BT, Zhang JK, van der Donk WA, Metcalf WW. 2010. Biosynthesis of rhizocticins, antifungal phosphonate oligopeptides produced by Bacillus subtilis ATCC6633. Chem. Biol. 17:28-37.
    • (2010) Chem. Biol. , vol.17 , pp. 28-37
    • Borisova, S.A.1    Circello, B.T.2    Zhang, J.K.3    Van Der Donk, W.A.4    Metcalf, W.W.5
  • 7
    • 0023785036 scopus 로고
    • Catalysis and thermodynamics of the phosphoenolpyruvate/phosphopyruvate rearrangement. Entry into the phosphonate class of naturally occurring organophosphorus compounds
    • Bowman E, McQueney M, Barry RJ, Dunaway-Mariano D. 1988. Catalysis and thermodynamics of the phosphoenolpyruvate/phosphopyruvate rearrangement. Entry into the phosphonate class of naturally occurring organophosphorus compounds. J. Am. Chem. Soc. 110:5575-5576.
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 5575-5576
    • Bowman, E.1    McQueney, M.2    Barry, R.J.3    Dunaway-Mariano, D.4
  • 8
    • 0014662821 scopus 로고
    • Phosphonomycin: Structure and synthesis
    • Christensen BG, et al. 1969. Phosphonomycin: structure and synthesis. Science 166:123-125.
    • (1969) Science , vol.166 , pp. 123-125
    • Christensen, B.G.1
  • 9
    • 78651187486 scopus 로고
    • The biosynthesis of phenylalanine and tyrosine; enzymes converting chorismic acid into prephenic acid and their relationships to prephenate dehydratase and prephenate dehydrogenase
    • Cotton RG, Gibson F. 1965. The biosynthesis of phenylalanine and tyrosine; enzymes converting chorismic acid into prephenic acid and their relationships to prephenate dehydratase and prephenate dehydrogenase. Biochim. Biophys. Acta 100:76-88.
    • (1965) Biochim. Biophys. Acta , vol.100 , pp. 76-88
    • Cotton, R.G.1    Gibson, F.2
  • 11
    • 0027385020 scopus 로고
    • Early and late responses of TOL promoters to pathway inducers: Identification of postexponential promoters in Pseudomonas putida with lacZ- tet bicistronic reporters
    • de Lorenzo V, Cases I, Herrero M, Timmis KN. 1993. Early and late responses of TOL promoters to pathway inducers: identification of postexponential promoters in Pseudomonas putida with lacZ-tet bicistronic reporters. J. Bacteriol. 175:6902-6907. (Pubitemid 23322440)
    • (1993) Journal of Bacteriology , vol.175 , Issue.21 , pp. 6902-6907
    • De Lorenzo, V.1    Cases, I.2    Herrero, M.3    Timmis, K.N.4
  • 12
    • 0031869639 scopus 로고    scopus 로고
    • Plasposons: Modular self-cloning minitransposon derivatives for rapid genetic analysis of gram-negative bacterial genomes
    • Dennis JJ, Zylstra GJ. 1998. Plasposons: modular self-cloning minitransposon derivatives for rapid genetic analysis of gram-negative bacterial genomes. Appl. Environ. Microbiol. 64:2710-2715. (Pubitemid 28303324)
    • (1998) Applied and Environmental Microbiology , vol.64 , Issue.7 , pp. 2710-2715
    • Dennis, J.J.1    Zylstra, G.J.2
  • 13
    • 0038056150 scopus 로고    scopus 로고
    • New insights on trehalose: A multifunctional molecule
    • DOI 10.1093/glycob/cwg047
    • Elbein AD, Pan YT, Pastuszak I, Carroll D. 2003. New insights on trehalose: a multifunctional molecule. Glycobiology 13:17R-27R. doi: 10.1093/glycob/cwg047. (Pubitemid 36592310)
    • (2003) Glycobiology , vol.13 , Issue.4
    • Elbein, A.D.1    Pan, Y.T.2    Pastuszak, I.3    Carroll, D.4
  • 14
    • 49449119076 scopus 로고    scopus 로고
    • Cloning, expression, and biochemical characterization of Streptomyces rubellomurinus genes required for biosynthesis of antimalarial compound FR900098
    • Eliot AC, et al. 2008. Cloning, expression, and biochemical characterization of Streptomyces rubellomurinus genes required for biosynthesis of antimalarial compound FR900098. Chem. Biol. 15:765-770.
    • (2008) Chem. Biol. , vol.15 , pp. 765-770
    • Eliot, A.C.1
  • 16
    • 0029008562 scopus 로고
    • Product of fosC, a gene from Pseudomonas syringae, mediates fosfomycin resistance by using ATP as cosubstrate
    • Garcia P, Arca P, Evaristo Suarez J. 1995. Product of fosC, a gene from Pseudomonas syringae, mediates fosfomycin resistance by using ATP as cosubstrate. Antimicrob. Agents Chemother. 39:1569-1573.
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 1569-1573
    • Garcia, P.1    Arca, P.2    Evaristo Suarez, J.3
  • 18
    • 70450195870 scopus 로고    scopus 로고
    • Polyketide decarboxylative chain termination preceded by o-sulfonation in curacin A biosynthesis
    • Gu L, et al. 2009. Polyketide decarboxylative chain termination preceded by o-sulfonation in curacin A biosynthesis. J. Am. Chem. Soc. 131:16033-16035.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 16033-16035
    • Gu, L.1
  • 19
    • 0008713567 scopus 로고
    • Biosynthesis of natural products with a P-C bond. Part 8. On the origin of the oxirane oxygen atom of fosfomycin in Streptomyces fradiae
    • Hammerschmidt F. 1991. Biosynthesis of natural products with a P-C bond. Part 8. On the origin of the oxirane oxygen atom of fosfomycin in Streptomyces fradiae. J. Chem. Soc. Perkin Trans. 1:1993-1996.
    • (1991) J. Chem. Soc. Perkin Trans. , vol.1 , pp. 1993-1996
    • Hammerschmidt, F.1
  • 20
    • 0027966348 scopus 로고
    • 18O]hydroxyethylphosphonic acid into fosfomycin in Streptomyces fradiae - An unusual methyl transfer
    • 18O]hydroxyethylphosphonic acid into fosfomycin in Streptomyces fradiae - an unusual methyl transfer. Angew. Chem. Int. Ed. Engl. 33:341-342.
    • (1994) Angew. Chem. Int. Ed. Engl. , vol.33 , pp. 341-342
    • Hammerschmidt, F.1
  • 22
    • 0028851951 scopus 로고
    • Cloning and nucleotide sequence of fosfomycin biosynthetic genes of Streptomyces wedmorensis
    • Hidaka T, et al. 1995. Cloning and nucleotide sequence of fosfomycin biosynthetic genes of Streptomyces wedmorensis. Mol. Gen. Genet. 249:274-280.
    • (1995) Mol. Gen. Genet. , vol.249 , pp. 274-280
    • Hidaka, T.1
  • 23
    • 0026755651 scopus 로고
    • Studies on the biosynthesis of fosfomycin. 3. Detection of phosphoenol-pyruvate phosphomutase activity in a fosfomycin high-producing strain of Streptomyces wedmorensis and characterization of its blocked mutant NP-7
    • Hidaka T, Iwakura H, Imai S, Seto H. 1992. Studies on the biosynthesis of fosfomycin. 3. Detection of phosphoenol-pyruvate phosphomutase activity in a fosfomycin high-producing strain of Streptomyces wedmorensis and characterization of its blocked mutant NP-7. J. Antibiot. 45:1008-1010.
    • (1992) J. Antibiot. , vol.45 , pp. 1008-1010
    • Hidaka, T.1    Iwakura, H.2    Imai, S.3    Seto, H.4
  • 24
    • 0032715475 scopus 로고    scopus 로고
    • Studies on the biosynthesis of bialaphos (SF-1293). 18. 2-phosphinomethylmalic acid synthase: A descendant of (R)-citrate synthase? [2]
    • Hidaka T, Shimotohno KW, Morishita T, Seto H. 1999. Studies on the biosynthesis of bialaphos (SF-1293). 18. 2-Phosphinomethylmalic acid synthase: a descendant of (R)-citrate synthase? J. Antibiot. 52:925-931. (Pubitemid 29532966)
    • (1999) Journal of Antibiotics , vol.52 , Issue.10 , pp. 925-931
    • Hidaka, T.1    Shimotohno, K.W.2    Morishita, T.3    Seto, H.4
  • 25
    • 27144467824 scopus 로고    scopus 로고
    • Structural insight into antibiotic fosfomycin biosynthesis by a mononuclear iron enzyme
    • DOI 10.1038/nature03924, PII N03924
    • Higgins LJ, Yan F, Liu P, Liu HW, Drennan CL. 2005. Structural insight into antibiotic fosfomycin biosynthesis by a mononuclear iron enzyme. Nature 437:838-844. (Pubitemid 41486753)
    • (2005) Nature , vol.437 , Issue.7060 , pp. 838-844
    • Higgins, L.J.1    Yan, F.2    Liu, P.3    Liu, H.-W.4    Drennan, C.L.5
  • 26
    • 0022460061 scopus 로고
    • Mevalonate-5-diphosphate decarboxylase: Stereochemical course of ATP-dependent phosphorylation of mevalonate 5-diphosphate
    • Iyengar R, Cardemil E, Frey PA. 1986. Mevalonate-5-diphosphate decarboxylase: stereochemical course of ATP-dependent phosphorylation of mevalonate 5-diphosphate. Biochemistry 25:4693-4698. (Pubitemid 16010202)
    • (1986) Biochemistry , vol.25 , Issue.16 , pp. 4693-4698
    • Iyengar, R.1    Cardemil, E.2    Frey, P.A.3
  • 27
    • 75149146564 scopus 로고    scopus 로고
    • Deciphering the late biosynthetic steps of antimalarial compound FR-900098
    • Johannes TW, et al. 2010. Deciphering the late biosynthetic steps of antimalarial compound FR-900098. Chem. Biol. 17:57-64.
    • (2010) Chem. Biol. , vol.17 , pp. 57-64
    • Johannes, T.W.1
  • 28
    • 67650729745 scopus 로고    scopus 로고
    • The structural and biochemical foundations of thiamin biosynthesis
    • Jurgenson CT, Begley TP, Ealick SE. 2009. The structural and biochemical foundations of thiamin biosynthesis. Annu. Rev. Biochem. 78:569-603.
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 569-603
    • Jurgenson, C.T.1    Begley, T.P.2    Ealick, S.E.3
  • 30
    • 0025257307 scopus 로고
    • Fosfadecin and fosfocytocin, new nucleotide antibiotics produced by bacteria
    • Katayama N, Tsubotani S, Nozaki Y, Harada S, Ono H. 1990. Fosfadecin and fosfocytocin, new nucleotide antibiotics produced by bacteria. J. Antibiot. 43:238-246. (Pubitemid 20106386)
    • (1990) Journal of Antibiotics , vol.43 , Issue.3 , pp. 238-246
    • Katayama, N.1    Tsubotani, S.2    Nozaki, Y.3    Harada, S.4    Ono, H.5
  • 31
    • 0034001144 scopus 로고    scopus 로고
    • Characterization of the fomA and fomB gene products from Streptomyces wedmorensis, which confer fosfomycin resistance on Escherichia coli
    • DOI 10.1128/AAC.44.3.647-650.2000
    • Kobayashi S, Kuzuyama T, Seto H. 2000. Characterization of the fomA and fomB gene products from Streptomyces wedmorensis, which confer fosfomycin resistance on Escherichia coli. Antimicrob. Agents Chemother. 44:647-650. (Pubitemid 30117955)
    • (2000) Antimicrobial Agents and Chemotherapy , vol.44 , Issue.3 , pp. 647-650
    • Kobayashi, S.1    Kuzuyama, T.2    Seto, H.3
  • 32
    • 78651391299 scopus 로고    scopus 로고
    • Protein thiocarboxylate-dependent methionine biosynthesis in Wolinella succinogenes
    • Krishnamoorthy K, Begley TP. 2011. Protein thiocarboxylate-dependent methionine biosynthesis in Wolinella succinogenes. J. Am. Chem. Soc. 133:379-386.
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 379-386
    • Krishnamoorthy, K.1    Begley, T.P.2
  • 33
    • 0027433707 scopus 로고
    • Studies on the biosynthesis of fosfomycin V cloning of genes for fosfomycin biosynthesis
    • Kuzuyama T, Hidaka T, Imai S, Seto H. 1993. Studies on the biosynthesis of fosfomycin. V. Cloning of genes for fosfomycin biosynthesis. J. Antibiot. 46:1478-1480. (Pubitemid 23290998)
    • (1993) Journal of Antibiotics , vol.46 , Issue.9 , pp. 1478-1480
    • Kuzuyama, T.1    Hidaka, T.2    Imai, S.3    Seto, H.4
  • 34
    • 0027051383 scopus 로고
    • Studies on the biosynthesis of fosfomycin. 4. The biosynthetic origin of the methyl group of fosfomycin
    • Kuzuyama T, Hidaka T, Kamigiri K, Imai S, Seto H. 1992. Studies on the biosynthesis of fosfomycin. 4. The biosynthetic origin of the methyl group of fosfomycin. J. Antibiot. 45:1812-1814. (Pubitemid 23015468)
    • (1992) Journal of Antibiotics , vol.45 , Issue.11 , pp. 1812-1814
    • Kuzuyama, T.1    Hidaka, T.2    Kamigiri, K.3    Imai, S.4    Seto, H.5
  • 35
    • 0029951989 scopus 로고    scopus 로고
    • Fosfomycin monophosphate and fosfomycin diphosphate, two inactivated fosfomycin derivatives formed by gene products of fomA and fomB from a fosfomycin producing organism Streptomyces wedmorensis [1]
    • Kuzuyama T, Kobayashi S, O'Hara K, Hidaka T, Seto H. 1996. Fosfomycin monophosphate and fosfomycin diphosphate, two inactivated fosfomycin derivatives formed by gene products of FomA and FomB from a fosfomycin producing organism Streptomyces wedmorensis. J. Antibiot. 49:502-504. (Pubitemid 26178958)
    • (1996) Journal of Antibiotics , vol.49 , Issue.5 , pp. 502-504
    • Kuzuyama, T.1    Kobayashi, S.2    O'Hara, K.3    Hidaka, T.4    Seto, H.5
  • 36
    • 0033253437 scopus 로고    scopus 로고
    • Cloning and expression in Escherichia coli of 2-hydroxypropylphosphonic acid epoxidase from the fosfomycin-producing organism, Pseudomonas syringae PB-5123
    • Kuzuyama T, Seki T, Kobayashi S, Hidaka T, Seto H. 1999. Cloning and expression in Escherichia coli of 2-hydroxypropylphosphonic acid epoxidase from the fosfomycin-producing organism, Pseudomonas syringae PB-5123. Biosci. Biotechnol. Biochem. 63:2222-2224. (Pubitemid 129549052)
    • (1999) Bioscience, Biotechnology and Biochemistry , vol.63 , Issue.12 , pp. 2222-2224
    • Kuzuyama, T.1    Seki, T.2    Kobayashi, S.3    Hidaka, T.4    Seto, H.5
  • 38
    • 0028070055 scopus 로고
    • Kinetics, stoichiometry, and identification of the reactive thiolate in the inactivation of UDP-GlcNAc enolpyruvoyl transferase by the antibiotic fosfomycin
    • Marquardt JL, et al. 1994. Kinetics, stoichiometry, and identification of the reactive thiolate in the inactivation of UDP-GlcNAc enolpyruvoyl transferase by the antibiotic fosfomycin. Biochemistry 33:10646-10651. (Pubitemid 24292285)
    • (1994) Biochemistry , vol.33 , Issue.35 , pp. 10646-10651
    • Marquardt, J.L.1    Brown, E.D.2    Lane, W.S.3    Haley, T.M.4    Ichikawa, Y.5    Wong, C.H.6    Walsh, C.T.7
  • 39
    • 67650743221 scopus 로고    scopus 로고
    • Biosynthesis of phosphonic and phosphinic acid natural products
    • Metcalf WW, van der Donk WA. 2009. Biosynthesis of phosphonic and phosphinic acid natural products. Annu. Rev. Biochem. 78:65-94.
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 65-94
    • Metcalf, W.W.1    Van Der Donk, W.A.2
  • 40
    • 49749099580 scopus 로고    scopus 로고
    • Purification and characterization of the epoxidase catalyzing the formation of fosfomycin from Pseudomonas syringae
    • Munos JW, et al. 2008. Purification and characterization of the epoxidase catalyzing the formation of fosfomycin from Pseudomonas syringae. Biochemistry 47:8726-8735.
    • (2008) Biochemistry , vol.47 , pp. 8726-8735
    • Munos, J.W.1
  • 41
    • 0033969032 scopus 로고    scopus 로고
    • Identification and expression of the gene encoding phosphonopyruvate decarboxylase of Streptomyces hygroscopicus
    • DOI 10.1016/S0167-4781(99)00249-3, PII S0167478199002493
    • Nakashita H, Kozuka K, Hidaka T, Hara O, Seto H. 2000. Identification and expression of the gene encoding phosphonopyruvate decarboxylase of Streptomyces hygroscopicus. Biochim. Biophys. Acta 1490:159-162. (Pubitemid 30070147)
    • (2000) Biochimica et Biophysica Acta - Gene Structure and Expression , vol.1490 , Issue.1-2 , pp. 159-162
    • Nakashita, H.1    Kozuka, K.2    Hidaka, T.3    Hara, O.4    Seto, H.5
  • 42
    • 57649115441 scopus 로고    scopus 로고
    • Crystal structure of fosfomycin resistance kinase FomA from Streptomyces wedmorensis
    • Pakhomova S, Bartlett SG, Augustus A, Kuzuyama T, Newcomer ME. 2008. Crystal structure of fosfomycin resistance kinase FomA from Streptomyces wedmorensis. J. Biol. Chem. 283:28518-28526.
    • (2008) J. Biol. Chem. , vol.283 , pp. 28518-28526
    • Pakhomova, S.1    Bartlett, S.G.2    Augustus, A.3    Kuzuyama, T.4    Newcomer, M.E.5
  • 43
    • 0031003980 scopus 로고    scopus 로고
    • Fosfomycin Tromethamine. A review of its antibacterial activity, pharmacokinetic properties and therapeutic efficacy as a single-dose oral treatment for acute uncomplicated lower urinary tract infections
    • Patel SS, Balfour JA, Bryson HM. 1997. Fosfomycin tromethamine. A review of its antibacterial activity, pharmacokinetic properties and therapeutic efficacy as a single-dose oral treatment for acute uncomplicated lower urinary tract infections. Drugs 53:637-656. (Pubitemid 27145957)
    • (1997) Drugs , vol.53 , Issue.4 , pp. 637-656
    • Patel, S.S.1    Balfour, J.A.2    Bryson, H.M.3
  • 44
    • 0026657239 scopus 로고
    • Cloning, overexpression and mechanistic studies of carboxyphosphonoenolpyruvate mutase from Streptomyces hygroscopicus
    • Pollack SJ, Freeman S, Pompliano DL, Knowles JR. 1992. Cloning, overexpression and mechanistic studies of carboxyphosphonoenolpyruvate mutase from Streptomyces hygroscopicus. Eur. J. Biochem. 209:735-743.
    • (1992) Eur. J. Biochem. , vol.209 , pp. 735-743
    • Pollack, S.J.1    Freeman, S.2    Pompliano, D.L.3    Knowles, J.R.4
  • 45
    • 0027058460 scopus 로고
    • Treatment of bacteriuria in pregnancy with single dose fosfomycin trometamol: A review
    • Reeves DS. 1992. Treatment of bacteriuria in pregnancy with single dose fosfomycin trometamol: a review. Infection 20(Suppl 4):S313-S316. (Pubitemid 23081503)
    • (1992) Infection , vol.20 , Issue.SUPPL. 4
    • Reeves, D.S.1
  • 47
    • 0014444031 scopus 로고
    • Chorismate mutase-prephenate dehydratase. Partial purification and properties of the enzyme from Salmonella typhimurium
    • Schmit JC, Zalkin H. 1969. Chorismate mutase-prephenate dehydratase. Partial purification and properties of the enzyme from Salmonella typhimurium. Biochemistry 8:174-181.
    • (1969) Biochemistry , vol.8 , pp. 174-181
    • Schmit, J.C.1    Zalkin, H.2
  • 49
    • 0026050593 scopus 로고
    • Studies on the biosynthesis of fosfomycin. 2. Conversion of 2-hydroxypropyl-phosphonic acid to fosfomycin by blocked mutants of Streptomyces wedmorensis
    • Seto H, et al. 1991. Studies on the biosynthesis of fosfomycin. 2. Conversion of 2-hydroxypropyl-phosphonic acid to fosfomycin by blocked mutants of Streptomyces wedmorensis. J. Antibiot. 44:1286-1288.
    • (1991) J. Antibiot. , vol.44 , pp. 1286-1288
    • Seto, H.1
  • 50
    • 0033213404 scopus 로고    scopus 로고
    • Bioactive natural products with carbon-phosphorus bonds and their biosynthesis
    • DOI 10.1039/a809398i
    • Seto H, Kuzuyama T. 1999. Bioactive natural products with carbonphosphorus bonds and their biosynthesis. Nat. Prod. Rep. 16:589-596. (Pubitemid 29501613)
    • (1999) Natural Product Reports , vol.16 , Issue.5 , pp. 589-596
    • Seto, H.1    Kuzuyama, T.2
  • 51
    • 53149083025 scopus 로고    scopus 로고
    • Biosynthesis of 2-hydroxyethylphosphonate, an unexpected intermediate common to multiple phosphonate biosynthetic pathways
    • Shao Z, et al. 2008. Biosynthesis of 2-hydroxyethylphosphonate, an unexpected intermediate common to multiple phosphonate biosynthetic pathways. J. Biol. Chem. 283:23161-23168.
    • (2008) J. Biol. Chem. , vol.283 , pp. 23161-23168
    • Shao, Z.1
  • 52
    • 0023788731 scopus 로고
    • Studies on the biosynthesis of bialaphos (SF-1293). 8. Purification and characterization of 2-phosphinomethylmalic acid synthase from Streptomyces hygroscopicus SF-1293
    • Shimotohno KW, Seto H, Otake N, Imai S, Murakami T. 1988. Studies on the biosynthesis of bialaphos (SF-1293). 8. Purification and characterization of 2-phosphinomethylmalic acid synthase from Streptomyces hygroscopicus SF-1293. J. Antibiot. 41:1057-1065.
    • (1988) J. Antibiot. , vol.41 , pp. 1057-1065
    • Shimotohno, K.W.1    Seto, H.2    Otake, N.3    Imai, S.4    Murakami, T.5
  • 53
    • 0022459868 scopus 로고
    • Production of fosfomycin (phosphonomycin) by Pseudomonas syringae
    • Shoji J, et al. 1986. Production of fosfomycin (phosphonomycin) by Pseudomonas syringae. J. Antibiot. 39:1011-1012. (Pubitemid 16038823)
    • (1986) Journal of Antibiotics , vol.39 , Issue.7 , pp. 1011-1012
    • Shoji, J.1    Kato, T.2    Hinoo, H.3
  • 54
    • 0014427410 scopus 로고
    • A new silylation reagent for amino acids bis(trimethylsilyl) trifluoroacetamide (BSTFA)
    • Stalling DL, Gehrke CW, Zumwalt RW. 1968. A new silylation reagent for amino acids bis(trimethylsilyl)trifluoroacetamide (BSTFA). Biochem. Biophys. Res. Commun. 31:616-622.
    • (1968) Biochem. Biophys. Res. Commun. , vol.31 , pp. 616-622
    • Stalling, D.L.1    Gehrke, C.W.2    Zumwalt, R.W.3
  • 56
    • 0031893912 scopus 로고    scopus 로고
    • Single-dose treatment of acute cystitis with fosfomycin tromethamine
    • DOI 10.1345/aph.17227
    • Stein GE. 1998. Single-dose treatment of acute cystitis with fosfomycin tromethamine. Ann. Pharmacother. 32:215-219. (Pubitemid 28082335)
    • (1998) Annals of Pharmacotherapy , vol.32 , Issue.2 , pp. 215-219
    • Stein, G.E.1
  • 57
    • 0025283867 scopus 로고
    • Use of T7 RNA polymerase to direct expression of cloned genes
    • DOI 10.1016/0076-6879(90)85008-C
    • Studier FW, Rosenberg AH, Dunn JJ, Dubendorff JW. 1990. Use of T7 RNA polymerase to direct expression of cloned genes. Methods Enzymol. 185:60-89. (Pubitemid 20219811)
    • (1990) Methods in Enzymology , vol.185 , pp. 60-89
    • Studier, F.W.1    Rosenberg, A.H.2    Dunn, J.J.3    Dubendorff, J.W.4
  • 58
    • 33845955006 scopus 로고    scopus 로고
    • Rings, radicals, and regeneration: The early years of a bioorganic laboratory
    • van der Donk WA. 2006. Rings, radicals, and regeneration: the early years of a bioorganic laboratory. J. Org. Chem. 71:9561-9571.
    • (2006) J. Org. Chem. , vol.71 , pp. 9561-9571
    • Van Der Donk, W.A.1
  • 59
    • 33846241262 scopus 로고    scopus 로고
    • New insight into the mechanism of methyl transfer during the biosynthesis of fosfomycin
    • DOI 10.1039/b614678c
    • Woodyer RD, Li G, Zhao H, van der Donk WA. 2007. New insight into the mechanism of methyl transfer during the biosynthesis of fosfomycin. Chem. Commun. (Camb.), p359-361. (Pubitemid 46105515)
    • (2007) Chemical Communications , Issue.4 , pp. 359-361
    • Woodyer, R.D.1    Li, G.2    Zhao, H.3    Van Der, D.W.A.4
  • 61
    • 84859891708 scopus 로고    scopus 로고
    • Radical-mediated enzymatic methylation: A tale of two SAMs
    • Zhang Q, van der Donk WA, Liu W. 2012. Radical-mediated enzymatic methylation: a tale of two SAMs. Acc. Chem. Res. 45:555-564.
    • (2012) Acc. Chem. Res. , vol.45 , pp. 555-564
    • Zhang, Q.1    Van Der Donk, W.A.2    Liu, W.3
  • 62
    • 0037011396 scopus 로고    scopus 로고
    • Mechanistic studies of HPP epoxidase: Configuration of the substrate governs its enzymatic fate
    • Zhao ZB, et al. 2002. Mechanistic studies of HPP epoxidase: configuration of the substrate governs its enzymatic fate. Angew. Chem. Int. Ed. Engl. 41:4529-4532.
    • (2002) Angew. Chem. Int. Ed. Engl. , vol.41 , pp. 4529-4532
    • Zhao, Z.B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.