메뉴 건너뛰기




Volumn 50, Issue 33, 2011, Pages 7184-7197

Insights into the reaction mechanism of the prolyl - Acyl carrier protein oxidase involved in anatoxin-a and homoanatoxin-a biosynthesis

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; ACYL CARRIER PROTEINS; ACYL-COA; CATALYTIC CONSTANTS; CATALYTIC ROLE; CONJUGATED IMINE; DEUTERIUM LABELING; ENOLIZATION; EXPERIMENTAL EVIDENCE; GENE CLUSTERS; IN-VITRO; LC-MS/MS; LIQUID CHROMATOGRAPHY COUPLED TO TANDEM MASS SPECTROMETRY; REACTION MECHANISM; SEQUENCE ALIGNMENTS; SLOW OXIDATION; TWO-ELECTRON OXIDATION;

EID: 80051775847     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi200892a     Document Type: Article
Times cited : (25)

References (47)
  • 2
    • 0026808336 scopus 로고
    • Identification of anatoxin-a in benthic cyanobacteria (blue-green algae) and in associated dog poisoning at Loch Insh, Scotland
    • Edwards, C., Beattie, K., Scrimgeour, C., and Codd, G. (1992) Identification of anatoxin-a in benthic cyanobacteria (blue-green algae) and in associated dog poisoning at Loch Insh, Scotland Toxicon 30, 1165-1175
    • (1992) Toxicon , vol.30 , pp. 1165-1175
    • Edwards, C.1    Beattie, K.2    Scrimgeour, C.3    Codd, G.4
  • 3
    • 19344373344 scopus 로고    scopus 로고
    • First report in a river in France of the benthic cyanobacterium Phormidium favosum producing anatoxin-a associated with dog neurotoxicosis
    • DOI 10.1016/j.toxicon.2005.02.031, PII S0041010105000917
    • Gugger, M., Lenoir, S., Berger, C., Ledreux, A., Druart, J. C., Humbert, J. F., Guette, C., and Bernard, C. (2005) First report in a river in France of the benthic cyanobacterium Phormidium favosum producing anatoxin-a associated with dog neurotoxicosis Toxicon 45, 919-928 (Pubitemid 40719794)
    • (2005) Toxicon , vol.45 , Issue.7 , pp. 919-928
    • Gugger, M.1    Lenoir, S.2    Berger, C.3    Ledreux, A.4    Druart, J.-C.5    Humbert, J.-F.6    Guette, C.7    Bernard, C.8
  • 5
    • 34447293235 scopus 로고    scopus 로고
    • First report of homoanatoxin-a and associated dog neurotoxicosis in New Zealand
    • DOI 10.1016/j.toxicon.2007.03.025, PII S0041010107001274
    • Wood, S. A., Selwood, A. I., Rueckert, A., Holland, P. T., Milne, J. R., Smith, K. F., Smits, B., Watts, L. F., and Cary, C. S. (2007) First report of homoanatoxin-a and associated dog neurotoxicosis in New Zealand Toxicon 50, 292-301 (Pubitemid 47042145)
    • (2007) Toxicon , vol.50 , Issue.2 , pp. 292-301
    • Wood, S.A.1    Selwood, A.I.2    Rueckert, A.3    Holland, P.T.4    Milne, J.R.5    Smith, K.F.6    Smits, B.7    Watts, L.F.8    Cary, C.S.9
  • 7
    • 77958456224 scopus 로고    scopus 로고
    • Treatment and diagnosis of a dog with fulminant neurological deterioration due to anatoxin-a intoxication
    • Puschner, B., Pratt, C., and Tor, E. R. (2010) Treatment and diagnosis of a dog with fulminant neurological deterioration due to anatoxin-a intoxication J. Vet. Emerg. Crit. Care (San Antonio) 20, 518-522
    • (2010) J. Vet. Emerg. Crit. Care (San Antonio) , vol.20 , pp. 518-522
    • Puschner, B.1    Pratt, C.2    Tor, E.R.3
  • 8
    • 33646786810 scopus 로고    scopus 로고
    • The chemistry and pharmacology of anatoxin-a and related homotropanes with respect to nicotinic acetylcholine receptors
    • Wonnacott, S. and Gallagher, T. (2006) The chemistry and pharmacology of anatoxin-a and related homotropanes with respect to nicotinic acetylcholine receptors Mar. Drugs. 4, 228-254 (Pubitemid 43763914)
    • (2006) Marine Drugs , vol.4 , Issue.3 , pp. 228-254
    • Wonnacott, S.1    Gallagher, T.2
  • 9
    • 67650519382 scopus 로고    scopus 로고
    • Evidence that biosynthesis of the neurotoxic alkaloids anatoxin-a and homoanatoxin-a in the cyanobacterium Oscillatoria PCC 6506 occurs on a modular polyketide synthase initiated by L-proline
    • Méjean, A., Mann, S., Maldiney, T., Vassiliadis, G., Lequin, O., and Ploux, O. (2009) Evidence that biosynthesis of the neurotoxic alkaloids anatoxin-a and homoanatoxin-a in the cyanobacterium Oscillatoria PCC 6506 occurs on a modular polyketide synthase initiated by L-proline J. Am. Chem. Soc. 131, 7512-7513
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 7512-7513
    • Méjean, A.1    Mann, S.2    Maldiney, T.3    Vassiliadis, G.4    Lequin, O.5    Ploux, O.6
  • 10
    • 67650497679 scopus 로고    scopus 로고
    • Identification of a polyketide synthase coding sequence specific for anatoxin-a-producing Oscillatoria cyanobacteria
    • Cadel-Six, S., Iteman, I., Peyraud-Thomas, C., Mann, S., Ploux, O., and Méjean, A. (2009) Identification of a polyketide synthase coding sequence specific for anatoxin-a-producing Oscillatoria cyanobacteria Appl. Environ. Microbiol. 75, 4909-4912
    • (2009) Appl. Environ. Microbiol. , vol.75 , pp. 4909-4912
    • Cadel-Six, S.1    Iteman, I.2    Peyraud-Thomas, C.3    Mann, S.4    Ploux, O.5    Méjean, A.6
  • 11
    • 78449249368 scopus 로고    scopus 로고
    • Fine-scale spatial variability in anatoxin-a and homoanatoxin-a concentrations in benthic cyanobacterial mats: Implication for monitoring and management
    • Wood, S. A., Heath, M. W., Kuhajek, J., and Ryan, K. G. (2010) Fine-scale spatial variability in anatoxin-a and homoanatoxin-a concentrations in benthic cyanobacterial mats: implication for monitoring and management J. Appl. Microbiol. 109, 2011-2018
    • (2010) J. Appl. Microbiol. , vol.109 , pp. 2011-2018
    • Wood, S.A.1    Heath, M.W.2    Kuhajek, J.3    Ryan, K.G.4
  • 12
    • 77956058948 scopus 로고    scopus 로고
    • First report of anatoxin-a-producing cyanobacterium Aphanizomenon issatschenkoi in northeastern Germany
    • Ballot, A., Fastner, J., Lentz, M., and Wiedner, C. (2010) First report of anatoxin-a-producing cyanobacterium Aphanizomenon issatschenkoi in northeastern Germany Toxicon 56, 964-971
    • (2010) Toxicon , vol.56 , pp. 964-971
    • Ballot, A.1    Fastner, J.2    Lentz, M.3    Wiedner, C.4
  • 13
    • 73449134513 scopus 로고    scopus 로고
    • In vitro reconstitution of the first steps of anatoxin-a biosynthesis in Oscillatoria PCC 6506: From free L-proline to acyl carrier protein bound dehydroproline
    • Méjean, A., Mann, S., Vassiliadis, G., Lombard, B., Loew, D., and Ploux, O. (2010) In vitro reconstitution of the first steps of anatoxin-a biosynthesis in Oscillatoria PCC 6506: from free L-proline to acyl carrier protein bound dehydroproline Biochemistry 49, 103-113
    • (2010) Biochemistry , vol.49 , pp. 103-113
    • Méjean, A.1    Mann, S.2    Vassiliadis, G.3    Lombard, B.4    Loew, D.5    Ploux, O.6
  • 14
    • 0032936731 scopus 로고    scopus 로고
    • Characterization of the pyoluteorin biosynthetic gene cluster of Pseudomonas fluorescens Pf-5
    • Nowak-Thompson, B., Chaney, N., Wing, J. S., Gould, S. J., and Loper, J. E. (1999) Characterization of the pyoluteorin biosynthetic gene cluster of Pseudomonas fluorescens Pf-5 J. Bacteriol. 181, 2166-2174 (Pubitemid 29164971)
    • (1999) Journal of Bacteriology , vol.181 , Issue.7 , pp. 2166-2174
    • Nowak-Thompson, B.1    Chaney, N.2    Wing, J.S.3    Gould, S.J.4    Loper, J.E.5
  • 15
    • 0033743319 scopus 로고    scopus 로고
    • Identification of the coumermycin A(1) biosynthetic gene cluster of Streptomyces rishiriensis DSM 40489
    • Wang, Z. X., Li, S. M., and Heide, L. (2000) Identification of the coumermycin A(1) biosynthetic gene cluster of Streptomyces rishiriensis DSM 40489 Antimicrob. Agents Chemother. 44, 3040-3048
    • (2000) Antimicrob. Agents Chemother. , vol.44 , pp. 3040-3048
    • Wang, Z.X.1    Li, S.M.2    Heide, L.3
  • 16
    • 0034872156 scopus 로고    scopus 로고
    • Analysis of the prodiginine biosynthesis gene cluster of Streptomyces coelicolor A3(2): New mechanisms for chain initiation and termination in modular multienzymes
    • DOI 10.1016/S1074-5521(01)00054-0, PII S1074552101000540
    • Cerdeño, A. M., Bibb, M. J., and Challis, G. L. (2001) Analysis of the prodiginine biosynthesis gene cluster of Streptomyces coelicolor A3(2): new mechanisms for chain initiation and termination in modular multienzymes Chem. Biol. 8, 817-829 (Pubitemid 32752460)
    • (2001) Chemistry and Biology , vol.8 , Issue.8 , pp. 817-829
    • Cerdeno, A.M.1    Bibb, M.J.2    Challis, G.L.3
  • 17
    • 0036953085 scopus 로고    scopus 로고
    • Molecular cloning and sequence analysis of the clorobiocin biosynthetic gene cluster: New insights into the biosynthesis of aminocoumarin antibiotics
    • Pojer, F., Li, S. M., and Heide, L. (2002) Molecular cloning and sequence analysis of the clorobiocin biosynthetic gene cluster: new insights into the biosynthesis of aminocoumarin antibiotics Microbiology 148, 3901-3911 (Pubitemid 36097452)
    • (2002) Microbiology , vol.148 , Issue.12 , pp. 3901-3911
    • Pojer, F.1    Li, S.-H.2    Heide, L.3
  • 18
    • 9144222164 scopus 로고    scopus 로고
    • The Serratia gene cluster encoding biosynthesis of the red antibiotic, prodigiosin, shows species- and strain-dependent genome context variation
    • DOI 10.1099/mic.0.27222-0
    • Harris, A. K., Williamson, N. R., Slater, H., Cox, A., Abbasi, S., Foulds, I., Simonsen, H. T., Leeper, F. J., and Salmond, G. P. (2004) The Serratia gene cluster encoding biosynthesis of the red antibiotic, prodigiosin, shows species- and strain-dependent genome context variation Microbiology 150, 3547-3560 (Pubitemid 39545305)
    • (2004) Microbiology , vol.150 , Issue.11 , pp. 3547-3560
    • Harris, A.K.P.1    Williamson, N.R.2    Slater, H.3    Cox, A.4    Abbasi, S.5    Foulds, I.6    Simonsen, H.T.7    Leeper, F.J.8    Salmond, G.P.C.9
  • 19
    • 0036008844 scopus 로고    scopus 로고
    • Conversion of L-proline to pyrrolyl-2-carboxyl-S-PCP during undecylprodigiosin and pyoluteorin biosynthesis
    • DOI 10.1016/S1074-5521(02)00100-X, PII S107455210200100X
    • Thomas, M. G., Burkart, M. D., and Walsh, C. T. (2002) Conversion of L-proline to pyrrolyl-2-carboxyl-S-PCP during undecylprodigiosin and pyoluteorin biosynthesis Chem. Biol. 9, 171-84 (Pubitemid 34196655)
    • (2002) Chemistry and Biology , vol.9 , Issue.2 , pp. 171-184
    • Thomas, M.G.1    Burkart, M.D.2    Walsh, C.T.3
  • 20
    • 14344261742 scopus 로고    scopus 로고
    • 1 biosynthesis
    • DOI 10.1021/bi0476329
    • Garneau, S., Dorrestein, P. C., Kelleher, N. L., and Walsh, C. T. (2005) Characterization of the formation of the pyrrole moiety during clorobiocin and coumermycin A1 biosynthesis Biochemistry 44, 2770-2780 (Pubitemid 40293653)
    • (2005) Biochemistry , vol.44 , Issue.8 , pp. 2770-2780
    • Garneau, S.1    Dorrestein, P.C.2    Kelleher, N.L.3    Walsh, C.T.4
  • 21
    • 33749512427 scopus 로고    scopus 로고
    • Protein assembly line components in prodigiosin biosynthesis: Characterization of PigA,G,H,I,J
    • DOI 10.1021/ja063611l
    • Garneau-Tsodikova, S., Dorrestein, P. C., Kelleher, N. L., and Walsh, C. T. (2006) Protein assembly line components in prodigiosin biosynthesis: characterization of PigA,G,H,I,J J. Am. Chem. Soc. 128, 12600-12601 (Pubitemid 44527710)
    • (2006) Journal of the American Chemical Society , vol.128 , Issue.39 , pp. 12600-12601
    • Garneau-Tsodikova, S.1    Dorrestein, P.C.2    Kelleher, N.L.3    Walsh, C.T.4
  • 22
    • 33746608987 scopus 로고    scopus 로고
    • Biological formation of pyrroles: Nature's logic and enzymatic machinery
    • DOI 10.1039/b605245m
    • Walsh, C. T., Garneau-Tsodikova, S., and Howard-Jones, A. R. (2006) Biological formation of pyrroles: nature's logic and enzymatic machinery Nat. Prod. Rep. 23, 517-531 (Pubitemid 44144208)
    • (2006) Natural Product Reports , vol.23 , Issue.4 , pp. 517-531
    • Walsh, C.T.1    Garneau-Tsodikova, S.2    Howard-Jones, A.R.3
  • 23
    • 33847681412 scopus 로고    scopus 로고
    • Cloning and characterization of the pyrrolomycin biosynthetic gene clusters from Actinosporangium vitaminophilum ATCC 31673 and Streptomyces sp. strain UC 11065
    • DOI 10.1128/AAC.01214-06
    • Zhang, X. and Parry, R. J. (2007) Cloning and characterization of the pyrrolomycin biosynthetic gene clusters from Actinosporangium vitaminophilum ATCC 31673 and Streptomyces sp. strain UC 11065 Antimicrob. Agents Chemother. 51, 946-957 (Pubitemid 46355279)
    • (2007) Antimicrobial Agents and Chemotherapy , vol.51 , Issue.3 , pp. 946-957
    • Zhang, X.1    Parry, R.J.2
  • 24
    • 49449110566 scopus 로고    scopus 로고
    • DKxanthene biosynthesis: Understanding the basis for diversity-oriented synthesis in myxobacterial secondary metabolism
    • Meiser, P., Weissman, K. J., Bode, H. B., Krug, D., Dickschat, J. S., Sandmann, A., and Müller, R. (2008) DKxanthene biosynthesis: understanding the basis for diversity-oriented synthesis in myxobacterial secondary metabolism Chem. Biol. 15, 771-781
    • (2008) Chem. Biol. , vol.15 , pp. 771-781
    • Meiser, P.1    Weissman, K.J.2    Bode, H.B.3    Krug, D.4    Dickschat, J.S.5    Sandmann, A.6    Müller, R.7
  • 25
    • 65549102503 scopus 로고    scopus 로고
    • Analysis of the indanomycin biosynthetic gene cluster from Streptomyces antibioticus NRRL 8167
    • Li, C., Roege, K. E., and Kelly, W. L. (2009) Analysis of the indanomycin biosynthetic gene cluster from Streptomyces antibioticus NRRL 8167 ChemBioChem 10, 1064-1072
    • (2009) ChemBioChem , vol.10 , pp. 1064-1072
    • Li, C.1    Roege, K.E.2    Kelly, W.L.3
  • 27
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • DOI 10.1093/nar/25.24.4876
    • Thompson, J. D., Gibson, T. J., Plewniak, F., Jeanmougin, F., and Higgins, D. G. (1997) The ClustalX windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools Nucleic Acids Res. 25, 4876-4882 (Pubitemid 28022245)
    • (1997) Nucleic Acids Research , vol.25 , Issue.24 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 28
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the 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
  • 30
    • 80051734222 scopus 로고
    • Proline: Synthesis from ornithine, citrulline, or arginine
    • Hamilton, P. B. (1952) Proline: synthesis from ornithine, citrulline, or arginine J. Biol. Chem. 198, 587-597
    • (1952) J. Biol. Chem. , vol.198 , pp. 587-597
    • Hamilton, P.B.1
  • 34
    • 0030740677 scopus 로고    scopus 로고
    • Structure of human isovaleryl-CoA dehydrogenase at 2.6 a resolution: Structural basis for substrate specificity
    • DOI 10.1021/bi970422u
    • Tiffany, K. A., Roberts, D. L., Wang, M., Paschke, R., Mohsen, A. W., Vockley, J., and Kim, J. J. (1997) Structure of human isovaleryl-CoA dehydrogenase at 2.6 a resolution: structural basis for substrate specificity Biochemistry 36, 8455-8464 (Pubitemid 27305127)
    • (1997) Biochemistry , vol.36 , Issue.28 , pp. 8455-8464
    • Tiffany, K.A.1    Roberts, D.L.2    Wang, M.3    Paschke, R.4    Mohsen, A.-W.A.5    Vockley, J.6    Kim, J.-J.P.7
  • 35
    • 33750360806 scopus 로고    scopus 로고
    • Facile detection of acyl and peptidyl intermediates on thiotemplate carrier domains via phosphopantetheinyl elimination reactions during tandem mass spectrometry
    • DOI 10.1021/bi061169d
    • Dorrestein, P. C., Bumpus, S. B., Calderone, C. T., Garneau-Tsodikova, S., Aron, Z. D., Straight, P. D., Kolter, R., Walsh, C. T., and Kelleher, N. L. (2006) Facile detection of acyl and peptidyl intermediates on thiotemplate carrier domains via phosphopantetheinyl elimination reactions during tandem mass spectrometry Biochemistry 45, 12756-12766 (Pubitemid 44630862)
    • (2006) Biochemistry , vol.45 , Issue.42 , pp. 12756-12766
    • Dorrestein, P.C.1    Bumpus, S.B.2    Calderone, C.T.3    Garneau-Tsodikova, S.4    Aron, Z.D.5    Straight, P.D.6    Kolter, R.7    Walsh, C.T.8    Kelleher, N.L.9
  • 36
    • 33750364236 scopus 로고    scopus 로고
    • Dissecting non-ribosomal and polyketide biosynthetic machineries using electrospray ionization Fourier-Transform mass spectrometry
    • DOI 10.1039/b511400b
    • Dorrestein, P. C. and Kelleher, N. L. (2006) Dissecting non-ribosomal and polyketide biosynthetic machineries using electrospray ionization Fourier-Transform mass spectrometry Nat. Prod. Rep. 23, 893-918 (Pubitemid 44808993)
    • (2006) Natural Product Reports , vol.23 , Issue.6 , pp. 893-918
    • Dorrestein, P.C.1    Kelleher, N.L.2
  • 37
    • 43549120227 scopus 로고    scopus 로고
    • Top-down mass spectrometry on low-resolution instruments: Characterization of phosphopantetheinylated carrier domains in polyketide and non-ribosomal biosynthetic pathways
    • DOI 10.1016/j.bmcl.2007.10.104, PII S0960894X07012863
    • Meluzzi, D., Zheng, W. H., Hensler, M., Nizet, V., and Dorrestein, P. C. (2008) Top-down mass spectrometry on low-resolution instruments: characterization of phosphopantetheinylated carrier domains in polyketide and non-ribosomal biosynthetic pathways Bioorg. Med. Chem. Lett. 18, 3107-3111 (Pubitemid 351680379)
    • (2008) Bioorganic and Medicinal Chemistry Letters , vol.18 , Issue.10 , pp. 3107-3111
    • Meluzzi, D.1    Zheng, W.H.2    Hensler, M.3    Nizet, V.4    Dorrestein, P.C.5
  • 38
    • 0842330598 scopus 로고    scopus 로고
    • Acyl-CoA dehydrogenases. A mechanistic overview
    • Ghisla, S. and Thorpe, C. (2004) Acyl-CoA dehydrogenases. A mechanistic overview Eur. J. Biochem. 271, 494-508
    • (2004) Eur. J. Biochem. , vol.271 , pp. 494-508
    • Ghisla, S.1    Thorpe, C.2
  • 39
    • 0842265784 scopus 로고    scopus 로고
    • Acyl-CoA dehydrogenases and acyl-CoA oxidases: Structural basis for mechanistic similarities and differences
    • DOI 10.1046/j.1432-1033.2003.03948.x
    • Kim, J. J. and Miura, R. (2004) Acyl-CoA dehydrogenases and acyl-CoA oxidases. Structural basis for mechanistic similarities and differences Eur. J. Biochem. 271, 483-493 (Pubitemid 38183623)
    • (2004) European Journal of Biochemistry , vol.271 , Issue.3 , pp. 483-493
    • Kim, J.-J.P.1    Miura, R.2
  • 40
    • 0029969133 scopus 로고    scopus 로고
    • Studies of acyl-CoA dehydrogenase catalyzed allylic isomerization: A one-base or two-base mechanism?
    • DOI 10.1021/ja962532e, PII S0002786396025322
    • Dakoji, S., Shin, I., Becker, D. F., Stankovich, M. T., and Liu, H-w. (1996) Studies of Acyl-CoA Dehydrogenase Catalyzed Allylic Isomerization: A One-Base or Two-Base Mechanism? J. Am. Chem. Soc. 118, 10971-10979 (Pubitemid 26399720)
    • (1996) Journal of the American Chemical Society , vol.118 , Issue.45 , pp. 10971-10979
    • Dakoji, S.1    Shin, I.2    Becker, D.F.3    Stankovich, M.T.4    Liu, H.-W.5
  • 41
    • 0031438569 scopus 로고    scopus 로고
    • Redesigning the active-site of an acyl-CoA dehydrogenase: New evidence supporting a one-base mechanism
    • DOI 10.1016/S0968-0896(97)00159-4, PII S0968089697001594
    • Dakoji, S., Shin, I., Battaile, K. P., Vockley, J., and Liu, H. W. (1997) Redesigning the active-site of an acyl-CoA dehydrogenase: new evidence supporting a one-base mechanism Bioorg. Med. Chem. 5, 2157-2164 (Pubitemid 28012603)
    • (1997) Bioorganic and Medicinal Chemistry , vol.5 , Issue.12 , pp. 2157-2164
    • Dakoji, S.1    Shin, I.2    Battaile, K.P.3    Vockley, J.4    Liu, H.-W.5
  • 42
    • 17844389318 scopus 로고    scopus 로고
    • Intrinsic isomerase activity of medium-chain Acyl-CoA dehydrogenase
    • DOI 10.1021/bi047363m
    • Zeng, J. and Li, D. (2005) Intrinsic isomerase activity of medium-chain acyl-CoA dehydrogenase Biochemistry 44, 6715-6722 (Pubitemid 40593823)
    • (2005) Biochemistry , vol.44 , Issue.17 , pp. 6715-6722
    • Zeng, J.1    Li, D.2
  • 44
    • 21344467263 scopus 로고    scopus 로고
    • An acyl-CoA dehydrogenase is involved in the formation of the Δcis3 double bond in the acyl residue of the lipopeptide antibiotic friulimicin in Actinoplanes friuliensis
    • DOI 10.1099/mic.0.27844-0
    • Heinzelmann, E., Berger, S., Muller, C., Hartner, T., Poralla, K., Wohlleben, W., and Schwartz, D. (2005) An acyl-CoA dehydrogenase is involved in the formation of the Delta cis3 double bond in the acyl residue of the lipopeptide antibiotic friulimicin in Actinoplanes friuliensis Microbiology 151, 1963-1974 (Pubitemid 40909038)
    • (2005) Microbiology , vol.151 , Issue.6 , pp. 1963-1974
    • Heinzelmann, E.1    Berger, S.2    Muller, C.3    Hartner, T.4    Poralla, K.5    Wohlleben, W.6    Schwartz, D.7
  • 45
    • 0015948497 scopus 로고
    • The inibition of proline racemase by a transition state analogueue: α-1-pyrroline-2-carboxylate
    • Keenan, M. V. and Alworth, W. L. (1974) The inibition of proline racemase by a transition state analogueue: α-1-pyrroline-2-carboxylate Biochem. Biophys. Res. Commun. 57, 500-504
    • (1974) Biochem. Biophys. Res. Commun. , vol.57 , pp. 500-504
    • Keenan, M.V.1    Alworth, W.L.2
  • 47
    • 0027286219 scopus 로고
    • 1- pyrroline-2-carboxylic acid as revealed by NMR and electrospray mass spectroscopy
    • DOI 10.1016/S0960-894X(00)80313-3
    • Lewis, M. L., Rowe, C. J., Sewald, N., Sutherland, J. D., Wilson, E. J., and Wright, M. C. (1993) The effect of pH on the solution structure of α-1-pyrroline-2-carboxylic acid as revealed by NMR and electrospray mass spectroscopy Bioorg. Med. Chem. Lett. 3, 1193-1196 (Pubitemid 23185590)
    • (1993) Bioorganic and Medicinal Chemistry Letters , vol.3 , Issue.6 , pp. 1193-1196
    • Lewis, M.L.1    Rowe, C.J.2    Sewald, N.3    Sutherland, J.D.4    Wilson, E.J.5    Wright, M.C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.