메뉴 건너뛰기




Volumn 6, Issue 8, 2010, Pages 581-586

An ATP-independent strategy for amide bond formation in antibiotic biosynthesis

Author keywords

[No Author keywords available]

Indexed keywords

A 503083B; BETA LACTAMASE; CAPROLACTAM DERIVATIVE; CAPURAMYCIN; CARBOXYLTRANSFERASE; UNCLASSIFIED DRUG; A 503083 A; ADENOSINE TRIPHOSPHATE; AMIDE; ANTIINFECTIVE AGENT; AZEPINE DERIVATIVE; BACTERIAL DNA; CARBOXYLIC ACID; DRUG DERIVATIVE; ESTER; LYSINE; PROTEIN METHYLTRANSFERASE; URIDINE;

EID: 77955919815     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio.393     Document Type: Article
Times cited : (58)

References (38)
  • 1
    • 8144221722 scopus 로고    scopus 로고
    • A-503083 A, B, e and F, novel inhibitors of bacterial translocase I, produced by Streptomyces sp. SANK 62799
    • Muramatsu, Y. et al. A-503083 A, B, E and F, novel inhibitors of bacterial translocase I, produced by Streptomyces sp. SANK 62799. J. Antibiot. (Tokyo) 57, 639-646 (2004).
    • (2004) J. Antibiot. (Tokyo) , vol.57 , pp. 639-646
    • Muramatsu, Y.1
  • 2
    • 0344404062 scopus 로고    scopus 로고
    • Studies on novel bacterial translocase i inhibitors, A-500359s. I. Taxonomy, fermentation, isolation, physic-chemical properties and structure elucidation of A-500359 A, C, D, and G
    • Muramatsu, Y. et al. Studies on novel bacterial translocase I inhibitors, A-500359s. I. Taxonomy, fermentation, isolation, physic-chemical properties and structure elucidation of A-500359 A, C, D, and G. J. Antibiot. (Tokyo) 56, 243-252 (2003).
    • (2003) J. Antibiot. (Tokyo) , vol.56 , pp. 243-252
    • Muramatsu, Y.1
  • 3
    • 33745090237 scopus 로고    scopus 로고
    • Phospho-MurNAc-pentapeptide translocase (MraY) as a target for antibacterial agents and antibacterial proteins
    • Bugg, T.D.H., Lloyd, A.J. & Roper, D.I. Phospho-MurNAc-pentapeptide translocase (MraY) as a target for antibacterial agents and antibacterial proteins. Infect. Disord. Drug Targets 6, 85-106 (2006).
    • (2006) Infect. Disord. Drug Targets , vol.6 , pp. 85-106
    • Bugg, T.D.H.1    Lloyd, A.J.2    Roper, D.I.3
  • 4
    • 85153643203 scopus 로고    scopus 로고
    • Bacterial cell wall morphology and biochemistry
    • 2nd edn (eds. Goldman, E. & Green, L.H.) (CRC Press, Boca Raton, Florida, USA
    • Suvorov, M., Fisher, J.F. & Mobashery, S. Bacterial cell wall morphology and biochemistry. in Practical Handbook of Microbiology 2nd edn (eds. Goldman, E. & Green, L.H.) 159-190 (CRC Press, Boca Raton, Florida, USA, 2008).
    • (2008) Practical Handbook of Microbiology , pp. 159-190
    • Suvorov, M.1    Fisher, J.F.2    Mobashery, S.3
  • 5
    • 37349041697 scopus 로고    scopus 로고
    • Lipid intermediates in the biosynthesis of bacterial peptidoglycan
    • van Heijenoort, J. Lipid intermediates in the biosynthesis of bacterial peptidoglycan. Microbiol. Mol. Biol. Rev. 71, 620-635 (2007).
    • (2007) Microbiol. Mol. Biol. Rev. , vol.71 , pp. 620-635
    • Van Heijenoort, J.1
  • 6
    • 0023938632 scopus 로고
    • The structure of a new nucleoside antibiotic, capuramycin
    • Seto, H. et al. The structure of a new nucleoside antibiotic, capuramycin. Tetrahedr. Lett. 29, 2343-2346 (1988).
    • (1988) Tetrahedr. Lett. , vol.29 , pp. 2343-2346
    • Seto, H.1
  • 7
    • 68149156215 scopus 로고    scopus 로고
    • Identification of the biosynthetic gene cluster of A-500359s in Streptomyces griseus SANK60196
    • Funabashi, M. et al. Identification of the biosynthetic gene cluster of A-500359s in Streptomyces griseus SANK60196. J. Antibiot. (Tokyo) 62, 325-332 (2009).
    • (2009) J. Antibiot. (Tokyo) , vol.62 , pp. 325-332
    • Funabashi, M.1
  • 8
    • 59649084249 scopus 로고    scopus 로고
    • How nature morphs peptide scaffolds into antibiotics
    • Nolan, E.M. & Walsh, C.T. How nature morphs peptide scaffolds into antibiotics. ChemBioChem 10, 34-53 (2009).
    • (2009) ChemBioChem , vol.10 , pp. 34-53
    • Nolan, E.M.1    Walsh, C.T.2
  • 9
    • 14844362964 scopus 로고    scopus 로고
    • Bacterial resistance to β-lactam antibiotics: Compelling opportunism, compelling opportunity
    • Fisher, J.F., Meroueh, S.O. & Mobashery, S. Bacterial resistance to β-lactam antibiotics: compelling opportunism, compelling opportunity. Chem. Rev. 105, 395-424 (2005).
    • (2005) Chem. Rev. , vol.105 , pp. 395-424
    • Fisher, J.F.1    Meroueh, S.O.2    Mobashery, S.3
  • 10
    • 0027428548 scopus 로고
    • Evolution of an enzyme activity: Crystallographic structure of 2-Å resolution of cephalosporinase from the ampC gene of Enterobacter cloacae P99 and comparison with a class A penicillinase
    • Lobkovsky, E. et al. Evolution of an enzyme activity: crystallographic structure of 2-Å resolution of cephalosporinase from the ampC gene of Enterobacter cloacae P99 and comparison with a class A penicillinase. Proc. Natl. Acad. Sci. USA 90, 11257-11261 (1993).
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 11257-11261
    • Lobkovsky, E.1
  • 11
    • 0015999336 scopus 로고
    • Kinetics of aminoacyl-tRNA synthetases catalyzed ATP-PPi exchange
    • Santi, D.V., Webster, R.W. Jr. & Cleland, W.W. Kinetics of aminoacyl-tRNA synthetases catalyzed ATP-PPi exchange. Methods Enzymol. 29, 620-627 (1974).
    • (1974) Methods Enzymol , vol.29 , pp. 620-627
    • Santi, D.V.1    Webster Jr., R.W.2    Cleland, W.W.3
  • 12
    • 0345698604 scopus 로고    scopus 로고
    • Studies on novel bacterial translocase I inhibitors, A-500359s. IV. Biosynthesis of A-500359s
    • Ohnuki, T., Muramatsu, Y., Miyakoshi, S., Takatsu, T. & Inukai, M. Studies on novel bacterial translocase I inhibitors, A-500359s. IV. Biosynthesis of A-500359s. J. Antibiot. (Tokyo) 56, 268-279 (2003). (Pubitemid 36443395)
    • (2003) Journal of Antibiotics , vol.56 , Issue.3 , pp. 268-279
    • Ohnuki, T.1    Muramatsu, Y.2    Miyakoshi, S.3    Takatsu, T.4    Inukai, M.5
  • 13
    • 0032859029 scopus 로고    scopus 로고
    • Enzymes as biocatalysts in the modification of natural lipids
    • Gunstone, F.D. Enzymes as biocatalysts in the modification of natural lipids. J. Sci. Food Agric. 79, 1535-1549 (1999).
    • (1999) J. Sci. Food Agric. , vol.79 , pp. 1535-1549
    • Gunstone, F.D.1
  • 14
    • 47749153740 scopus 로고    scopus 로고
    • Substrate specificity of bacterial DD-peptidases (penicillin-binding proteins)
    • Pratt, R.F. Substrate specificity of bacterial DD-peptidases (penicillin-binding proteins). Cell. Mol. Life Sci. 65, 2138-2155 (2008).
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 2138-2155
    • Pratt, R.F.1
  • 15
    • 0035666321 scopus 로고    scopus 로고
    • The structure of the feruloyl esterase module of xylanase 10B from the Clostridium thermocellum provides insights into substrate recognition
    • Prates, J.A.M. et al. The structure of the feruloyl esterase module of xylanase 10B from the Clostridium thermocellum provides insights into substrate recognition. Structure 9, 1183-1190 (2001).
    • (2001) Structure , vol.9 , pp. 1183-1190
    • Prates, J.A.M.1
  • 16
    • 0014201592 scopus 로고
    • Three-dimensional structure of tosyl-α-chymotrypsin
    • Matthews, B.W., Sigler, P.B., Henderson, R. & Blow, D.M. Three-dimensional structure of tosyl-α-chymotrypsin. Nature 214, 652-656 (1967).
    • (1967) Nature , vol.214 , pp. 652-656
    • Matthews, B.W.1    Sigler, P.B.2    Henderson, R.3    Blow, D.M.4
  • 17
    • 0027428548 scopus 로고
    • Evolution of an enzyme activity: Crystallographic structure of 2-Å resolution of cephalosporinase from the ampC gene of Enterobacter cloacae P99 and comparison with a class A penicillinase
    • Lobkovsky, E. et al. Evolution of an enzyme activity: crystallographic structure of 2-Å resolution of cephalosporinase from the ampC gene of Enterobacter cloacae P99 and comparison with a class A penicillinase. Proc. Natl. Acad. Sci. USA 90, 11257-11261 (1993).
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 11257-11261
    • Lobkovsky, E.1
  • 18
    • 67649544588 scopus 로고    scopus 로고
    • Physically discrete β-lactamase-type thioesterase catalyzes product release in atrochrysone synthesis by iterative type i polyketide synthase
    • Awakawa, T. et al. Physically discrete β-lactamase-type thioesterase catalyzes product release in atrochrysone synthesis by iterative type I polyketide synthase. Chem. Biol. 16, 613-623 (2009).
    • (2009) Chem. Biol. , vol.16 , pp. 613-623
    • Awakawa, T.1
  • 19
    • 35348851337 scopus 로고    scopus 로고
    • Macrolactin is the polyketide biosynthesis product of the pks2 cluster of Bacillus amyloliquefaciens FZB42
    • Schneider, K. et al. Macrolactin is the polyketide biosynthesis product of the pks2 cluster of Bacillus amyloliquefaciens FZB42. J. Nat. Prod. 70, 1417-1423 (2007).
    • (2007) J. Nat. Prod. , vol.70 , pp. 1417-1423
    • Schneider, K.1
  • 20
    • 0347361709 scopus 로고    scopus 로고
    • Five additional genes are involved in clavulanic acid biosynthesis in Streptomyces clavuligerus
    • Jensen, S.E. et al. Five additional genes are involved in clavulanic acid biosynthesis in Streptomyces clavuligerus. Antimicrob. Agents Chemother. 48, 192-202 (2004).
    • (2004) Antimicrob. Agents Chemother. , vol.48 , pp. 192-202
    • Jensen, S.E.1
  • 21
    • 33748631825 scopus 로고    scopus 로고
    • Assembly-line enzymology for polyketide and nonribosomal peptide antiobiotics: Logic, machinery, and mechanisms
    • Fischbach, M.A. & Walsh, C.T. Assembly-line enzymology for polyketide and nonribosomal peptide antiobiotics: logic, machinery, and mechanisms. Chem. Rev. 106, 3468-3496 (2006).
    • (2006) Chem. Rev. , vol.106 , pp. 3468-3496
    • Fischbach, M.A.1    Walsh, C.T.2
  • 23
    • 0025061844 scopus 로고
    • Molecular characterization of the acyl-coenzyme A:Isopenicillin N acyltransferase gene (penDE) from Penicillium chrysogenum and Aspergillus nidulans and activity of recombinant enzyme in Escherichia coli
    • Tobin, M.B., Fleming, M.D., Skatrud, P.L. & Miller, J.R. Molecular characterization of the acyl-coenzyme A:isopenicillin N acyltransferase gene (penDE) from Penicillium chrysogenum and Aspergillus nidulans and activity of recombinant enzyme in Escherichia coli. J. Bacteriol. 172, 5908-5914 (1990).
    • (1990) J. Bacteriol. , vol.172 , pp. 5908-5914
    • Tobin, M.B.1    Fleming, M.D.2    Skatrud, P.L.3    Miller, J.R.4
  • 24
    • 0344442901 scopus 로고    scopus 로고
    • An unusual amide synthetase (CouL) from the coumermycin A1 biosynthetic gene cluster from Streptomyces rishiriensis DSM 40489
    • Schmutz, E. et al. An unusual amide synthetase (CouL) from the coumermycin A1 biosynthetic gene cluster from Streptomyces rishiriensis DSM 40489. Eur. J. Biochem. 270, 4413-4419 (2003).
    • (2003) Eur. J. Biochem. , vol.270 , pp. 4413-4419
    • Schmutz, E.1
  • 25
    • 34548688717 scopus 로고    scopus 로고
    • A new family of ATP-dependent oligomerization-macrocyclization biocatalysts
    • Kadi, N., Over-Costales, D., Barona-Gomez, F. & Challis, G.L. A new family of ATP-dependent oligomerization-macrocyclization biocatalysts. Nat. Chem. Biol. 3, 652-656 (2007).
    • (2007) Nat. Chem. Biol. , vol.3 , pp. 652-656
    • Kadi, N.1    Over-Costales, D.2    Barona-Gomez, F.3    Challis, G.L.4
  • 26
    • 60249096190 scopus 로고    scopus 로고
    • AcsD catalyzes enantioselective citrate desymmetrization in siderophore biosynthesis
    • Schmelz, S. et al. AcsD catalyzes enantioselective citrate desymmetrization in siderophore biosynthesis. Nat. Chem. Biol. 5, 174-182 (2009).
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 174-182
    • Schmelz, S.1
  • 27
    • 70350475683 scopus 로고    scopus 로고
    • The ATP-dependent amide ligases DdaG and DdaF assemble the fumaramoyl-dipeptide scaffold of the dapdiamide antibiotics
    • Hollenhorst, M.A., Clardy, J. & Walsh, C.T. The ATP-dependent amide ligases DdaG and DdaF assemble the fumaramoyl-dipeptide scaffold of the dapdiamide antibiotics. Biochemistry 48, 10467-10472 (2009).
    • (2009) Biochemistry , vol.48 , pp. 10467-10472
    • Hollenhorst, M.A.1    Clardy, J.2    Walsh, C.T.3
  • 28
    • 33644870792 scopus 로고    scopus 로고
    • ORF17 from the clavulanic acid biosynthesis gene cluster catalyzes the ATP-dependent formation of N-glycyl-clavaminic acid
    • Arulanantham, H. et al. ORF17 from the clavulanic acid biosynthesis gene cluster catalyzes the ATP-dependent formation of N-glycyl-clavaminic acid. J. Biol. Chem. 281, 279-287 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 279-287
    • Arulanantham, H.1
  • 29
    • 65949084690 scopus 로고    scopus 로고
    • Cyclodipeptide synthases are a family of tRNA-dependent peptide bond-forming enzymes
    • Gondry, M. et al. Cyclodipeptide synthases are a family of tRNA-dependent peptide bond-forming enzymes. Nat. Chem. Biol. 5, 414-420 (2009).
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 414-420
    • Gondry, M.1
  • 30
    • 0035834493 scopus 로고    scopus 로고
    • Crystal structure of a protein repair methyltransferase from Pyrococcus furiosus with its L-isoaspartyl peptide substrate
    • Griffith, S.C. et al. Crystal structure of a protein repair methyltransferase from Pyrococcus furiosus with its L-isoaspartyl peptide substrate. J. Mol. Biol. 313, 1103-1116 (2001).
    • (2001) J. Mol. Biol. , vol.313 , pp. 1103-1116
    • Griffith, S.C.1
  • 31
    • 0141683556 scopus 로고    scopus 로고
    • The blasticidin S biosynthesis gene cluster from Streptomyces griseochromogenes: Sequence analysis, organization, and initial characterization
    • Cone, M.C., Yin, X., Grochowski, L.L., Parker, M.R. & Zabriskie, T.M. The blasticidin S biosynthesis gene cluster from Streptomyces griseochromogenes: sequence analysis, organization, and initial characterization. ChemBioChem 4, 821-828 (2003).
    • (2003) ChemBioChem , vol.4 , pp. 821-828
    • Cone, M.C.1    Yin, X.2    Grochowski, L.L.3    Parker, M.R.4    Zabriskie, T.M.5
  • 32
    • 33746218295 scopus 로고    scopus 로고
    • Production of hygromycin A analogs in Streptomyces hygroscopicus NRRL 2388 through identification and manipulation of the biosynthetic gene cluster
    • Palaniappan, N., Ayers, S., Gupta, S., Habib, E.-S. & Reynolds, K.A. Production of hygromycin A analogs in Streptomyces hygroscopicus NRRL 2388 through identification and manipulation of the biosynthetic gene cluster. Chem. Biol. 13, 753-764 (2006).
    • (2006) Chem. Biol. , vol.13 , pp. 753-764
    • Palaniappan, N.1    Ayers, S.2    Gupta, S.3    Habib, E.-S.4    Reynolds, K.A.5
  • 33
    • 0036441179 scopus 로고    scopus 로고
    • Identification of a set of genes involved in the biosynthesis of the aminonucleoside moiety of antibiotic A201A from Streptomyces capreolus
    • Saugar, I., Sanz, E., Rubio, M.A., Espinose, J.C. & Jimenez, A. Identification of a set of genes involved in the biosynthesis of the aminonucleoside moiety of antibiotic A201A from Streptomyces capreolus. Eur. J. Biochem. 269, 5527-5535 (2002).
    • (2002) Eur. J. Biochem. , vol.269 , pp. 5527-5535
    • Saugar, I.1    Sanz, E.2    Rubio, M.A.3    Espinose, J.C.4    Jimenez, A.5
  • 34
    • 0036185101 scopus 로고    scopus 로고
    • A new type of aminoacyltransferase from Saccharothrix sp. AS-2 favorable for the synthesis of d-amino acid-containing peptides
    • Sugihara, A. et al. A new type of aminoacyltransferase from Saccharothrix sp. AS-2 favorable for the synthesis of d-amino acid-containing peptides. J. Biochem. 131, 247-254 (2002).
    • (2002) J. Biochem. , vol.131 , pp. 247-254
    • Sugihara, A.1
  • 35
    • 0037363273 scopus 로고    scopus 로고
    • Studies on novel bacterial translocase i inhibitors, A-500359s III. Deaminocaprolactam derivatives of capuramycin: A-500359 E, F, H, M-1 and M-2
    • Muramatsu, Y. et al. Studies on novel bacterial translocase I inhibitors, A-500359s III. Deaminocaprolactam derivatives of capuramycin: A-500359 E, F, H, M-1 and M-2. J. Antibiot. (Tokyo) 56, 259-267 (2003).
    • (2003) J. Antibiot. (Tokyo) , vol.56 , pp. 259-267
    • Muramatsu, Y.1
  • 36
  • 38
    • 23944436899 scopus 로고    scopus 로고
    • Biosynthesis of the β-amino acid moiety of the enediyne antitumor antibiotic C-1027 featuring β-amino acyl-S-carrier protein intermediates
    • Van Lanen, S.G. et al. Biosynthesis of the β-amino acid moiety of the enediyne antitumor antibiotic C-1027 featuring β-amino acyl-S-carrier protein intermediates. J. Am. Chem. Soc. 127, 11594-11595 (2005).
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 11594-11595
    • Van Lanen, S.G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.