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Volumn 43, Issue 32, 2004, Pages 10314-10327

The formylglycinamide ribonucleotide amidotransferase complex from Bacillus subtilis: Metabolite-mediated complex formation

Author keywords

[No Author keywords available]

Indexed keywords

BIOSYNTHESIS; CATALYSIS; ENZYMES; ESCHERICHIA COLI; METABOLITES; SEPARATION;

EID: 4043093379     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi049127h     Document Type: Article
Times cited : (30)

References (36)
  • 1
    • 0033776964 scopus 로고    scopus 로고
    • Modular evolution of the purine biosynthetic pathway
    • Kappock, T. J., Ealick, S. E., and Stubbe, J. (2000) Modular evolution of the purine biosynthetic pathway, Curr. Opin. Chem. Biol. 4, 567-572.
    • (2000) Curr. Opin. Chem. Biol. , vol.4 , pp. 567-572
    • Kappock, T.J.1    Ealick, S.E.2    Stubbe, J.3
  • 2
    • 0028898649 scopus 로고
    • Investigation of the mechanism of phosphoribosylamine transfer from glutamine phosphoribosylpyrophosphate amidotransferase to glycinamide ribonucleotide synthetase
    • Rudolph, J., and Stubbe, J. (1995) Investigation of the mechanism of phosphoribosylamine transfer from glutamine phosphoribosylpyrophosphate amidotransferase to glycinamide ribonucleotide synthetase, Biochemistry 34, 2241-2250.
    • (1995) Biochemistry , vol.34 , pp. 2241-2250
    • Rudolph, J.1    Stubbe, J.2
  • 4
    • 0001007592 scopus 로고    scopus 로고
    • X-ray crystal structure of aminoimidazole ribonucleotide synthetase (PurM), from the Escherichia coli purine biosynthetic pathway at 2.5 Å resolution
    • Li, C., Kappock, T. J., Stubbe, J., Weaver, T. M., and Ealick, S. E. (1999) X-ray crystal structure of aminoimidazole ribonucleotide synthetase (PurM), from the Escherichia coli purine biosynthetic pathway at 2.5 Å resolution, Struct. Fold. Des. 7, 1155-1166.
    • (1999) Struct. Fold. Des. , vol.7 , pp. 1155-1166
    • Li, C.1    Kappock, T.J.2    Stubbe, J.3    Weaver, T.M.4    Ealick, S.E.5
  • 5
    • 0033520069 scopus 로고    scopus 로고
    • Investigation of the ATP binding site of Escherichia coli aminoimidazole ribonucleotide synthetase using affinity labeling and site-directed mutagenesis
    • Mueller, E. J., Oh, S., Kavalerchik, E., Kappock, T. J., Meyer, E., Li, C., Ealick, S. E., and Stubbe, J. (1999) Investigation of the ATP binding site of Escherichia coli aminoimidazole ribonucleotide synthetase using affinity labeling and site-directed mutagenesis, Biochemistry 38, 9831-9839.
    • (1999) Biochemistry , vol.38 , pp. 9831-9839
    • Mueller, E.J.1    Oh, S.2    Kavalerchik, E.3    Kappock, T.J.4    Meyer, E.5    Li, C.6    Ealick, S.E.7    Stubbe, J.8
  • 6
    • 0023655214 scopus 로고
    • Cloning and characterization of a 12-gene cluster from Bacillus subtilis encoding nine enzymes for de novo purine nucleotide synthesis
    • Ebbole, D. J., and Zalkin, H. (1987) Cloning and characterization of a 12-gene cluster from Bacillus subtilis encoding nine enzymes for de novo purine nucleotide synthesis, J. Biol. Chem. 262, 8274-8287.
    • (1987) J. Biol. Chem. , vol.262 , pp. 8274-8287
    • Ebbole, D.J.1    Zalkin, H.2
  • 7
    • 0034038010 scopus 로고    scopus 로고
    • The yexA gene product is required for phosphoribosylformylglycinamidine synthetase activity in Bacillus subtilis
    • Saxild, H. H., and Nygaard, P. (2000) The yexA gene product is required for phosphoribosylformylglycinamidine synthetase activity in Bacillus subtilis, Microbiology 146 (Part 4), 807-814.
    • (2000) Microbiology , vol.146 , Issue.PART 4 , pp. 807-814
    • Saxild, H.H.1    Nygaard, P.2
  • 9
    • 0028298029 scopus 로고
    • Cloning and characterization of a new purine biosynthetic enzyme: A non-folate glycinamide ribonucleotide transformylase from E. coli
    • Marolewski, A., Smith, J. M., and Benkovic, S. J. (1994) Cloning and characterization of a new purine biosynthetic enzyme: a non-folate glycinamide ribonucleotide transformylase from E. coli, Biochemistry 33, 2531-2537.
    • (1994) Biochemistry , vol.33 , pp. 2531-2537
    • Marolewski, A.1    Smith, J.M.2    Benkovic, S.J.3
  • 10
    • 0037189553 scopus 로고    scopus 로고
    • PurT-encoded glycinamide ribonucleotide transformylase. Accommodation of adenosine nucleotide analogues within the active site
    • Thoden, J. B., Firestine, S. M., Benkovic, S. J., and Holden, H. M. (2002) PurT-encoded glycinamide ribonucleotide transformylase. Accommodation of adenosine nucleotide analogues within the active site, J. Biol. Chem. 277, 23898-23908.
    • (2002) J. Biol. Chem. , vol.277 , pp. 23898-23908
    • Thoden, J.B.1    Firestine, S.M.2    Benkovic, S.J.3    Holden, H.M.4
  • 11
    • 0024596256 scopus 로고
    • Formylglycinamide ribonucleotide synthetase from Escherichia coli: Cloning, sequencing, overproduction, isolation, and characterization
    • Schendel, F. J., Mueller, E., Stubbe, J., Shiau, A., and Smith, J. M. (1989) Formylglycinamide ribonucleotide synthetase from Escherichia coli: cloning, sequencing, overproduction, isolation, and characterization, Biochemistry 28, 2459-2471.
    • (1989) Biochemistry , vol.28 , pp. 2459-2471
    • Schendel, F.J.1    Mueller, E.2    Stubbe, J.3    Shiau, A.4    Smith, J.M.5
  • 12
    • 4043055054 scopus 로고    scopus 로고
    • Domain organization of Salmonella typhimurium forymylglycinamide ribonucleotide amidotransferase revealed by x-ray crystallography
    • Anand, R., Hoskins, A. A., Stubbe, J., and Ealick, S. E. (2004) Domain Organization of Salmonella typhimurium Forymylglycinamide Ribonucleotide Amidotransferase Revealed by X-ray Crystallography, Biochemistry 43, 10328-10342.
    • (2004) Biochemistry , vol.43 , pp. 10328-10342
    • Anand, R.1    Hoskins, A.A.2    Stubbe, J.3    Ealick, S.E.4
  • 13
    • 71849104860 scopus 로고
    • Protein measurement with the Folin phenol reagent
    • Lowry, O. H. R., Nira J., Farr, A. L., and Randall, R. J. (1951) Protein measurement with the Folin phenol reagent, J. Biol. Chem. 193, 265-275.
    • (1951) J. Biol. Chem. , vol.193 , pp. 265-275
    • Lowry, O.H.R.1    Nira, J.2    Farr, A.L.3    Randall, R.J.4
  • 14
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schaegger, H., and Von Jagow, G. (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa, Anal. Biochem. 166, 368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schaegger, H.1    Von Jagow, G.2
  • 16
    • 0027254139 scopus 로고
    • Imidazole glycerol phosphate synthase: The glutamine amidotransferase in histidine biosynthesis
    • Klem, T. J., and Davisson, V. J. (1993) Imidazole glycerol phosphate synthase: the glutamine amidotransferase in histidine biosynthesis, Biochemistry 32, 5177-5186.
    • (1993) Biochemistry , vol.32 , pp. 5177-5186
    • Klem, T.J.1    Davisson, V.J.2
  • 17
    • 0023055073 scopus 로고
    • Substrate specificity of formylglycinamidine synthetase
    • Schendel, F. J., and Stubbe, J. (1986) Substrate specificity of formylglycinamidine synthetase, Biochemistry 25, 2256-2264.
    • (1986) Biochemistry , vol.25 , pp. 2256-2264
    • Schendel, F.J.1    Stubbe, J.2
  • 18
    • 0026643934 scopus 로고
    • p-aminobenzoate synthesis in Escherichia coli: Kinetic and mechanistic characterization of the amidotransferase PabA
    • Roux, B., and Walsh, C. T. (1992) p-Aminobenzoate synthesis in Escherichia coli: kinetic and mechanistic characterization of the amidotransferase PabA, Biochemistry 31, 6904-6910.
    • (1992) Biochemistry , vol.31 , pp. 6904-6910
    • Roux, B.1    Walsh, C.T.2
  • 19
    • 0013818092 scopus 로고
    • N-formimino-L-glutamate formiminohydrolase of Aerobacter aerogenes
    • Lund, P., and Magasanik, B. (1965) N-Formimino-L-glutamate Formiminohydrolase of Aerobacter aerogenes, J. Biol. Chem. 240, 4316-4319.
    • (1965) J. Biol. Chem. , vol.240 , pp. 4316-4319
    • Lund, P.1    Magasanik, B.2
  • 21
    • 0015218425 scopus 로고
    • Biosynthesis of the purines. XXXIII. Catalytic properties of the glutamine site of formylglycinamide ribonucleotide amidotransferase from chicken liver
    • Li, H. C., and Buchanan, J. M. (1971) Biosynthesis of the purines. XXXIII. Catalytic properties of the glutamine site of formylglycinamide ribonucleotide amidotransferase from chicken liver, J. Biol. Chem. 246, 4713-4719.
    • (1971) J. Biol. Chem. , vol.246 , pp. 4713-4719
    • Li, H.C.1    Buchanan, J.M.2
  • 22
    • 0014430020 scopus 로고
    • Biosynthesis of the purines. XXX. Isolation and characterization of formylglycinamide ribonucleotide amidotransferase-glutamyl complex
    • Mizobuchi, K., and Buchanan, J. M. (1968) Biosynthesis of the purines. XXX. Isolation and characterization of formylglycinamide ribonucleotide amidotransferase-glutamyl complex, J. Biol. Chem. 243, 4853-4862.
    • (1968) J. Biol. Chem. , vol.243 , pp. 4853-4862
    • Mizobuchi, K.1    Buchanan, J.M.2
  • 23
    • 0014430004 scopus 로고
    • Biosynthesis of the purines. XXIX. Purification and properties of formylglycinamide ribonucleotide amidotransferase from chicken liver
    • Mizobuchi, K., and Buchanan, J. M. (1968) Biosynthesis of the purines. XXIX. Purification and properties of formylglycinamide ribonucleotide amidotransferase from chicken liver, J. Biol. Chem. 243, 4842-4852.
    • (1968) J. Biol. Chem. , vol.243 , pp. 4842-4852
    • Mizobuchi, K.1    Buchanan, J.M.2
  • 24
    • 0342894815 scopus 로고    scopus 로고
    • Coupled formation of an amidotransferase nterdomain ammonia channel and a phosphoribosyltransferase active site
    • Krahn, J. M., Kim, J. H., Burns, M. R., Parry, R. J., Zalkin, H., and Smith, J. L. (1997) Coupled formation of an amidotransferase nterdomain ammonia channel and a phosphoribosyltransferase active site, Biochemistry 36, 11061-11068.
    • (1997) Biochemistry , vol.36 , pp. 11061-11068
    • Krahn, J.M.1    Kim, J.H.2    Burns, M.R.3    Parry, R.J.4    Zalkin, H.5    Smith, J.L.6
  • 25
    • 0030957783 scopus 로고    scopus 로고
    • Structure of carbamoyl phosphate synthetase: A journey of 96 Å from substrate to product
    • Thoden, J. B., Holden, H. M., Wesenberg, G., Raushel, F. M., and Rayment, I. (1997) Structure of carbamoyl phosphate synthetase: a journey of 96 Å from substrate to product, Biochemistry 36, 6305-6316.
    • (1997) Biochemistry , vol.36 , pp. 6305-6316
    • Thoden, J.B.1    Holden, H.M.2    Wesenberg, G.3    Raushel, F.M.4    Rayment, I.5
  • 26
    • 0033594447 scopus 로고    scopus 로고
    • Channeling of ammonia through the intermolecular tunnel contained within carbamoyl phosphate synthetase
    • Mullins, L. S., and Raushel, F. M. (1999) Channeling of Ammonia through the Intermolecular Tunnel Contained within Carbamoyl Phosphate Synthetase, J. Am. Chem. Soc. 121, 3803-3804.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 3803-3804
    • Mullins, L.S.1    Raushel, F.M.2
  • 27
    • 0015133872 scopus 로고
    • Reversible dissociation of carbamyl phosphate synthetase into a regulated synthesis subunit and a subunit required for glutamine utilization
    • Trotta, P. P., Burt, M. E., Haschemeyer, R. H., and Meister, A. (1971) Reversible Dissociation of Carbamyl Phosphate Synthetase into a Regulated Synthesis Subunit and a Subunit Required for Glutamine Utilization, Proc. Natl. Acad. Sci. U.S.A. 68, 2599-2603.
    • (1971) Proc. Natl. Acad. Sci. U.S.A. , vol.68 , pp. 2599-2603
    • Trotta, P.P.1    Burt, M.E.2    Haschemeyer, R.H.3    Meister, A.4
  • 28
    • 0001395809 scopus 로고
    • Anthranilate synthetase from Serratia marcescens
    • Zalkin, H., and Hwang, L. H. (1971) Anthranilate Synthetase from Serratia marcescens, J. Biol. Chem. 216, 6899-6907.
    • (1971) J. Biol. Chem. , vol.216 , pp. 6899-6907
    • Zalkin, H.1    Hwang, L.H.2
  • 29
    • 0030573517 scopus 로고    scopus 로고
    • Escherichia coli aminodeoxychorismate synthase: Analysis of pabB mutations affecting catalysis and subunit association
    • Rayl, E. A., Green, J. M., and Nichols, B. P. (1996) Escherichia coli aminodeoxychorismate synthase: analysis of pabB mutations affecting catalysis and subunit association, Biochim. Biophys. Acta 1295, 81-88.
    • (1996) Biochim. Biophys. Acta , vol.1295 , pp. 81-88
    • Rayl, E.A.1    Green, J.M.2    Nichols, B.P.3
  • 30
    • 4043110518 scopus 로고    scopus 로고
    • A model for the Bacillus subtilis formylgycinamide ribonucleotide amidotransferase complex
    • Anand, R., Hoskins, A. A., Sintchak, M. D., Bennet, E. M., Stubbe, J., and Ealick, S. E. (2004) A Model for the Bacillus subtilis Formylgycinamide Ribonucleotide Amidotransferase Complex, Biochemistry 43, 10343-10352.
    • (2004) Biochemistry , vol.43 , pp. 10343-10352
    • Anand, R.1    Hoskins, A.A.2    Sintchak, M.D.3    Bennet, E.M.4    Stubbe, J.5    Ealick, S.E.6
  • 31
    • 0036836521 scopus 로고    scopus 로고
    • Crystal structure of MTH169, a crucial component of phosphoribosylformylglycinamidine synthetase
    • Batra, R., Christendat, D., Edwards, A., Arrowsmith, C., and Tong, L. (2002) Crystal structure of MTH169, a crucial component of phosphoribosylformylglycinamidine synthetase, Proteins 49, 285-288.
    • (2002) Proteins , vol.49 , pp. 285-288
    • Batra, R.1    Christendat, D.2    Edwards, A.3    Arrowsmith, C.4    Tong, L.5
  • 32
    • 0034714314 scopus 로고    scopus 로고
    • Restricted passage of reaction intermediates through the ammonia tunnel of carbamoyl phosphate synthetase
    • Huang, X., and Raushel, F. M. (2000) Restricted passage of reaction intermediates through the ammonia tunnel of carbamoyl phosphate synthetase, J. Biol. Chem. 275, 26233-26240.
    • (2000) J. Biol. Chem. , vol.275 , pp. 26233-26240
    • Huang, X.1    Raushel, F.M.2
  • 33
    • 0037133196 scopus 로고    scopus 로고
    • Structure of Escherichia coli aminodeoxychorismate synthase: Architectural conservation and diversity in chorismate-utilizing enzymes
    • Parsons, J. F., Jensen, P. Y., Pachikara, A. S., Howard, A. J., Eisenstein, E., and Ladner, J. E. (2002) Structure of Escherichia coli Aminodeoxychorismate Synthase: Architectural Conservation and Diversity in Chorismate-Utilizing Enzymes, Biochemistry 41, 2198-2208.
    • (2002) Biochemistry , vol.41 , pp. 2198-2208
    • Parsons, J.F.1    Jensen, P.Y.2    Pachikara, A.S.3    Howard, A.J.4    Eisenstein, E.5    Ladner, J.E.6
  • 34
    • 0033533463 scopus 로고    scopus 로고
    • Tryptophan fluorescence monitors multiple conformational changes required for glutamine phosphoribosylpyrophosphate amidotransferase interdomain signaling and catalysis
    • Chen, S., Burgner, J. W., Krahn, J. M., Smith, J. L., and Zalkin, H. (1999) Tryptophan fluorescence monitors multiple conformational changes required for glutamine phosphoribosylpyrophosphate amidotransferase interdomain signaling and catalysis, Biochemistry 38, 11659-11669.
    • (1999) Biochemistry , vol.38 , pp. 11659-11669
    • Chen, S.1    Burgner, J.W.2    Krahn, J.M.3    Smith, J.L.4    Zalkin, H.5
  • 35
    • 0033619728 scopus 로고    scopus 로고
    • Deconstruction of the catalytic array within the amidotransferase subunit of carbamoyl phosphate synthetase
    • Huang, X., and Raushel, F. M. (1999) Deconstruction of the catalytic array within the amidotransferase subunit of carbamoyl phosphate synthetase, Biochemistry 38, 15909-15914.
    • (1999) Biochemistry , vol.38 , pp. 15909-15914
    • Huang, X.1    Raushel, F.M.2
  • 36
    • 0023666970 scopus 로고
    • Chorismate aminations: Partial purification of Escherichia coli PABA synthase and mechanistic comparison with anthranilate synthase
    • Walsh, C. T., Erion, M. D., Walts, A. E., Delany, J. J., 3rd, and Berchtold, G. A. (1987) Chorismate aminations: partial purification of Escherichia coli PABA synthase and mechanistic comparison with anthranilate synthase, Biochemistry 26, 4734-4745.
    • (1987) Biochemistry , vol.26 , pp. 4734-4745
    • Walsh, C.T.1    Erion, M.D.2    Walts, A.E.3    Delany III, J.J.4    Berchtold, G.A.5


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