메뉴 건너뛰기




Volumn 107, Issue 41, 2010, Pages 17557-17562

Characterization and structure of DhpI, a phosphonate O-methyltransferase involved in dehydrophos biosynthesis

Author keywords

Antibiotics; Bioengineering; Conformational change; Domain swap; X ray crystallography

Indexed keywords

1 HYDROXYETHYLPHOSPHONATE; 1,2 DIHYDROXYETHYLPHOSPHONATE; ACETYL 1 AMINOETHYLPHOSPHONATE; DEHYDROPHOS; PHOSPHONATE O METHYLTRANSFERASE; PHOSPHONIC ACID DERIVATIVE; PROTEIN METHYLTRANSFERASE; S ADENOSYLMETHIONINE; TRIPEPTIDE DERIVATIVE; UNCLASSIFIED DRUG;

EID: 78049274321     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1006848107     Document Type: Article
Times cited : (40)

References (38)
  • 1
    • 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
  • 2
    • 0033213404 scopus 로고    scopus 로고
    • Bioactive natural products with carbon-phosphorus bonds and their biosynthesis
    • Seto H, Kuzuyama T (1999) Bioactive natural products with carbon-phosphorus bonds and their biosynthesis. Nat Prod Rep 16:589-596.
    • (1999) Nat Prod Rep , vol.16 , pp. 589-596
    • Seto, H.1    Kuzuyama, T.2
  • 3
    • 33846241262 scopus 로고    scopus 로고
    • New insight into the mechanism of methyl transfer during the biosynthesis of fosfomycin
    • 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 359-361.
    • (2007) Chem Commun , pp. 359-361
    • Woodyer, R.D.1    Li, G.2    Zhao, H.3    Van Der Donk, W.A.4
  • 4
    • 33750971144 scopus 로고    scopus 로고
    • Heterologous production of fosfomycin and identification of the minimal biosynthetic cluster
    • Woodyer RD, et al. (2006) Heterologous production of fosfomycin and identification of the minimal biosynthetic cluster. Chem Biol 13:1171-1182.
    • (2006) Chem Biol , vol.13 , pp. 1171-1182
    • Woodyer, R.D.1
  • 5
    • 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
  • 6
    • 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
  • 7
    • 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
  • 8
    • 34447544332 scopus 로고    scopus 로고
    • Unusual transformations in the biosynthesis of the antibiotic phosphinothricin tripeptide
    • Blodgett JA, et al. (2007) Unusual transformations in the biosynthesis of the antibiotic phosphinothricin tripeptide. Nat Chem Biol 3:480-485.
    • (2007) Nat Chem Biol , vol.3 , pp. 480-485
    • Blodgett, J.A.1
  • 9
    • 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
  • 10
    • 67149140355 scopus 로고    scopus 로고
    • An unusual carbon-carbon bond cleavage reaction during phosphinothricin biosynthesis
    • Cicchillo RM, et al. (2009) An unusual carbon-carbon bond cleavage reaction during phosphinothricin biosynthesis. Nature 459:871-874.
    • (2009) Nature , vol.459 , pp. 871-874
    • Cicchillo, R.M.1
  • 11
    • 70450208557 scopus 로고    scopus 로고
    • Hydroperoxylation by hydroxyethylphosphonate dioxygenase
    • Whitteck JT, Cicchillo RM, van der Donk WA (2009) Hydroperoxylation by hydroxyethylphosphonate dioxygenase. J Am Chem Soc 131:16225-16232.
    • (2009) J Am Chem Soc , vol.131 , pp. 16225-16232
    • Whitteck, J.T.1    Cicchillo, R.M.2    Van Der Donk, W.A.3
  • 12
    • 67049115710 scopus 로고    scopus 로고
    • In vitro characterization of a heterologously expressed nonribosomal peptide synthetase involved in phosphinothricin tripeptide biosynthesis
    • Lee JH, Evans BS, Li G, Kelleher NL, van der Donk WA(2009) In vitro characterization of a heterologously expressed nonribosomal peptide synthetase involved in phosphinothricin tripeptide biosynthesis. Biochemistry 48:5054-5056.
    • (2009) Biochemistry , vol.48 , pp. 5054-5056
    • Lee, J.H.1    Evans, B.S.2    Li, G.3    Kelleher, N.L.4    Van Der Donk, W.A.5
  • 13
    • 0002970187 scopus 로고
    • Inhibition of pea leaf glutamine synthetase by methionine sulfoximine, phosphinothricin, and other glutamate analogs
    • Leason M, Cunliffe D, Parkin D, Lea PJ, Miflin BJ (1982) Inhibition of pea leaf glutamine synthetase by methionine sulfoximine, phosphinothricin, and other glutamate analogs. Phytochemistry 21:855-857.
    • (1982) Phytochemistry , vol.21 , pp. 855-857
    • Leason, M.1    Cunliffe, D.2    Parkin, D.3    Lea, P.J.4    Miflin, B.J.5
  • 14
    • 84996303998 scopus 로고
    • Action mechanism of bialaphos. I. Inhibition of glutamine synthetase and quantitative changes of free amino acids in shoots of bialaphos-treated Japanese barnyard millet
    • Tachibana K, Watanabe T, Sekizawa Y, Takematsu T (1986) Action mechanism of bialaphos. I. Inhibition of glutamine synthetase and quantitative changes of free amino acids in shoots of bialaphos-treated Japanese barnyard millet. Nippon Noyaku Gakkaishi; J Pestic Sci 11:27-31.
    • (1986) Nippon Noyaku Gakkaishi; J Pestic Sci , vol.11 , pp. 27-31
    • Tachibana, K.1    Watanabe, T.2    Sekizawa, Y.3    Takematsu, T.4
  • 15
    • 36849070538 scopus 로고    scopus 로고
    • Reassignment of the structure of the antibiotic A53868 reveals an unusual amino dehydrophosphonic acid
    • Whitteck JT, et al. (2007) Reassignment of the structure of the antibiotic A53868 reveals an unusual amino dehydrophosphonic acid. Angew Chem Int Ed 46:9089-9092.
    • (2007) Angew Chem Int Ed , vol.46 , pp. 9089-9092
    • Whitteck, J.T.1
  • 16
    • 0018682364 scopus 로고
    • Phosphonopeptides as antibacterial agents: Metabolism and pharmacokinetics of alafosfalin in animals and humans
    • Allen JG, Havas L, Leicht E, Lenox-Smith I, Nisbet LJ (1979) Phosphonopeptides as antibacterial agents: Metabolism and pharmacokinetics of alafosfalin in animals and humans. Antimicrob Agents Chemother 16:306-313. (Pubitemid 10224022)
    • (1979) Antimicrobial Agents and Chemotherapy , vol.16 , Issue.3 , pp. 306-313
    • Allen, J.G.1    Havas, L.2    Leicht, E.3
  • 17
    • 0020616474 scopus 로고
    • Phosphonopeptides as substrates for peptide transport systems and peptidases of Escherichia coli
    • Atherton FR, et al. (1983) Phosphonopeptides as substrates for peptide transport systems and peptidases of Escherichia coli. Antimicrob Agents Chemother 24:522-528.
    • (1983) Antimicrob Agents Chemother , vol.24 , pp. 522-528
    • Atherton, F.R.1
  • 19
    • 77950960667 scopus 로고    scopus 로고
    • Molecular cloning and heterologous expression of the dehydrophos biosynthetic gene cluster
    • Circello BT, Eliot AC, Lee J-L, van der Donk WA, Metcalf WW (2010) Molecular cloning and heterologous expression of the dehydrophos biosynthetic gene cluster. Chem Biol 17:402-411.
    • (2010) Chem Biol , vol.17 , pp. 402-411
    • Circello, B.T.1    Eliot, A.C.2    Lee, J.-L.3    Van Der Donk, W.A.4    Metcalf, W.W.5
  • 20
    • 0842303035 scopus 로고    scopus 로고
    • An enzyme-coupled colorimetric assay for S-adenosylmethionine-dependent methyltransferases
    • Hendricks CL, Ross JR, Pichersky E, Noel JP, Zhou ZS (2004) An enzyme-coupled colorimetric assay for S-adenosylmethionine-dependent methyltransferases. Anal Biochem 326:100-105.
    • (2004) Anal Biochem , vol.326 , pp. 100-105
    • Hendricks, C.L.1    Ross, J.R.2    Pichersky, E.3    Noel, J.P.4    Zhou, Z.S.5
  • 21
    • 19544377011 scopus 로고    scopus 로고
    • A nucleosidase required for in vivo function of the S-adenosyl-L- methionine radical enzyme, biotin synthase
    • Choi-Rhee E, Cronan JE (2005) A nucleosidase required for in vivo function of the S-adenosyl-L-methionine radical enzyme, biotin synthase. Chem Biol 12:589-593.
    • (2005) Chem Biol , vol.12 , pp. 589-593
    • Choi-Rhee, E.1    Cronan, J.E.2
  • 22
    • 0023944122 scopus 로고
    • Tritylamine (Triphenylmethylamine) in organic-synthesis. 1. The synthesis of N-(Triphenylmethyl)alkanimines, 1-(Triphenylmethylamino)alkylphosphonic esters, and 1-Aminoalkylphosphonic acids and esters
    • Soroka M, Zygmunt J (1988) Tritylamine (Triphenylmethylamine) in organic-synthesis. 1. The synthesis of N-(Triphenylmethyl)alkanimines, 1-(Triphenylmethylamino)alkylphosphonic esters, and 1-Aminoalkylphosphonic acids and esters. Synthesis 370-375.
    • (1988) Synthesis , pp. 370-375
    • Soroka, M.1    Zygmunt, J.2
  • 23
    • 0024375849 scopus 로고
    • Phosphonate analogues of carboxypeptidase A substrates are potent transition-state analogue inhibitors
    • Hanson JE, Kaplan AP, Bartlett PA (1989) Phosphonate analogues of carboxypeptidase A substrates are potent transition-state analogue inhibitors. Biochemistry 28:6294-6305.
    • (1989) Biochemistry , vol.28 , pp. 6294-6305
    • Hanson, J.E.1    Kaplan, A.P.2    Bartlett, P.A.3
  • 24
    • 0242460576 scopus 로고    scopus 로고
    • Generation, representation and flow of phase information in structure determination: Recent developments in and around SHARP 2.0
    • Bricogne G, Vonrhein C, Flensburg C, Schiltz M, Paciorek W (2003) Generation, representation and flow of phase information in structure determination: recent developments in and around SHARP 2.0. Acta Crystallogr D 59:2023-2030.
    • (2003) Acta Crystallogr D , vol.59 , pp. 2023-2030
    • Bricogne, G.1    Vonrhein, C.2    Flensburg, C.3    Schiltz, M.4    Paciorek, W.5
  • 25
    • 33846426122 scopus 로고    scopus 로고
    • Solving structures of protein complexes by molecular replacement with Phaser
    • McCoy AJ (2007) Solving structures of protein complexes by molecular replacement with Phaser. Acta Crystallogr D 63:32-41.
    • (2007) Acta Crystallogr D , vol.63 , pp. 32-41
    • McCoy, A.J.1
  • 26
    • 0036917889 scopus 로고    scopus 로고
    • SAM (dependent) I AM: The S-adenosylmethionine-dependent methyltransferase fold
    • Martin JL, McMillan FM (2002) SAM (dependent) I AM: The S-adenosylmethionine-dependent methyltransferase fold. Curr Opin Struct Biol 12:783-793.
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 783-793
    • Martin, J.L.1    McMillan, F.M.2
  • 27
    • 53049087315 scopus 로고    scopus 로고
    • Structure and mechanism of the rebeccamycin sugar 4′-O- methyltransferase RebM
    • Singh S, et al. (2008) Structure and mechanism of the rebeccamycin sugar 4′-O-methyltransferase RebM. J Biol Chem 283:22628-22636.
    • (2008) J Biol Chem , vol.283 , pp. 22628-22636
    • Singh, S.1
  • 28
    • 0028871926 scopus 로고
    • Dali: A network tool for protein structure comparison
    • Holm L, Sander C (1995) Dali: A network tool for protein structure comparison. Trends Biochem Sci 20:478-480.
    • (1995) Trends Biochem Sci , vol.20 , pp. 478-480
    • Holm, L.1    Sander, C.2
  • 29
    • 0021746042 scopus 로고
    • Identification of methylphosphomannosyl residues as components of the high mannose oligosaccharides of Dictyostelium discoideum glycoproteins
    • Gabel CA, Costello CE, Reinhold VN, Kurz L, Kornfeld S (1984) Identification of methylphosphomannosyl residues as components of the high mannose oligosaccharides of Dictyostelium discoideum glycoproteins. J Biol Chem 259:13762-13769.
    • (1984) J Biol Chem , vol.259 , pp. 13762-13769
    • Gabel, C.A.1    Costello, C.E.2    Reinhold, V.N.3    Kurz, L.4    Kornfeld, S.5
  • 30
    • 0027161989 scopus 로고
    • On the revised structure of the major phospholipid of Halobacterium salinarium
    • Kates M, Moldoveanu N, Stewart LC (1993) On the revised structure of the major phospholipid of Halobacterium salinarium. Biochim Biophys Acta 1169:46-53.
    • (1993) Biochim Biophys Acta , vol.1169 , pp. 46-53
    • Kates, M.1    Moldoveanu, N.2    Stewart, L.C.3
  • 32
    • 2942595715 scopus 로고    scopus 로고
    • A methylated phosphate group and four amide-linked acyl chains in leptospira interrogans lipid A. The membrane anchor of an unusual lipopolysaccharide that activates TLR2
    • Que-Gewirth NL, et al. (2004) A methylated phosphate group and four amide-linked acyl chains in leptospira interrogans lipid A. The membrane anchor of an unusual lipopolysaccharide that activates TLR2. J Biol Chem 279:25420-25429.
    • (2004) J Biol Chem , vol.279 , pp. 25420-25429
    • Que-Gewirth, N.L.1
  • 33
    • 0026744108 scopus 로고
    • A novel pathway for phosphorylated oligosaccharide biosynthesis. Identification of an oligosaccharide-specific phosphate methyltransferase in dictyostelium discoideum
    • Freeze HH, Hindsgaul O, Ichikawa M (1992) A novel pathway for phosphorylated oligosaccharide biosynthesis. Identification of an oligosaccharide-specific phosphate methyltransferase in dictyostelium discoideum. J Biol Chem 267:4431-4439.
    • (1992) J Biol Chem , vol.267 , pp. 4431-4439
    • Freeze, H.H.1    Hindsgaul, O.2    Ichikawa, M.3
  • 34
    • 0028359622 scopus 로고
    • Purification of human U6 small nuclear RNA capping enzyme: Evidence for a common capping enzyme for gamma-monomethyl-capped small RNAs
    • Shimba S, Reddy R (1994) Purification of human U6 small nuclear RNA capping enzyme. Evidence for a common capping enzyme for gamma-monomethyl-capped small RNAs. J Biol Chem 269:12419-12423. (Pubitemid 24982268)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.17 , pp. 12419-12423
    • Shimba, S.1    Reddy, R.2
  • 35
    • 24044511808 scopus 로고    scopus 로고
    • A Leptospira interrogans enzyme with similarity to yeast Ste14p that methylates the 1-phosphate group of lipid A
    • Boon Hinckley M, et al. (2005) A Leptospira interrogans enzyme with similarity to yeast Ste14p that methylates the 1-phosphate group of lipid A. J Biol Chem 280:30214-30224.
    • (2005) J Biol Chem , vol.280 , pp. 30214-30224
    • Boon Hinckley, M.1
  • 36
    • 0018845646 scopus 로고
    • Phosphonate analogues of pyruvate. Probes of substrate binding to pyruvate oxidase and other thiamin pyrophosphate-dependent decarboxylases
    • O'Brien TA, Kluger R, Pike DC, Gennis RB (1980) Phosphonate analogues of pyruvate. Probes of substrate binding to pyruvate oxidase and other thiamin pyrophosphate-dependent decarboxylases. Biochim Biophys Acta 613:10-17.
    • (1980) Biochim Biophys Acta , vol.613 , pp. 10-17
    • O'Brien, T.A.1    Kluger, R.2    Pike, D.C.3    Gennis, R.B.4
  • 37
    • 0017781164 scopus 로고
    • Active site generated analogues of reactive intermediates in enzymic reactions. Potent inhibition of pyruvate dehydrogenase by a phosphonate analogue of pyruvate
    • Kluger R, Pike DC (1977) Active site generated analogues of reactive intermediates in enzymic reactions. Potent inhibition of pyruvate dehydrogenase by a phosphonate analogue of pyruvate. J Am Chem Soc 99:4504-4506.
    • (1977) J Am Chem Soc , vol.99 , pp. 4504-4506
    • Kluger, R.1    Pike, D.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.