메뉴 건너뛰기




Volumn 17, Issue 6, 2007, Pages 653-664

Conformational changes in ammonia-channeling glutamine amidotransferases

Author keywords

[No Author keywords available]

Indexed keywords

AMMONIA; GLUTAMINE PHENYLPYRUVATE AMINOTRANSFERASE;

EID: 36549013217     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.sbi.2007.09.003     Document Type: Review
Times cited : (83)

References (49)
  • 4
    • 0042377362 scopus 로고    scopus 로고
    • + synthetase Qns1 contains an essential, obligate intramolecular thiol glutamine amidotransferase domain related to nitrilase
    • + synthetase Qns1 contains an essential, obligate intramolecular thiol glutamine amidotransferase domain related to nitrilase. J Biol Chem 278 (2003) 33049-33055
    • (2003) J Biol Chem , vol.278 , pp. 33049-33055
    • Bieganowski, P.1    Pace, H.C.2    Brenner, C.3
  • 5
    • 0032872139 scopus 로고    scopus 로고
    • Fundamental mechanisms of substrate channeling
    • Anderson K.S. Fundamental mechanisms of substrate channeling. Methods Enzymol 308 (1999) 111-145
    • (1999) Methods Enzymol , vol.308 , pp. 111-145
    • Anderson, K.S.1
  • 6
    • 0033617187 scopus 로고    scopus 로고
    • The molecular basis of substrate channeling
    • Miles E.W., Rhee S., and Davies D.R. The molecular basis of substrate channeling. J Biol Chem 274 (1999) 12193-12196
    • (1999) J Biol Chem , vol.274 , pp. 12193-12196
    • Miles, E.W.1    Rhee, S.2    Davies, D.R.3
  • 7
    • 0033594932 scopus 로고    scopus 로고
    • The amidotransferase family of enzymes: molecular machines for the production and delivery of ammonia
    • Raushel F.M., Thoden J.B., and Holden H.M. The amidotransferase family of enzymes: molecular machines for the production and delivery of ammonia. Biochemistry 38 (1999) 7891-7899
    • (1999) Biochemistry , vol.38 , pp. 7891-7899
    • Raushel, F.M.1    Thoden, J.B.2    Holden, H.M.3
  • 8
    • 0034919604 scopus 로고    scopus 로고
    • Channeling of substrates and intermediates in enzyme-catalyzed reactions
    • Huang X., Holden H.M., and Raushel F.M. Channeling of substrates and intermediates in enzyme-catalyzed reactions. Annu Rev Biochem 70 (2001) 149-180
    • (2001) Annu Rev Biochem , vol.70 , pp. 149-180
    • Huang, X.1    Holden, H.M.2    Raushel, F.M.3
  • 9
    • 33645240462 scopus 로고    scopus 로고
    • Glutamine binding opens the ammonia channel and activates glucosamine-6P synthase
    • The crystal structures of acceptor-bound GlmS with and without a glutamine affinity analog at 2.35 and 2.05 Å resolution, respectively, show that glutamine binding activates the enzyme through the closing of a loop to shield the glutaminase site, the positioning of several catalytic residues, and the opening of the ammonia channel thanks to a rotation of the Trp74 indole group.
    • Mouilleron S., Badet-Denisot M.-A., and Golinelli-Pimpaneau B. Glutamine binding opens the ammonia channel and activates glucosamine-6P synthase. J Biol Chem 281 (2006) 4404-4412. The crystal structures of acceptor-bound GlmS with and without a glutamine affinity analog at 2.35 and 2.05 Å resolution, respectively, show that glutamine binding activates the enzyme through the closing of a loop to shield the glutaminase site, the positioning of several catalytic residues, and the opening of the ammonia channel thanks to a rotation of the Trp74 indole group.
    • (2006) J Biol Chem , vol.281 , pp. 4404-4412
    • Mouilleron, S.1    Badet-Denisot, M.-A.2    Golinelli-Pimpaneau, B.3
  • 10
    • 0342894815 scopus 로고    scopus 로고
    • Coupled formation of an amidotransferase interdomain 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. Coupled formation of an amidotransferase interdomain ammonia channel and a phosphoribosyltransferase active site. Biochemistry 36 (1997) 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
  • 11
    • 0031941411 scopus 로고    scopus 로고
    • Crystal structure of glutamine phosphoribosylpyrophosphate amidotransferase from Escherichia coli
    • Muchmore C.R., Krahn J.M., Kim J.H., Zalkin H., and Smith J.L. Crystal structure of glutamine phosphoribosylpyrophosphate amidotransferase from Escherichia coli. Protein Sci 7 (1998) 39-51
    • (1998) Protein Sci , vol.7 , pp. 39-51
    • Muchmore, C.R.1    Krahn, J.M.2    Kim, J.H.3    Zalkin, H.4    Smith, J.L.5
  • 12
    • 0038614879 scopus 로고    scopus 로고
    • Toward understanding the mechanism of the complex cyclization reaction catalyzed by imidazole glycerolphosphate synthase: crystal structures of a ternary complex and the free enzyme
    • Chaudhuri B.N., Lange S.C., Myers R.S., Davisson V.J., and Smith J.L. Toward understanding the mechanism of the complex cyclization reaction catalyzed by imidazole glycerolphosphate synthase: crystal structures of a ternary complex and the free enzyme. Biochemistry 42 (2003) 7003-7012
    • (2003) Biochemistry , vol.42 , pp. 7003-7012
    • Chaudhuri, B.N.1    Lange, S.C.2    Myers, R.S.3    Davisson, V.J.4    Smith, J.L.5
  • 13
    • 0036175240 scopus 로고    scopus 로고
    • Structural evidence for ammonia tunneling across the (beta alpha)(8) barrel of the imidazole glycerol phosphate synthase bienzyme complex
    • Douangamath A., Walker M., Beismann-Driemeyer S., Vega-Fernandez M.C., Sterner R., and Wilmanns M. Structural evidence for ammonia tunneling across the (beta alpha)(8) barrel of the imidazole glycerol phosphate synthase bienzyme complex. Structure 10 (2002) 185-193
    • (2002) Structure , vol.10 , pp. 185-193
    • Douangamath, A.1    Walker, M.2    Beismann-Driemeyer, S.3    Vega-Fernandez, M.C.4    Sterner, R.5    Wilmanns, M.6
  • 15
    • 26444567797 scopus 로고    scopus 로고
    • Structural basis for tRNA-dependent amidotransferase function
    • Schmitt E., Panvert M., Blanquet S., and Mechulam Y. Structural basis for tRNA-dependent amidotransferase function. Structure 13 (2005) 1421-1433
    • (2005) Structure , vol.13 , pp. 1421-1433
    • Schmitt, E.1    Panvert, M.2    Blanquet, S.3    Mechulam, Y.4
  • 16
    • 33745596803 scopus 로고    scopus 로고
    • Ammonia channel couples glutaminase with transamidase reactions in GatCAB
    • Glu by GatCAB is shown to be achieved by specific recognition of the U1-A72 base pair whereas the insertion of a U in the D-loop of tRNA serves as a negative determinant.
    • Glu by GatCAB is shown to be achieved by specific recognition of the U1-A72 base pair whereas the insertion of a U in the D-loop of tRNA serves as a negative determinant.
    • (2006) Science , vol.312 , pp. 1954-1958
    • Nakamura, A.1    Yao, M.2    Chimnaronk, S.3    Sakai, N.4    Tanaka, I.5
  • 17
    • 0033534161 scopus 로고    scopus 로고
    • Three-dimensional structure of Escherichia coli asparagine synthetase B: a short journey from substrate to product
    • Larsen T.M., Boehlein S.K., Schuster S.M., Richards N.G., Thoden J.B., Holden H.M., and Rayment I. Three-dimensional structure of Escherichia coli asparagine synthetase B: a short journey from substrate to product. Biochemistry 38 (1999) 16146-16157
    • (1999) Biochemistry , vol.38 , pp. 16146-16157
    • Larsen, T.M.1    Boehlein, S.K.2    Schuster, S.M.3    Richards, N.G.4    Thoden, J.B.5    Holden, H.M.6    Rayment, I.7
  • 18
    • 0030024963 scopus 로고    scopus 로고
    • The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families
    • Tesmer J.J., Klem T.J., Deras M.L., Davisson V.J., and Smith J.L. The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families. Nat Struct Biol 3 (1996) 74-86
    • (1996) Nat Struct Biol , vol.3 , pp. 74-86
    • Tesmer, J.J.1    Klem, T.J.2    Deras, M.L.3    Davisson, V.J.4    Smith, J.L.5
  • 19
    • 4143092510 scopus 로고    scopus 로고
    • Crystal structures of CTP synthetase reveal ATP, UTP, and glutamine binding sites
    • Goto M., Omi R., Nakagawa N., Miyahara I., and Hirotsu K. Crystal structures of CTP synthetase reveal ATP, UTP, and glutamine binding sites. Structure 12 (2004) 1413-1423
    • (2004) Structure , vol.12 , pp. 1413-1423
    • Goto, M.1    Omi, R.2    Nakagawa, N.3    Miyahara, I.4    Hirotsu, K.5
  • 20
    • 0035123059 scopus 로고    scopus 로고
    • Structure of the cooperative allosteric anthranilate synthase from Salmonella typhimurium
    • Morollo A.A., and Eck M.J. Structure of the cooperative allosteric anthranilate synthase from Salmonella typhimurium. Nat Struct Biol 8 (2001) 243-247
    • (2001) Nat Struct Biol , vol.8 , pp. 243-247
    • Morollo, A.A.1    Eck, M.J.2
  • 21
    • 0029920154 scopus 로고    scopus 로고
    • Structure and function of the glutamine phosphoribosylpyrophosphate amidotransferase glutamine site and communication with the phosphoribosylpyrophosphate site
    • Kim J.H., Krahn J.M., Tomchick D.R., Smith J.L., and Zalkin H. Structure and function of the glutamine phosphoribosylpyrophosphate amidotransferase glutamine site and communication with the phosphoribosylpyrophosphate site. J Biol Chem 271 (1996) 15549-15557
    • (1996) J Biol Chem , vol.271 , pp. 15549-15557
    • Kim, J.H.1    Krahn, J.M.2    Tomchick, D.R.3    Smith, J.L.4    Zalkin, H.5
  • 22
    • 4043055054 scopus 로고    scopus 로고
    • Domain organization of Salmonella typhimurium formylglycinamide ribonucleotide amidotransferase revealed by X-ray crystallography
    • Anand R., Hoskins A.A., Stubbe J., and Ealick S.E. Domain organization of Salmonella typhimurium formylglycinamide ribonucleotide amidotransferase revealed by X-ray crystallography. Biochemistry 43 (2004) 10328-10342
    • (2004) Biochemistry , vol.43 , pp. 10328-10342
    • Anand, R.1    Hoskins, A.A.2    Stubbe, J.3    Ealick, S.E.4
  • 23
    • 1842610703 scopus 로고    scopus 로고
    • Glutamate synthase: a fascinating pathway from l-glutamine to l-glutamate
    • Van den Heuvel R.H., Curti B., Vanoni M.A., and Mattevi A. Glutamate synthase: a fascinating pathway from l-glutamine to l-glutamate. Cell Mol Life Sci 61 (2004) 669-681
    • (2004) Cell Mol Life Sci , vol.61 , pp. 669-681
    • Van den Heuvel, R.H.1    Curti, B.2    Vanoni, M.A.3    Mattevi, A.4
  • 25
    • 0034793603 scopus 로고    scopus 로고
    • Crystal structure of imidazole glycerol phosphate synthase: a tunnel through a (beta/alpha)8 barrel joins two active sites
    • Chaudhuri B.N., Lange S.C., Myers R.S., Chittur S.V., Davisson V.J., and Smith J.L. Crystal structure of imidazole glycerol phosphate synthase: a tunnel through a (beta/alpha)8 barrel joins two active sites. Structure (Camb) 9 (2001) 987-997
    • (2001) Structure (Camb) , vol.9 , pp. 987-997
    • Chaudhuri, B.N.1    Lange, S.C.2    Myers, R.S.3    Chittur, S.V.4    Davisson, V.J.5    Smith, J.L.6
  • 27
    • 34247188490 scopus 로고    scopus 로고
    • Activation and coupling of the glutaminase and synthase reaction of glutamate synthase is mediated by E1013 of the ferredoxin-dependent enzyme, belonging to loop 4 of the synthase domain
    • Dossena L., Curti B., and Vanoni M.A. Activation and coupling of the glutaminase and synthase reaction of glutamate synthase is mediated by E1013 of the ferredoxin-dependent enzyme, belonging to loop 4 of the synthase domain. Biochemistry 46 (2007) 4473-4485
    • (2007) Biochemistry , vol.46 , pp. 4473-4485
    • Dossena, L.1    Curti, B.2    Vanoni, M.A.3
  • 28
    • 0037938734 scopus 로고    scopus 로고
    • Substrate-induced changes in the ammonia channel for imidazole glycerol phosphate synthase
    • Myers R.S., Jensen J.R., Deras I.L., Smith J.L., and Davisson V.J. Substrate-induced changes in the ammonia channel for imidazole glycerol phosphate synthase. Biochemistry 42 (2003) 7013-7022
    • (2003) Biochemistry , vol.42 , pp. 7013-7022
    • Myers, R.S.1    Jensen, J.R.2    Deras, I.L.3    Smith, J.L.4    Davisson, V.J.5
  • 29
    • 33847262173 scopus 로고    scopus 로고
    • Domain motions of glucosamine-6P synthase: comparison of the anisotropic displacements in the crystals and the catalytic hinge-bending rotation
    • The analysis of the anisotropic domain displacements observed in the crystals of GlmS in complex with acceptor, and in complex with both acceptor and glutamine affinity analog, suggests that the intramolecular mobility of the sugar-bound enzyme contributes to facilitate the domain motion that occurs upon glutamine binding during catalysis.
    • Mouilleron S., and Golinelli-Pimpaneau B. Domain motions of glucosamine-6P synthase: comparison of the anisotropic displacements in the crystals and the catalytic hinge-bending rotation. Protein Sci 16 (2007) 485-493. The analysis of the anisotropic domain displacements observed in the crystals of GlmS in complex with acceptor, and in complex with both acceptor and glutamine affinity analog, suggests that the intramolecular mobility of the sugar-bound enzyme contributes to facilitate the domain motion that occurs upon glutamine binding during catalysis.
    • (2007) Protein Sci , vol.16 , pp. 485-493
    • Mouilleron, S.1    Golinelli-Pimpaneau, B.2
  • 30
    • 33845928807 scopus 로고    scopus 로고
    • Structure of a bacterial pyridoxal 5′-phosphate synthase complex
    • The structure of PLP synthase from Bacillus subtilis in complex with glutamine at 2.1 Å resolution as well as those of the individual glutaminase and synthase subunits is reported. The complex consists of a core of 12 synthase monomers with 12 noninteracting glutaminase subunits attached to the core. Comparison of the different structures shows the structural changes occurring upon complex formation.
    • Strohmeier M., Raschle T., Mazurkiewicz J., Rippe K., Sinning I., Fitzpatrick T.B., and Tews I. Structure of a bacterial pyridoxal 5′-phosphate synthase complex. Proc Natl Acad Sci U S A 103 (2006) 19284-19289. The structure of PLP synthase from Bacillus subtilis in complex with glutamine at 2.1 Å resolution as well as those of the individual glutaminase and synthase subunits is reported. The complex consists of a core of 12 synthase monomers with 12 noninteracting glutaminase subunits attached to the core. Comparison of the different structures shows the structural changes occurring upon complex formation.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 19284-19289
    • Strohmeier, M.1    Raschle, T.2    Mazurkiewicz, J.3    Rippe, K.4    Sinning, I.5    Fitzpatrick, T.B.6    Tews, I.7
  • 31
    • 33845468647 scopus 로고    scopus 로고
    • Structural insights into the mechanism of the PLP synthase holoenzyme from Thermotoga maritima
    • The structure of PLP synthase from Thermotoga maritima at 2.9 Å resolution reveals that the complex consists of a core of 12 synthase monomers with 12 noninteracting glutaminase subunits attached to the core. The acceptor substrate, ribulose-5-P, is bound via an imine bond to the synthase site, which allows the authors to propose a mechanism for the reaction.
    • Zein F., Zhang Y., Kang Y.N., Burns K., Begley T.P., and Ealick S.E. Structural insights into the mechanism of the PLP synthase holoenzyme from Thermotoga maritima. Biochemistry 45 (2006) 14609-14620. The structure of PLP synthase from Thermotoga maritima at 2.9 Å resolution reveals that the complex consists of a core of 12 synthase monomers with 12 noninteracting glutaminase subunits attached to the core. The acceptor substrate, ribulose-5-P, is bound via an imine bond to the synthase site, which allows the authors to propose a mechanism for the reaction.
    • (2006) Biochemistry , vol.45 , pp. 14609-14620
    • Zein, F.1    Zhang, Y.2    Kang, Y.N.3    Burns, K.4    Begley, T.P.5    Ealick, S.E.6
  • 32
    • 23044515503 scopus 로고    scopus 로고
    • A new arrangement of (beta/alpha)8 barrels in the synthase subunit of PLP synthase
    • Zhu J., Burgner J.W., Harms E., Belitsky B.R., and Smith J.L. A new arrangement of (beta/alpha)8 barrels in the synthase subunit of PLP synthase. J Biol Chem 280 (2005) 27914-27923
    • (2005) J Biol Chem , vol.280 , pp. 27914-27923
    • Zhu, J.1    Burgner, J.W.2    Harms, E.3    Belitsky, B.R.4    Smith, J.L.5
  • 33
    • 1642453681 scopus 로고    scopus 로고
    • Three-dimensional structure of YaaE from Bacillus subtilis, a glutaminase implicated in pyridoxal-5′-phosphate biosynthesis
    • Bauer J.A., Bennett E.M., Begley T.P., and Ealick S.E. Three-dimensional structure of YaaE from Bacillus subtilis, a glutaminase implicated in pyridoxal-5′-phosphate biosynthesis. J Biol Chem 279 (2004) 2704-2711
    • (2004) J Biol Chem , vol.279 , pp. 2704-2711
    • Bauer, J.A.1    Bennett, E.M.2    Begley, T.P.3    Ealick, S.E.4
  • 35
    • 0030586024 scopus 로고    scopus 로고
    • Substrate binding is required for assembly of the active conformation of the catalytic site in Ntn amidotransferases: evidence from the 1.8 Å crystal structure of the glutaminase domain of glucosamine 6-phosphate synthase
    • Isupov M.N., Obmolova G., Butterworth S., Badet-Denisot M.A., Badet B., Polikarpov I., Littlechild J.A., and Teplyakov A. Substrate binding is required for assembly of the active conformation of the catalytic site in Ntn amidotransferases: evidence from the 1.8 Å crystal structure of the glutaminase domain of glucosamine 6-phosphate synthase. Structure 4 (1996) 801-810
    • (1996) Structure , vol.4 , pp. 801-810
    • Isupov, M.N.1    Obmolova, G.2    Butterworth, S.3    Badet-Denisot, M.A.4    Badet, B.5    Polikarpov, I.6    Littlechild, J.A.7    Teplyakov, A.8
  • 37
    • 23244441019 scopus 로고    scopus 로고
    • Reaction coupling through interdomain contacts in imidazole glycerol phosphate synthase
    • Myers R.S., Amaro R.E., Luthey-Schulten Z.A., and Davisson V.J. Reaction coupling through interdomain contacts in imidazole glycerol phosphate synthase. Biochemistry 44 (2005) 11974-11985
    • (2005) Biochemistry , vol.44 , pp. 11974-11985
    • Myers, R.S.1    Amaro, R.E.2    Luthey-Schulten, Z.A.3    Davisson, V.J.4
  • 38
    • 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. Structure of carbamoyl phosphate synthetase: a journey of 96 Å from substrate to product. Biochemistry 36 (1997) 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
  • 39
    • 0035827583 scopus 로고    scopus 로고
    • Imidazole glycerol phosphate synthase from Thermotoga maritima. Quaternary structure, steady-state kinetics, and reaction mechanism of the bienzyme complex
    • Beismann-Driemeyer S., and Sterner R. Imidazole glycerol phosphate synthase from Thermotoga maritima. Quaternary structure, steady-state kinetics, and reaction mechanism of the bienzyme complex. J Biol Chem 276 (2001) 20387-20396
    • (2001) J Biol Chem , vol.276 , pp. 20387-20396
    • Beismann-Driemeyer, S.1    Sterner, R.2
  • 40
    • 0038325358 scopus 로고    scopus 로고
    • Structure of imidazole glycerol phosphate synthase from Thermus thermophilus HB8: open-closed conformational change and ammonia tunnelling
    • Omi R., Mizuguchi H., Goto M., Miyahara I., Hayashi H., Kagamiyama H., and Hirotsu K. Structure of imidazole glycerol phosphate synthase from Thermus thermophilus HB8: open-closed conformational change and ammonia tunnelling. J Biochem (Tokyo) 132 (2002) 759-765
    • (2002) J Biochem (Tokyo) , vol.132 , pp. 759-765
    • Omi, R.1    Mizuguchi, H.2    Goto, M.3    Miyahara, I.4    Hayashi, H.5    Kagamiyama, H.6    Hirotsu, K.7
  • 41
    • 2542604739 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli cytidine triphosphate synthetase, a nucleotide-regulated glutamine amidotransferase/ATP-dependent amidoligase fusion protein and homologue of anticancer and antiparasitic drug targets
    • Endrizzi J.A., Kim H., Anderson P.M., and Baldwin E.P. Crystal structure of Escherichia coli cytidine triphosphate synthetase, a nucleotide-regulated glutamine amidotransferase/ATP-dependent amidoligase fusion protein and homologue of anticancer and antiparasitic drug targets. Biochemistry 43 (2004) 6447-6463
    • (2004) Biochemistry , vol.43 , pp. 6447-6463
    • Endrizzi, J.A.1    Kim, H.2    Anderson, P.M.3    Baldwin, E.P.4
  • 42
    • 0029989648 scopus 로고    scopus 로고
    • + induces local and long-range changes in the three-dimensional structure of the tryptophan synthase alpha2beta2 complex
    • + induces local and long-range changes in the three-dimensional structure of the tryptophan synthase alpha2beta2 complex. Biochemistry 35 (1996) 4211-4221
    • (1996) Biochemistry , vol.35 , pp. 4211-4221
    • Rhee, S.1    Parris, K.D.2    Ahmed, S.A.3    Miles, E.W.4    Davies, D.R.5
  • 44
    • 0033534173 scopus 로고    scopus 로고
    • The small subunit of carbamoyl phosphate synthetase: snapshots along the reaction pathway
    • Thoden J.B., Huang X., Raushel F.M., and Holden H.M. The small subunit of carbamoyl phosphate synthetase: snapshots along the reaction pathway. Biochemistry 38 (1999) 16158-16166
    • (1999) Biochemistry , vol.38 , pp. 16158-16166
    • Thoden, J.B.1    Huang, X.2    Raushel, F.M.3    Holden, H.M.4
  • 45
    • 0035933197 scopus 로고    scopus 로고
    • The structures of anthranilate synthase of Serratia marcescens crystallized in the presence of (i) its substrates, chorismate and glutamine, and a product, glutamate, and (ii) its end-product inhibitor, l-tryptophan
    • Spraggon G., Kim C., Nguyen-Huu X., Yee M.C., Yanofsky C., and Mills S.E. The structures of anthranilate synthase of Serratia marcescens crystallized in the presence of (i) its substrates, chorismate and glutamine, and a product, glutamate, and (ii) its end-product inhibitor, l-tryptophan. Proc Natl Acad Sci U S A 98 (2001) 6021-6026
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 6021-6026
    • Spraggon, G.1    Kim, C.2    Nguyen-Huu, X.3    Yee, M.C.4    Yanofsky, C.5    Mills, S.E.6
  • 46
    • 0033596743 scopus 로고    scopus 로고
    • Carbamoyl phosphate synthetase: closure of the B-domain as a result of nucleotide binding
    • Thoden J.B., Wesenberg G., Raushel F.M., and Holden H.M. Carbamoyl phosphate synthetase: closure of the B-domain as a result of nucleotide binding. Biochemistry 38 (1999) 2347-2357
    • (1999) Biochemistry , vol.38 , pp. 2347-2357
    • Thoden, J.B.1    Wesenberg, G.2    Raushel, F.M.3    Holden, H.M.4
  • 48
    • 0030772416 scopus 로고    scopus 로고
    • Mechanism of the synergistic end-product regulation of Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase by nucleotides
    • Chen S., Tomchick D.R., Wolle D., Hu P., Smith J.L., Switzer R.L., and Zalkin H. Mechanism of the synergistic end-product regulation of Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase by nucleotides. Biochemistry 36 (1997) 10718-10726
    • (1997) Biochemistry , vol.36 , pp. 10718-10726
    • Chen, S.1    Tomchick, D.R.2    Wolle, D.3    Hu, P.4    Smith, J.L.5    Switzer, R.L.6    Zalkin, H.7
  • 49
    • 33845582675 scopus 로고    scopus 로고
    • Complexed structures of formylglycinamide ribonucleotide amidotransferase from Thermotoga maritima describe a novel ATP binding protein superfamily
    • Five different structures of the synthetase subunit of FGAR-AT from Thermotoga maritima have been determined in the presence of substrates, a substrate analog, and a product. The comparison of these structures to that of unliganded enzyme illuminate the conformational changes occurring upon acceptor and ATP binding to the synthase site.
    • Morar M., Anand R., Hoskins A.A., Stubbe J., and Ealick S.E. Complexed structures of formylglycinamide ribonucleotide amidotransferase from Thermotoga maritima describe a novel ATP binding protein superfamily. Biochemistry 45 (2006) 14880-14895. Five different structures of the synthetase subunit of FGAR-AT from Thermotoga maritima have been determined in the presence of substrates, a substrate analog, and a product. The comparison of these structures to that of unliganded enzyme illuminate the conformational changes occurring upon acceptor and ATP binding to the synthase site.
    • (2006) Biochemistry , vol.45 , pp. 14880-14895
    • Morar, M.1    Anand, R.2    Hoskins, A.A.3    Stubbe, J.4    Ealick, S.E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.