Dual binding sites for translocation catalysis by Escherichia coli glutathionylspermidine synthetase
dc.contributor.author | Pai, Chien‐hua | en_US |
dc.contributor.author | Chiang, Bing‐yu | en_US |
dc.contributor.author | Ko, Tzu‐ Ping | en_US |
dc.contributor.author | Chou, Chia‐cheng | en_US |
dc.contributor.author | Chong, Cheong‐meng | en_US |
dc.contributor.author | Yen, Fang‐jiun | en_US |
dc.contributor.author | Chen, Shoujun | en_US |
dc.contributor.author | Coward, James K | en_US |
dc.contributor.author | Wang, Andrew H‐j | en_US |
dc.contributor.author | Lin, Chun‐hung | en_US |
dc.date.accessioned | 2014-01-08T20:34:56Z | |
dc.date.available | 2014-01-08T20:34:56Z | |
dc.date.issued | 2006-12-13 | en_US |
dc.identifier.citation | Pai, Chien‐hua ; Chiang, Bing‐yu ; Ko, Tzu‐ Ping ; Chou, Chia‐cheng ; Chong, Cheong‐meng ; Yen, Fang‐jiun ; Chen, Shoujun; Coward, James K; Wang, Andrew H‐j ; Lin, Chun‐hung (2006). "Dual binding sites for translocation catalysis by Escherichia coli glutathionylspermidine synthetase." The EMBO Journal 25(24): 5970-5982. <http://hdl.handle.net/2027.42/102183> | en_US |
dc.identifier.issn | 0261-4189 | en_US |
dc.identifier.issn | 1460-2075 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/102183 | |
dc.publisher | John Wiley & Sons, Ltd | en_US |
dc.subject.other | Binding Site | en_US |
dc.subject.other | Trypanothione | en_US |
dc.subject.other | Structure | en_US |
dc.subject.other | Mechanism | en_US |
dc.subject.other | Glutathionylspermidine | en_US |
dc.title | Dual binding sites for translocation catalysis by Escherichia coli glutathionylspermidine synthetase | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Molecular, Cellular and Developmental Biology | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.identifier.pmid | 17124497 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/102183/1/emboj7601440.pdf | |
dc.identifier.doi | 10.1038/sj.emboj.7601440 | en_US |
dc.identifier.source | The EMBO Journal | en_US |
dc.identifier.citedreference | Oza SL, Ariyanayagam MR, Aitcheson N, Fairlamb AH ( 2003 ) Properties of trypanothione synthetase from Trypanosoma brucei. Mol Biochem Parasitol 131: 25 – 33 | en_US |
dc.identifier.citedreference | Jones TA, Zou JY, Cowan SW, Kjeldgaard M ( 1991 ) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr A 47: 110 – 119 | en_US |
dc.identifier.citedreference | Kleywegt GJ, Jones TA ( 1998 ) Databases in protein crystallography. Acta Crystallogr D 54: 1119 – 1131 | en_US |
dc.identifier.citedreference | Krauth‐Siegel RL, Meiering SK, Schmidt H ( 2003 ) The parasite‐specific trypanothione metabolism of Trypanosoma and Leishmania. Biol Chem 384: 541 – 549 | en_US |
dc.identifier.citedreference | Kwon DS, Lin CH, Chen S, Coward JK, Walsh CT, Bollinger Jr JM ( 1997 ) Dissection of glutathionylspermidine synthetase/amidase from Escherichia coli into autonomously folding and functional synthetase and amidase domains. J Biol Chem 272: 2429 – 2436 | en_US |
dc.identifier.citedreference | Lin CH, Chen S, Kwon DS, Coward JK, Walsh CT ( 1997a ) Aldehyde and phosphinate analogs of glutathione and glutathionylspermidine: potent, selective binding inhibitors of the E. coli bifunctional glutathionylspermidine synthetase/amidase. Chem Biol 4: 859 – 866 | en_US |
dc.identifier.citedreference | Lin CH, Kwon DS, Bollinger Jr JM, Walsh CT ( 1997b ) Evidence for a glutathionyl‐enzyme intermediate in the amidase activity of the bifunctional glutathionylspermidine synthetase/amidase from Escherichia coli. Biochemistry 36: 14930 – 14938 | en_US |
dc.identifier.citedreference | Marton LJ, Pegg AE ( 1995 ) Polyamines as targets for therapeutic intervention. Annu Rev Pharmacol Toxicol 35: 55 – 91 | en_US |
dc.identifier.citedreference | McRee DE ( 1999 ) XtalView/Xfit—a versatile program for manipulating atomic coordinates and electron density. J Struct Biol 125: 156 – 165 | en_US |
dc.identifier.citedreference | Meister A, Anderson ME ( 1983 ) Glutathione. Annu Rev Biochem 52: 711 – 760 | en_US |
dc.identifier.citedreference | Müller S, Liebau E, Walter RD, Krauth‐Siegel RL ( 2003 ) Thiol‐based redox metabolism of protozoan parasites. Trends Parasiol 19 (7): 320 – 328 | en_US |
dc.identifier.citedreference | Murzin AG ( 1996 ) Structural classification of proteins: new superfamilies. Curr Opin Struct Biol 6: 386 – 394 | en_US |
dc.identifier.citedreference | Otwinowski Z, Minor W ( 1997 ) Processing of X‐ray diffraction data collected in oscillation mode: macromolecular crystallography Part A. Methods Enzymol 276: 307 – 326 | en_US |
dc.identifier.citedreference | Oza SL, Ariyanayagam MR, Fairlamb AH ( 2002a ) Characterization of recombinant glutathionylspermidine synthetase/amidase from Crithidia fasciculata. Biochem J 364: 679 – 686 | en_US |
dc.identifier.citedreference | Oza SL, Shaw MP, Wyllie S, Fairlamb AH ( 2005 ) Trypanothione biosynthesis in Leishmania major. Mol Biochem Parasitol 139: 107 – 116 | en_US |
dc.identifier.citedreference | Oza SL, Tetaud E, Ariyanayagam MR, Warnon SS, Fairlamb AH ( 2002b ) A single enzyme catalyses formation of trypanothione from glutathione and spermidine in Trypanosoma cruzi. J Biol Chem 277: 35853 – 35861 | en_US |
dc.identifier.citedreference | Pegg AE ( 1986 ) Recent advances in the biochemistry of polyamines in eukaryotes. Biochem J 234: 249 – 262 | en_US |
dc.identifier.citedreference | Penketh PG, Kennedy WP, Patton CL, Sartorelli AC ( 1987 ) Trypanosomatid hydrogen peroxide [corrected] metabolism. FEBS Lett 221: 421 – 437 | en_US |
dc.identifier.citedreference | Polekhina G, Board PG, Gali RR, Rossjohn J, Parker MW ( 1999 ) Molecular basis of glutathione synthetase deficiency and a rare gene permutation event. EMBO J 18: 3204 – 3213 | en_US |
dc.identifier.citedreference | Shames SL, Fairlamb AH, Cerami A, Walsh CT ( 1986 ) Purification and characterization of trypanothione reductase from Crithidia fasciculata, a newly discovered member of the family of disulfide‐containing flavoprotein reductases. Biochemistry 25: 3519 – 3526 | en_US |
dc.identifier.citedreference | Smith K, Nadeau K, Bradley M, Walsh C, Fairlamb AH ( 1992 ) Purification of glutathionylspermidine and trypanothione synthetases from Crithidia fasciculata. Protein Sci 1: 874 – 883 | en_US |
dc.identifier.citedreference | Tabor CW, Tabor H ( 1984 ) Polyamines. Annu Rev Biochem 53: 749 – 790 | en_US |
dc.identifier.citedreference | Tabor H, Tabor CW ( 1975 ) Isolation, characterization, and turnover of glutathionylspermidine from Escherichia coli. J Biol Chem 250: 2648 – 2654 | en_US |
dc.identifier.citedreference | Terwilliger TC, Berendzen J ( 1999 ) Automated MAD and MIR structure solution. Acta Crystallogr D 55: 849 – 861 | en_US |
dc.identifier.citedreference | Thoden JB, Blanchard CZ, Holden HM, Waldrop GL ( 2000 ) Movement of the biotin carboxylase B‐domain as a result of ATP binding. J Biol Chem 275: 16183 – 16190 | en_US |
dc.identifier.citedreference | Wang CC ( 1995 ) Molecular mechanisms and therapeutic approaches to the treatment of African trypanosomiasis. Annu Rev Pharmacol Toxicol 35: 93 – 127 | en_US |
dc.identifier.citedreference | Terwilliger TC ( 2000 ) Maximum‐likelihood density modification. Acta Crystallogr D 56: 965 – 972 | en_US |
dc.identifier.citedreference | Barton GJ ( 1993 ) ALSCRIPT: a tool to format multiple sequence alignments. Protein Eng 6: 37 – 40 | en_US |
dc.identifier.citedreference | Bateman A, Rawlings ND ( 2003 ) The CHAP domain: a large family of amidases including GSP amidase and peptidoglycan hydrolases. Trends Biochem Sci 28: 234 – 237 | en_US |
dc.identifier.citedreference | Bollinger Jr JM, Kwon DS, Huisman GW, Kolter R, Walsh CT ( 1995 ) Glutathionylspermidine metabolism in Escherichia coli. Purification, cloning, overproduction, and characterization of a bifunctional glutathionylspermidine synthetase/amidase. J Biol Chem 270: 14031 – 14041 | en_US |
dc.identifier.citedreference | Boveris A, Sies H, Martino EE, Docampo R, Turrens JF, Stoppani AO ( 1980 ) Deficient metabolic utilization of hydrogen peroxide in Trypanosoma cruzi. Biochem J 188: 643 – 648 | en_US |
dc.identifier.citedreference | Brünger AT, Adams PD, Clore GM, DeLano WL, Gros P, Grosse‐Kunstleve RW, Jiang JS, Kuszewski J, Nilges M, Pannu NS ( 1998 ) Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr D 54: 905 – 921 | en_US |
dc.identifier.citedreference | Chen S, Coward JK ( 1998 ) Investigations on new strategies for the facile synthesis of polyfunctionalized phosphinates: phosphinopeptide analogues of glutathionylspermidine. J Org Chem 63: 502 – 509 | en_US |
dc.identifier.citedreference | Chen S, Lin CH, Walsh CT, Coward JK ( 1997 ) Novel inhibitors of trypanothione biosynthesis: synthesis and evaluation of a phosphinate analog of glutathionyl spermidine (GSP), a potent, slow‐binding inhibitor of GSP synthetase. Bioorg Med Chem Lett 7: 505 – 510 | en_US |
dc.identifier.citedreference | Comini M, Menge U, Flohe L ( 2003 ) Biosynthesis of trypanothione in Trypanosoma brucei brucei. Biol Chem 384: 653 – 656 | en_US |
dc.identifier.citedreference | Comini M, Menge U, Wissing J, Flohe L ( 2005 ) Trypanothione synthesis in crithidia revisited. J Biol Chem 280: 6850 – 6860 | en_US |
dc.identifier.citedreference | Dubin T ( 1959 ) Evidence for conjugates between polyamines and glutathione in E. coli. Biochem Biophys Res Commun 1: 262 – 265 | en_US |
dc.identifier.citedreference | Fairlamb AH, Cerami A ( 1985 ) Identification of a novel, thiol‐containing co‐factor essential for glutathione reductase enzyme activity in trypanosomatids. Mol Biochem Parasitol 14: 187 – 198 | en_US |
dc.identifier.citedreference | Fairlamb AH, Cerami A ( 1992 ) Metabolism and functions of trypanothione in the Kinetoplastida. Annu Rev Microbiol 46: 695 – 729 | en_US |
dc.identifier.citedreference | Fan C, Moews PC, Shi Y, Walsh CT, Knox JR ( 1995 ) A common fold for peptide synthetases cleaving ATP to ADP: glutathione synthetase and D‐alanine:D‐alanine ligase of Escherichia coli. Proc Natl Acad Sci USA 92: 1172 – 1176 | en_US |
dc.identifier.citedreference | Fan C, Moews PC, Walsh CT, Knox JR ( 1994 ) Vancomycin resistance: structure of D‐alanine:D‐alanine ligase at 2.3 Å resolution. Science 266: 439 – 443 | en_US |
dc.identifier.citedreference | Guerrero SA, Hecht HJ, Hofmann B, Biebl H, Singh M ( 2001 ) Production of selenomethionine‐labelled proteins using simplified culture conditions and generally applicable host/vector systems. Appl Microbiol Biotechnol 56: 718 – 723 | en_US |
dc.identifier.citedreference | Henderson GB, Yamaguchi M, Novoa L, Fairlamb AH, Cerami A ( 1990 ) Biosynthesis of the trypanosomatid metabolite trypanothione: purification and characterization of trypanothione synthetase from Crithidia fasciculata. Biochemistry 29: 3924 – 3929 | en_US |
dc.identifier.citedreference | Hiratake J ( 2005 ) Enzyme inhibitors as chemical tools to study enzyme catalysis: rational design, synthesis, and applications. Chem Record 5: 209 – 228 | en_US |
dc.identifier.citedreference | Hiratake J, Kato H, Oda J ( 1994 ) Machanism‐based inactivation of glutathione synthetase by phosphinic acid transition‐state analogue. J Am Chem Soc 116: 12059 – 12060 | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
Files in this item
Remediation of Harmful Language
The University of Michigan Library aims to describe library materials in a way that respects the people and communities who create, use, and are represented in our collections. Report harmful or offensive language in catalog records, finding aids, or elsewhere in our collections anonymously through our metadata feedback form. More information at Remediation of Harmful Language.
Accessibility
If you are unable to use this file in its current format, please select the Contact Us link and we can modify it to make it more accessible to you.