-
4
-
-
0042377362
-
+ 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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
14
-
-
33745587780
-
Structural basis of RNA-dependent recruitment of glutamine to the genetic code
-
Gln between the GluRS and GatDE enzymes.
-
Gln between the GluRS and GatDE enzymes.
-
(2006)
Science
, vol.312
, pp. 1950-1954
-
-
Oshikane, H.1
Sheppard, K.2
Fukai, S.3
Nakamura, Y.4
Ishitani, R.5
Numata, T.6
Sherrer, R.L.7
Feng, L.8
Schmitt, E.9
Panvert, M.10
-
15
-
-
26444567797
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
24
-
-
0038342691
-
The active conformation of glutamate synthase and its binding to ferredoxin
-
Van den Heuvel R.H., Svergun D.I., Petoukhov M.V., Coda A., Curti B., Ravasio S., Vanoni M.A., and Mattevi A. The active conformation of glutamate synthase and its binding to ferredoxin. J Mol Biol 330 (2003) 113-128
-
(2003)
J Mol Biol
, vol.330
, pp. 113-128
-
-
Van den Heuvel, R.H.1
Svergun, D.I.2
Petoukhov, M.V.3
Coda, A.4
Curti, B.5
Ravasio, S.6
Vanoni, M.A.7
Mattevi, A.8
-
25
-
-
0034793603
-
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
-
26
-
-
0033578351
-
The crystal structure of anthranilate synthase from Sulfolobus solfataricus: functional implications
-
Knochel T., Ivens A., Hester G., Gonzalez A., Bauerle R., Wilmanns M., Kirschner K., and Jansonius J.N. The crystal structure of anthranilate synthase from Sulfolobus solfataricus: functional implications. Proc Natl Acad Sci U S A 96 (1999) 9479-9484
-
(1999)
Proc Natl Acad Sci U S A
, vol.96
, pp. 9479-9484
-
-
Knochel, T.1
Ivens, A.2
Hester, G.3
Gonzalez, A.4
Bauerle, R.5
Wilmanns, M.6
Kirschner, K.7
Jansonius, J.N.8
-
27
-
-
34247188490
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
34
-
-
33645646965
-
Vitamin B6 biosynthesis by the malaria parasite Plasmodium falciparum: biochemical and structural insights
-
Gengenbacher M., Fitzpatrick T.B., Raschle T., Flicker K., Sinning I., Muller S., Macheroux P., Tews I., and Kappes B. Vitamin B6 biosynthesis by the malaria parasite Plasmodium falciparum: biochemical and structural insights. J Biol Chem 281 (2006) 3633-3641
-
(2006)
J Biol Chem
, vol.281
, pp. 3633-3641
-
-
Gengenbacher, M.1
Fitzpatrick, T.B.2
Raschle, T.3
Flicker, K.4
Sinning, I.5
Muller, S.6
Macheroux, P.7
Tews, I.8
Kappes, B.9
-
35
-
-
0030586024
-
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
-
36
-
-
0037110533
-
Crystal structure of glutamine amidotransferase from Thermotoga maritima
-
Korolev S., Skarina T., Evdokimova E., Beasley S., Edwards A., Joachimiak A., and Savchenko A. Crystal structure of glutamine amidotransferase from Thermotoga maritima. Proteins 49 (2002) 420-422
-
(2002)
Proteins
, vol.49
, pp. 420-422
-
-
Korolev, S.1
Skarina, T.2
Evdokimova, E.3
Beasley, S.4
Edwards, A.5
Joachimiak, A.6
Savchenko, A.7
-
37
-
-
23244441019
-
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
-
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
-
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
-
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
-
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
-
+ 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
-
43
-
-
13044313466
-
The structure of carbamoyl phosphate synthetase determined to 2.1 Å resolution
-
Thoden J.B., Raushel F.M., Benning M.M., Rayment I., and Holden H.M. The structure of carbamoyl phosphate synthetase determined to 2.1 Å resolution. Acta Crystallogr D Biol Crystallogr 55 Pt 1 (1999) 8-24
-
(1999)
Acta Crystallogr D Biol Crystallogr
, vol.55
, Issue.PART 1
, pp. 8-24
-
-
Thoden, J.B.1
Raushel, F.M.2
Benning, M.M.3
Rayment, I.4
Holden, H.M.5
-
44
-
-
0033534173
-
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
-
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
-
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
-
47
-
-
0037025332
-
Structural studies on the synchronization of catalytic centers in glutamate synthase
-
van den Heuvel R.H., Ferrari D., Bossi R.T., Ravasio S., Curti B., Vanoni M.A., Florencio F.J., and Mattevi A. Structural studies on the synchronization of catalytic centers in glutamate synthase. J Biol Chem 277 (2002) 24579-24583
-
(2002)
J Biol Chem
, vol.277
, pp. 24579-24583
-
-
van den Heuvel, R.H.1
Ferrari, D.2
Bossi, R.T.3
Ravasio, S.4
Curti, B.5
Vanoni, M.A.6
Florencio, F.J.7
Mattevi, A.8
-
48
-
-
0030772416
-
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
-
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
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