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Volumn 54, Issue 3, 1998, Pages 205-222

The mechanism of glutamine-dependent amidotransferases

Author keywords

Ammonia transfer; Catalytic mechanism; Glutamine dependent amidotransferase

Indexed keywords

AMIDE; AMMONIA; CYSTEINE; GLUTAMIC ACID; GLUTAMINE; HISTIDINE; NITROGEN; SERINE PROTEINASE; TRANSFERASE;

EID: 0031982179     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s000180050145     Document Type: Review
Times cited : (183)

References (93)
  • 2
    • 0026637288 scopus 로고
    • Formation of 3-amino-5-hydroxybenzoic acid, the precursor of mC7N units in ansamycin antibiotics, by a new variant of the shikimate pathway
    • Kim C. G., Kirschning A., Bergon P., Ahn Y., Wang J. J., Shibuya M. et al. (1992) Formation of 3-amino-5-hydroxybenzoic acid, the precursor of mC7N units in ansamycin antibiotics, by a new variant of the shikimate pathway. J. Am. Chem. Soc. 114: 4941-4943
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 4941-4943
    • Kim, C.G.1    Kirschning, A.2    Bergon, P.3    Ahn, Y.4    Wang, J.J.5    Shibuya, M.6
  • 5
    • 0026335088 scopus 로고
    • Mechanistic studies on Azospirillum brasilense glutamate synthase
    • Vanoni M. A., Edmonson D. E., Rescigno M., Zanetti G. and Curti B. (1991) Mechanistic studies on Azospirillum brasilense glutamate synthase. Biochemistry 30: 11478-11484
    • (1991) Biochemistry , vol.30 , pp. 11478-11484
    • Vanoni, M.A.1    Edmonson, D.E.2    Rescigno, M.3    Zanetti, G.4    Curti, B.5
  • 6
    • 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
  • 7
    • 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
  • 8
    • 0016293208 scopus 로고
    • Glutamine-binding subunit of glutamate synthase and partial reactions catalyzed by this glutamine amidotransferase
    • Trotta P. P., Platzer K. E. B., Haschemeyer R. H. and Meister A. (1974) Glutamine-binding subunit of glutamate synthase and partial reactions catalyzed by this glutamine amidotransferase. Proc. Natl. Acad. Sci. USA 71: 4607-4611
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 4607-4611
    • Trotta, P.P.1    Platzer, K.E.B.2    Haschemeyer, R.H.3    Meister, A.4
  • 9
    • 0025349212 scopus 로고
    • Purification and functional characterization of the Glu-tRNA amidotransferase from Chlamydomonas reinhardtii
    • Jahn D., Kim Y.-C., Ishino Y., Chen M.-W. and Söll D. (1990) Purification and functional characterization of the Glu-tRNA amidotransferase from Chlamydomonas reinhardtii. J. Biol. Chem. 265: 8059-8064
    • (1990) J. Biol. Chem. , vol.265 , pp. 8059-8064
    • Jahn, D.1    Kim, Y.-C.2    Ishino, Y.3    Chen, M.-W.4    Söll, D.5
  • 10
    • 0015501559 scopus 로고
    • Purification and properties of yeast nicotinamide adenine dinucleotide synthetase
    • Yi C. K. and Dietrich L. S. (1972) Purification and properties of yeast nicotinamide adenine dinucleotide synthetase. J. Biol. Chem. 247: 4794-4802
    • (1972) J. Biol. Chem. , vol.247 , pp. 4794-4802
    • Yi, C.K.1    Dietrich, L.S.2
  • 11
    • 0018786695 scopus 로고
    • Glutamine phosphoribosylpyrophosphate amidotransferase from Escherichia coli: Purification and properties
    • Messenger L. J. and Zalkin H. (1979) Glutamine phosphoribosylpyrophosphate amidotransferase from Escherichia coli: purification and properties. J. Biol. Chem. 254: 3382-3392
    • (1979) J. Biol. Chem. , vol.254 , pp. 3382-3392
    • Messenger, L.J.1    Zalkin, H.2
  • 12
    • 0024369423 scopus 로고
    • The N-terminal cysteine of human asparagine synthetase is essential for glutamine-dependent activity
    • VanHeecke G. and Schuster S. M. (1989) The N-terminal cysteine of human asparagine synthetase is essential for glutamine-dependent activity. J. Biol. Chem. 264: 19475-19477
    • (1989) J. Biol. Chem. , vol.264 , pp. 19475-19477
    • VanHeecke, G.1    Schuster, S.M.2
  • 13
    • 0001083651 scopus 로고
    • Mechanistic investigations on glucosamine-6-phosphate synthase
    • Badet-Denisot M.-A., René L. and Badet B. (1993) Mechanistic investigations on glucosamine-6-phosphate synthase. Bull. Soc. Chim. Fr. 130: 249-255
    • (1993) Bull. Soc. Chim. Fr. , vol.130 , pp. 249-255
    • Badet-Denisot, M.-A.1    René, L.2    Badet, B.3
  • 14
    • 0027787583 scopus 로고
    • Molecular and kinetic characterization of glutamate synthase from the phototrophic bacterium Rhodobacter capsulatus E1F1
    • Igeno M. I., Calballero F. J. and Castillo F. (1993) Molecular and kinetic characterization of glutamate synthase from the phototrophic bacterium Rhodobacter capsulatus E1F1. J. Gen. Microbiol. 139: 2921-2929
    • (1993) J. Gen. Microbiol. , vol.139 , pp. 2921-2929
    • Igeno, M.I.1    Calballero, F.J.2    Castillo, F.3
  • 15
    • 0016720231 scopus 로고
    • Utilization of ammonia for tryptophan synthesis
    • Zalkin H. and Murphy T. (1975) Utilization of ammonia for tryptophan synthesis. Biochem. Biophys. Res. Commun. 67: 1370-1377
    • (1975) Biochem. Biophys. Res. Commun. , vol.67 , pp. 1370-1377
    • Zalkin, H.1    Murphy, T.2
  • 16
    • 0021242389 scopus 로고
    • Nucleotide sequence of Saccharomyces cerevisiae ADE4 encoding glutamine phosphoribosylpyrophosphate amidotransferase
    • Mäntsälä P. and Zalkin H. (1984) Nucleotide sequence of Saccharomyces cerevisiae ADE4 encoding glutamine phosphoribosylpyrophosphate amidotransferase. J. Biol. Chem. 259: 8478-8484
    • (1984) J. Biol. Chem. , vol.259 , pp. 8478-8484
    • Mäntsälä, P.1    Zalkin, H.2
  • 17
    • 0023664086 scopus 로고
    • 3 by the large subunit of Escherichia coli carbamyl phosphate synthetase
    • 3 by the large subunit of Escherichia coli carbamyl phosphate synthetase. J. Biol. Chem. 262: 4382-4386
    • (1987) J. Biol. Chem. , vol.262 , pp. 4382-4386
    • Rubino, S.D.1    Nyunoya, H.2    Lusty, C.J.3
  • 18
    • 0021796440 scopus 로고
    • Purification and characterization of glutamate synthase from Azospirillum brasilense
    • Ratti S., Curti B., Zanetti G. and Galli E. (1985) Purification and characterization of glutamate synthase from Azospirillum brasilense. J. Bacteriol. 163: 724-729
    • (1985) J. Bacteriol. , vol.163 , pp. 724-729
    • Ratti, S.1    Curti, B.2    Zanetti, G.3    Galli, E.4
  • 19
    • 0027479594 scopus 로고
    • Substitution of Glu841 by lysine in the carbamate domain of carbamyl phosphate synthetase alters the catalytic properties of the glutaminase subunit
    • Lusty C. J. and Liao M. (1993) Substitution of Glu841 by lysine in the carbamate domain of carbamyl phosphate synthetase alters the catalytic properties of the glutaminase subunit. Biochemistry 32: 1278-1284
    • (1993) Biochemistry , vol.32 , pp. 1278-1284
    • Lusty, C.J.1    Liao, M.2
  • 20
    • 0025851177 scopus 로고
    • Glucosamine-6P synthase yields two proteins upon limited proteolysis: Identification of the glutamine amidohydrolase and 2R ketose aldose isomerase-bearing domains based on their biochemical properties
    • Denisot M.-A., Le Goffic F. and Badet B. (1991) Glucosamine-6P synthase yields two proteins upon limited proteolysis: identification of the glutamine amidohydrolase and 2R ketose aldose isomerase-bearing domains based on their biochemical properties. Arch. Biochem. Biophys. 288: 225-230
    • (1991) Arch. Biochem. Biophys. , vol.288 , pp. 225-230
    • Denisot, M.-A.1    Le Goffic, F.2    Badet, B.3
  • 21
    • 0023664759 scopus 로고
    • Topographical separation of the catalytic sites of asparagine synthetase explored with monoclonal antibodies
    • Pfeiffer N. E., Mehlhaff P. M., Wylie D. E. and Schuster S. M. (1987) Topographical separation of the catalytic sites of asparagine synthetase explored with monoclonal antibodies. J. Biol. Chem. 262: 11565-11570
    • (1987) J. Biol. Chem. , vol.262 , pp. 11565-11570
    • Pfeiffer, N.E.1    Mehlhaff, P.M.2    Wylie, D.E.3    Schuster, S.M.4
  • 22
    • 0029880968 scopus 로고    scopus 로고
    • Characterization of a phosphoglucose isomerase-like activity associated with the carboxy-terminal domain of E. coli glucosamine-6P synthase
    • Leriche C., Badet-Denisot M.-A. and Badet B. (1996) Characterization of a phosphoglucose isomerase-like activity associated with the carboxy-terminal domain of E. coli glucosamine-6P synthase. J. Am. Chem. Soc. 118: 1797-1798
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 1797-1798
    • Leriche, C.1    Badet-Denisot, M.-A.2    Badet, B.3
  • 24
    • 0024085772 scopus 로고
    • Evolution of aminobenzoate synthases: Nucleotide sequences of Salmonella typhimurium and Klebsiella aerogenes pabB
    • Goncharoff P. and Nichols B. P. (1988) Evolution of aminobenzoate synthases: nucleotide sequences of Salmonella typhimurium and Klebsiella aerogenes pabB. Mol. Biol. Evol. 5: 531-548
    • (1988) Mol. Biol. Evol. , vol.5 , pp. 531-548
    • Goncharoff, P.1    Nichols, B.P.2
  • 25
    • 0024279308 scopus 로고
    • Structure and function of the Salmonella typhimurium and Escherichia coli K-12 histidine operons
    • Carlomagno M. S., Chiarotti L., Alifano P., Nappo A. G. and Bruni C. B. (1988) Structure and function of the Salmonella typhimurium and Escherichia coli K-12 histidine operons. J. Mol. Biol. 203: 585-606
    • (1988) J. Mol. Biol. , vol.203 , pp. 585-606
    • Carlomagno, M.S.1    Chiarotti, L.2    Alifano, P.3    Nappo, A.G.4    Bruni, C.B.5
  • 26
    • 0024489532 scopus 로고
    • Mechanism and regulation of the glutamine-dependent carbamyl phosphate synthetase of Escherichia coli
    • Meister A. (1989) Mechanism and regulation of the glutamine-dependent carbamyl phosphate synthetase of Escherichia coli. Adv. Enzymol. Relat. Areas Mol. Biol. 62: 315-374
    • (1989) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.62 , pp. 315-374
    • Meister, A.1
  • 27
    • 0030744665 scopus 로고    scopus 로고
    • Trapping an activated conformation of mammalian carbamyl-phosphate synthetase
    • Guy H. I. and Evans D. R. (1997) Trapping an activated conformation of mammalian carbamyl-phosphate synthetase. J. Biol. Chem. 272: 19906-19912
    • (1997) J. Biol. Chem. , vol.272 , pp. 19906-19912
    • Guy, H.I.1    Evans, D.R.2
  • 28
    • 0030855178 scopus 로고    scopus 로고
    • Activation by fusion of the glutaminase and synthetase subunits of Escherichia coli carbamyl-phosphate synthetase
    • Guy H. I., Rotgeri A. and Evans D. R. (1997) Activation by fusion of the glutaminase and synthetase subunits of Escherichia coli carbamyl-phosphate synthetase. J. Biol. Chem. 272: 19913-19918
    • (1997) J. Biol. Chem. , vol.272 , pp. 19913-19918
    • Guy, H.I.1    Rotgeri, A.2    Evans, D.R.3
  • 29
    • 2642654884 scopus 로고
    • The interaction of 6-diazo-5-oxo-L-norleucine with phosphoribosyl pyrophosphate amidotransferase
    • Hartmann S. C. (1963) The interaction of 6-diazo-5-oxo-L-norleucine with phosphoribosyl pyrophosphate amidotransferase. J. Biol. Chem. 238: 3036-3047
    • (1963) J. Biol. Chem. , vol.238 , pp. 3036-3047
    • Hartmann, S.C.1
  • 30
    • 0021036536 scopus 로고
    • The glutamine-utilizing site of Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase
    • Vollmer S. J., Switzer R. L., Hermodson M. A., Bower S. G. and Zalkin H. (1983) The glutamine-utilizing site of Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase. J. Biol. Chem. 258: 10582-10585
    • (1983) J. Biol. Chem. , vol.258 , pp. 10582-10585
    • Vollmer, S.J.1    Switzer, R.L.2    Hermodson, M.A.3    Bower, S.G.4    Zalkin, H.5
  • 31
    • 0023280276 scopus 로고
    • Glucosamine synthetase from Escherichia coli: Purification, properties, and glutamine-utilizing site location
    • Badet B., Vermoote P., Haumont P.-Y., Lederer F. and Le Goffic F. (1987) Glucosamine synthetase from Escherichia coli: purification, properties, and glutamine-utilizing site location. Biochemistry 26: 1940-1948
    • (1987) Biochemistry , vol.26 , pp. 1940-1948
    • Badet, B.1    Vermoote, P.2    Haumont, P.-Y.3    Lederer, F.4    Le Goffic, F.5
  • 32
    • 0025965466 scopus 로고
    • Bovine pancreatic asparagine synthetase explored with substrate analogs and specific monoclonal antibodies
    • Mehlhaff P. M. and Schuster S. M. (1991) Bovine pancreatic asparagine synthetase explored with substrate analogs and specific monoclonal antibodies. Arch. Biochem. Biophys. 284: 143-150
    • (1991) Arch. Biochem. Biophys. , vol.284 , pp. 143-150
    • Mehlhaff, P.M.1    Schuster, S.M.2
  • 33
    • 0028287640 scopus 로고
    • The pH-dependent behaviour of catalytic activities of Azospirillum brasilense glutamate synthase and iodoacetamide modification of the enzyme provide evidence for a catalytic Cys-His ion pair
    • Vanoni M. A., Accornero P., Carrera G. and Curti B. (1994) The pH-dependent behaviour of catalytic activities of Azospirillum brasilense glutamate synthase and iodoacetamide modification of the enzyme provide evidence for a catalytic Cys-His ion pair. Arch. Biochem. Biophys. 309: 222-230
    • (1994) Arch. Biochem. Biophys. , vol.309 , pp. 222-230
    • Vanoni, M.A.1    Accornero, P.2    Carrera, G.3    Curti, B.4
  • 34
    • 0013968442 scopus 로고
    • Selective inactivation of the glutamine binding site of Escherichia coli carbamyl phosphate synthetase by 2-amino-4-oxo-5-chloropentanoic acid
    • Khedouri E., Anderson P. M. and Meister A. (1966) Selective inactivation of the glutamine binding site of Escherichia coli carbamyl phosphate synthetase by 2-amino-4-oxo-5-chloropentanoic acid. Biochemistry 5: 3552-3557
    • (1966) Biochemistry , vol.5 , pp. 3552-3557
    • Khedouri, E.1    Anderson, P.M.2    Meister, A.3
  • 35
    • 0017115904 scopus 로고
    • Glutamate synthase: Properties of the glutamine-dependent activity
    • Mäntsälä P. and Zalkin H. (1976) Glutamate synthase: properties of the glutamine-dependent activity. J. Biol. Chem. 251: 3294-3299
    • (1976) J. Biol. Chem. , vol.251 , pp. 3294-3299
    • Mäntsälä, P.1    Zalkin, H.2
  • 36
    • 0014430020 scopus 로고
    • Biosynthesis of the purines. Isolation and characterization of formylglycinamide ribonucleotide amidotransferase-glutamyl complex
    • Mizobuchi K. and Buchanan J. M. (1968) Biosynthesis of the purines. 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
  • 37
    • 0027952295 scopus 로고
    • The kinetics of azaserine and phosphinothricin inhibition of glutamate synthase cycle enzymes from barley leaves
    • Baron A., Tobin A. and Wallsgrove R. M. (1994) The kinetics of azaserine and phosphinothricin inhibition of glutamate synthase cycle enzymes from barley leaves. Plant Physiol. Biochem. 32: 555-560
    • (1994) Plant Physiol. Biochem. , vol.32 , pp. 555-560
    • Baron, A.1    Tobin, A.2    Wallsgrove, R.M.3
  • 38
    • 0018939925 scopus 로고
    • Mechanism of inactivation of glutamine amidotransferases by the antitumor drug L-(aS, 5S)-α-amino-3-chloro-4,5-dih ydro-5-isoxazolacetic acid (AT-125)
    • Tso J. Y., Bower S. G. and Zalkin H. (1980) Mechanism of inactivation of glutamine amidotransferases by the antitumor drug L-(aS, 5S)-α-amino-3-chloro-4,5-dih ydro-5-isoxazolacetic acid (AT-125). J. Biol. Chem. 255: 6734-6738
    • (1980) J. Biol. Chem. , vol.255 , pp. 6734-6738
    • Tso, J.Y.1    Bower, S.G.2    Zalkin, H.3
  • 39
    • 0025777753 scopus 로고
    • The catalytic mechanism of the amidotransferase domain of the syrian hamster multifunctional protein CAD. Evidence for a CAD-glutamyl covalent intermediate in the formation of carbamyl phosphate
    • Chaparian M. G. and Evans D. R. (1991) The catalytic mechanism of the amidotransferase domain of the syrian hamster multifunctional protein CAD. Evidence for a CAD-glutamyl covalent intermediate in the formation of carbamyl phosphate. J. Biol. Chem. 266: 3387-3395
    • (1991) J. Biol. Chem. , vol.266 , pp. 3387-3395
    • Chaparian, M.G.1    Evans, D.R.2
  • 41
    • 0019875781 scopus 로고
    • Kinetic mechanism of beef pancreatic L-asparagine synthetase
    • Markin R. S., Luehr C. A. and Schuster S. M. (1981) Kinetic mechanism of beef pancreatic L-asparagine synthetase. Biochemistry 20: 7226-7232
    • (1981) Biochemistry , vol.20 , pp. 7226-7232
    • Markin, R.S.1    Luehr, C.A.2    Schuster, S.M.3
  • 42
    • 0018236372 scopus 로고
    • Glutamate synthase: On the kinetic mechanism of the enzyme from Escherichia coli
    • Rendina A. R. and Orme-Johnson W. H. (1978) Glutamate synthase: on the kinetic mechanism of the enzyme from Escherichia coli. Biochemistry 17: 5388-5393
    • (1978) Biochemistry , vol.17 , pp. 5388-5393
    • Rendina, A.R.1    Orme-Johnson, W.H.2
  • 43
    • 0026056062 scopus 로고
    • The kinetic mechanism of the reactions catalyzed by the glutamate synthase from Azospirillum brasilense
    • Vanoni M. A., Nuzzi L., Rescigno M., Zanetti G. and Curti B. (1991) The kinetic mechanism of the reactions catalyzed by the glutamate synthase from Azospirillum brasilense. Eur. J. Biochem. 202: 181-189
    • (1991) Eur. J. Biochem. , vol.202 , pp. 181-189
    • Vanoni, M.A.1    Nuzzi, L.2    Rescigno, M.3    Zanetti, G.4    Curti, B.5
  • 44
    • 0028809784 scopus 로고
    • Kinetic characterization of 4-amino 4-deoxychorismate synthase from Escherichia coli
    • Viswanathan V. K., Green J. M. and Nichols B. P. (1995) Kinetic characterization of 4-amino 4-deoxychorismate synthase from Escherichia coli. J. Bacteriol. 177: 5918-5923
    • (1995) J. Bacteriol. , vol.177 , pp. 5918-5923
    • Viswanathan, V.K.1    Green, J.M.2    Nichols, B.P.3
  • 45
    • 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. (1996) Structure and function of the glutamine phosphoribosylpyrophosphate amidotransferase glutamine site and communication with the phosphoribosylpyrophosphate site. J. Biol. Chem. 271: 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
  • 46
    • 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 3: 6904-6910
    • (1992) Biochemistry , vol.3 , pp. 6904-6910
    • Roux, B.1    Walsh, C.T.2
  • 47
    • 0028948403 scopus 로고
    • Nitrogen transfer in E. coli glucosamine-6P synthase. Investigations using substrate and bisubstrate analogs
    • Badet-Denisot M.-A., Leriche C., Massière F. and Badet B. (1995) Nitrogen transfer in E. coli glucosamine-6P synthase. Investigations using substrate and bisubstrate analogs. Bioorg. Med. Chem. Lett. 5: 815-820
    • (1995) Bioorg. Med. Chem. Lett. , vol.5 , pp. 815-820
    • Badet-Denisot, M.-A.1    Leriche, C.2    Massière, F.3    Badet, B.4
  • 48
    • 0029166093 scopus 로고
    • A stable carbocyclic analog of 5-phosphoribosyl-l-pyrophosphate to probe the mechanism of catalysis and regulation of glutamine phosphoribosylpyrophosphate amidotransferase
    • Kim J. H., Wolle D., Haridas K., Parry R. J., Smith J. L. and Zalkin H. (1995) A stable carbocyclic analog of 5-phosphoribosyl-l-pyrophosphate to probe the mechanism of catalysis and regulation of glutamine phosphoribosylpyrophosphate amidotransferase. J. Biol. Chem. 270: 17394-17399
    • (1995) J. Biol. Chem. , vol.270 , pp. 17394-17399
    • Kim, J.H.1    Wolle, D.2    Haridas, K.3    Parry, R.J.4    Smith, J.L.5    Zalkin, H.6
  • 49
    • 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
  • 50
    • 0028266614 scopus 로고
    • A molecular wedge for triggering the amidotransferase activity of carbamoyl phosphate synthetase
    • Mareya S. M. and Raushel F. M. (1994) A molecular wedge for triggering the amidotransferase activity of carbamoyl phosphate synthetase. Biochemistry 33: 2945-2950
    • (1994) Biochemistry , vol.33 , pp. 2945-2950
    • Mareya, S.M.1    Raushel, F.M.2
  • 51
    • 0024433662 scopus 로고
    • A cysteine-histidine-aspartate catalytic triad is involved in glutamine amide transfer function in purF-type glutamine amidotransferases
    • Mei B. and Zalkin H. (1989) A cysteine-histidine-aspartate catalytic triad is involved in glutamine amide transfer function in purF-type glutamine amidotransferases. J. Biol. Chem. 264: 16613-16619
    • (1989) J. Biol. Chem. , vol.264 , pp. 16613-16619
    • Mei, B.1    Zalkin, H.2
  • 52
    • 0028828360 scopus 로고
    • Structures of glutamine amidotransferases from the purine biosynthetic pathway
    • Smith J. L. (1995) Structures of glutamine amidotransferases from the purine biosynthetic pathway. Biochem. Soc. Trans. 23: 894-898
    • (1995) Biochem. Soc. Trans. , vol.23 , pp. 894-898
    • Smith, J.L.1
  • 53
    • 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
  • 54
    • 0025858242 scopus 로고
    • Role of the four conserved histidine residues in the amidotransferase domain of carbamoyl phosphate synthetase
    • Gaillard Miran S., Chang S. H. and Raushel F. M. (1991) Role of the four conserved histidine residues in the amidotransferase domain of carbamoyl phosphate synthetase. Biochemistry 30: 7901-7907
    • (1991) Biochemistry , vol.30 , pp. 7901-7907
    • Gaillard Miran, S.1    Chang, S.H.2    Raushel, F.M.3
  • 55
    • 0027174079 scopus 로고
    • p-Aminobenzoate synthesis in Escherichia coli: Mutational analysis of three conserved amino acid residues of the amidotransferase PabA
    • Roux B. and Walsh C. T. ( 1993) p-Aminobenzoate synthesis in Escherichia coli: mutational analysis of three conserved amino acid residues of the amidotransferase PabA. Biochemistry 32: 3763-3768
    • (1993) Biochemistry , vol.32 , pp. 3763-3768
    • Roux, B.1    Walsh, C.T.2
  • 56
    • 0022343905 scopus 로고
    • Replacement by site-directed mutagenesis indicates a role for histidine 170 in the glutamine amide transfer function of anthranilate synthase
    • Amuro N., Paluh J. L. and Zalkin H. (1985) Replacement by site-directed mutagenesis indicates a role for histidine 170 in the glutamine amide transfer function of anthranilate synthase. J. Biol. Chem. 260: 14844-14849
    • (1985) J. Biol. Chem. , vol.260 , pp. 14844-14849
    • Amuro, N.1    Paluh, J.L.2    Zalkin, H.3
  • 57
    • 0029941274 scopus 로고    scopus 로고
    • A theoretical study of the active sites of papain and S195C rat trypsin: Implications for the low reactivity of mutant serine proteinases
    • Beveridge A. J. (1996) A theoretical study of the active sites of papain and S195C rat trypsin: implications for the low reactivity of mutant serine proteinases. Protein Science 5: 1355-1365
    • (1996) Protein Science , vol.5 , pp. 1355-1365
    • Beveridge, A.J.1
  • 58
    • 0028762844 scopus 로고
    • Structure of the allosteric regulatory enzyme of purine biosynthesis
    • Smith J. L., Zaluzec E. J., Wery J.-P., Niu L., Switzer R. L., Zalkin H. et al. (1994) Structure of the allosteric regulatory enzyme of purine biosynthesis. Science 264: 1427-1433
    • (1994) Science , vol.264 , pp. 1427-1433
    • Smith, J.L.1    Zaluzec, E.J.2    Wery, J.-P.3    Niu, L.4    Switzer, R.L.5    Zalkin, H.6
  • 59
    • 0030586024 scopus 로고    scopus 로고
    • Substrate binding is required for assembly of the active conformation of the catalytic site from the 1.8 Å crystal structure of the glutaminase domain of glucosamine-6P synthase
    • Isupov M. N., Obmolova G., Butterworth S., Badet-Denisot M.-A., Badet B., Polikarpov I. et al. (1996) Substrate binding is required for assembly of the active conformation of the catalytic site from the 1.8 Å crystal structure of the glutaminase domain of glucosamine-6P synthase. Structure 4: 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
  • 60
    • 0026501816 scopus 로고
    • Chemical modification of glucosamine-6-phosphate synthase by diethyl pyrocarbonate: Evidence of histidine requirement for enzymatic activity
    • Badet-Denisot M.-A. and Badet B. (1992) Chemical modification of glucosamine-6-phosphate synthase by diethyl pyrocarbonate: evidence of histidine requirement for enzymatic activity. Arch. Biochem. Biophys. 292: 475-478
    • (1992) Arch. Biochem. Biophys. , vol.292 , pp. 475-478
    • Badet-Denisot, M.-A.1    Badet, B.2
  • 61
    • 0027412184 scopus 로고
    • Glutamate synthase genes of the diazotroph Azospirillum brasilense: Cloning, sequencing and analysis of functional domains
    • Pelanda R., Vanoni M. A., Perego M., Piubelli L., Galizzi A., Curti B. et al. (1993) Glutamate synthase genes of the diazotroph Azospirillum brasilense: cloning, sequencing and analysis of functional domains. J. Biol. Chem. 268: 3099-3106
    • (1993) J. Biol. Chem. , vol.268 , pp. 3099-3106
    • Pelanda, R.1    Vanoni, M.A.2    Perego, M.3    Piubelli, L.4    Galizzi, A.5    Curti, B.6
  • 62
    • 0028972449 scopus 로고
    • A protein catalytic framework with an N-terminal nucleophile is capable of self-activation
    • Brannigan J. A., Dodson G., Duggleby H. J., Moody P. C. E., Smith J. L., Tomchick D. R. et al. (1995) A protein catalytic framework with an N-terminal nucleophile is capable of self-activation. Nature 378: 416-419
    • (1995) Nature , vol.378 , pp. 416-419
    • Brannigan, J.A.1    Dodson, G.2    Duggleby, H.J.3    Moody, P.C.E.4    Smith, J.L.5    Tomchick, D.R.6
  • 63
    • 0029590248 scopus 로고
    • Engineering nitrile hydratase activity into a cysteine protease by a single mutation
    • Dufour E., Storer A. C. and Menard R. (1995) Engineering nitrile hydratase activity into a cysteine protease by a single mutation. Biochemistry 34: 16382-16388
    • (1995) Biochemistry , vol.34 , pp. 16382-16388
    • Dufour, E.1    Storer, A.C.2    Menard, R.3
  • 65
    • 0027941103 scopus 로고
    • A new family of carbon-nitrogen hydrolase
    • Bork P. and Koonin E. V. (1994) A new family of carbon-nitrogen hydrolase. Protein Sci. 3: 1344-1346
    • (1994) Protein Sci. , vol.3 , pp. 1344-1346
    • Bork, P.1    Koonin, E.V.2
  • 66
    • 0030849770 scopus 로고    scopus 로고
    • Catalytic activity of the N-terminal domain of E. coli asparagine synthetase B can be reengineered by single point mutation
    • Boehlein S. K., Rosa-Rodriguez J. C., Schuster S. M. and Richards N. G. J. (1997) Catalytic activity of the N-terminal domain of E. coli asparagine synthetase B can be reengineered by single point mutation. J. Am. Chem. Soc. 119: 5785-5791
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 5785-5791
    • Boehlein, S.K.1    Rosa-Rodriguez, J.C.2    Schuster, S.M.3    Richards, N.G.J.4
  • 67
    • 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. G., Klem T. J., Deras M. L., Davisson V. J. and Smith J. L. (1996) The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families. Nat. Struct. Biol. 3: 74-86
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 74-86
    • Tesmer, J.J.G.1    Klem, T.J.2    Deras, M.L.3    Davisson, V.J.4    Smith, J.L.5
  • 68
    • 0028980589 scopus 로고
    • Glutamate g-semialdehyde as a natural transition state analogue inhibitor of Escherichia coli glucosamine-6-phosphate synthase
    • Bearne S. L. and Wolfenden R. (1995) Glutamate g-semialdehyde as a natural transition state analogue inhibitor of Escherichia coli glucosamine-6-phosphate synthase. Biochemistry 34: 11515-11520
    • (1995) Biochemistry , vol.34 , pp. 11515-11520
    • Bearne, S.L.1    Wolfenden, R.2
  • 69
    • 0015247088 scopus 로고
    • Cytidine triphosphate synthetase. Covalent intermediates and mechanism of action
    • Levitzki A. and Koshland D. E. Jr (1971) Cytidine triphosphate synthetase. Covalent intermediates and mechanism of action. Biochemistry 10: 3365-3371
    • (1971) Biochemistry , vol.10 , pp. 3365-3371
    • Levitzki, A.1    Koshland Jr., D.E.2
  • 71
    • 0015932719 scopus 로고
    • Interaction of Escherichia coli carbamyl phosphate synthetase with glutamine
    • Wellner V. P., Anderson P. M. and Meister A. (1973) Interaction of Escherichia coli carbamyl phosphate synthetase with glutamine. Biochemistry 12: 2061-2066
    • (1973) Biochemistry , vol.12 , pp. 2061-2066
    • Wellner, V.P.1    Anderson, P.M.2    Meister, A.3
  • 72
    • 0026443991 scopus 로고
    • Detection of an enzyme-bound γ-glutamyl acyl ester of carbamyl phosphate synthetase of Escherichia coli
    • Lusty C. J. (1992) Detection of an enzyme-bound γ-glutamyl acyl ester of carbamyl phosphate synthetase of Escherichia coli. FEBS Lett. 314: 135-138
    • (1992) FEBS Lett. , vol.314 , pp. 135-138
    • Lusty, C.J.1
  • 73
    • 0017403064 scopus 로고
    • Characterization of the glutamine site of Escherichia coli guanosine 5′-monophosphate synthetase
    • Zalkin H. and Truitt C. D. (1977) Characterization of the glutamine site of Escherichia coli guanosine 5′-monophosphate synthetase. J. Biol. Chem. 252: 5431-5436
    • (1977) J. Biol. Chem. , vol.252 , pp. 5431-5436
    • Zalkin, H.1    Truitt, C.D.2
  • 74
    • 0030041610 scopus 로고    scopus 로고
    • Active site-directed inactivation of E. coli glucosamine-6P synthase
    • Bearne S. L. (1996) Active site-directed inactivation of E. coli glucosamine-6P synthase. J. Biol. Chem. 271: 3052-3057
    • (1996) J. Biol. Chem. , vol.271 , pp. 3052-3057
    • Bearne, S.L.1
  • 75
    • 0030948176 scopus 로고    scopus 로고
    • Affinity labeling of E. coli glucosamine-6P synthase with a fructose-6P analog
    • Leriche C., Badet-Denisot M.-A. and Badet B. (1997) Affinity labeling of E. coli glucosamine-6P synthase with a fructose-6P analog. Eur. J. Biochem. 245: 418-422
    • (1997) Eur. J. Biochem. , vol.245 , pp. 418-422
    • Leriche, C.1    Badet-Denisot, M.-A.2    Badet, B.3
  • 76
    • 0001523706 scopus 로고
    • A mechanistic proposal for asparagine-linked glycosylation
    • Imperiali B., Shannon K. L., Unno M. and Rickert K. W. (1992) A mechanistic proposal for asparagine-linked glycosylation. J. Am. Chem. Soc. 114: 7944-7945
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 7944-7945
    • Imperiali, B.1    Shannon, K.L.2    Unno, M.3    Rickert, K.W.4
  • 77
    • 0026468562 scopus 로고
    • An alternative mechanism for the nitrogen transfer reaction in asparagine synthetase
    • Richards N. G. J. and Schuster S. M. (1992) An alternative mechanism for the nitrogen transfer reaction in asparagine synthetase. FEBS Lett. 313: 98-102
    • (1992) FEBS Lett. , vol.313 , pp. 98-102
    • Richards, N.G.J.1    Schuster, S.M.2
  • 78
    • 0029670135 scopus 로고    scopus 로고
    • Glutamic acid γg-monohydroxamate and hydroxylamine are alternate substrates for E. coli asparagine synthetase B
    • Boehlein S. K., Schuster S. M. and Richards N. G. J. (1996) Glutamic acid γg-monohydroxamate and hydroxylamine are alternate substrates for E. coli asparagine synthetase B. Biochemistry 35: 3031-3037
    • (1996) Biochemistry , vol.35 , pp. 3031-3037
    • Boehlein, S.K.1    Schuster, S.M.2    Richards, N.G.J.3
  • 79
    • 85023128997 scopus 로고
    • An improved synthesis of symetrical N,N′-alkylidene bis-amides
    • Gilbert E. E. (1972) An improved synthesis of symetrical N,N′-alkylidene bis-amides. Synthesis 30-32
    • (1972) Synthesis , pp. 30-32
    • Gilbert, E.E.1
  • 80
    • 0001644801 scopus 로고
    • N-benzoylbenzaldimines and N-α-alkoxybenzylbenzamides
    • Breuer S. W., Bernath T. and Ben-Ishai D. (1967) N-benzoylbenzaldimines and N-α-alkoxybenzylbenzamides. Tetrahedron 23: 2869-2877
    • (1967) Tetrahedron , vol.23 , pp. 2869-2877
    • Breuer, S.W.1    Bernath, T.2    Ben-Ishai, D.3
  • 81
    • 84986674101 scopus 로고
    • Synthesis of 1-aminoalkylphosphonic acids via amidoalkylation of phosphorous acid by N,N′alkylidene bis-amides
    • Soroka M., Jaworska D. and Szezesny (1990) Synthesis of 1-aminoalkylphosphonic acids via amidoalkylation of phosphorous acid by N,N′alkylidene bis-amides. Liebigs Ann. Chem. 11: 1153-1155
    • (1990) Liebigs Ann. Chem. , vol.11 , pp. 1153-1155
    • Soroka, M.1    Jaworska, D.2    Szezesny3
  • 82
    • 0028593789 scopus 로고
    • Synthesis of N-[1-(imidazol-1-yl)alkyl]amides
    • Pernak J., Mrowczynski B. and Weglewski J. (1994) Synthesis of N-[1-(imidazol-1-yl)alkyl]amides. Synthesis 1415-1417
    • (1994) Synthesis , pp. 1415-1417
    • Pernak, J.1    Mrowczynski, B.2    Weglewski, J.3
  • 83
    • 0029865432 scopus 로고    scopus 로고
    • Probing the mechanism of nitrogen transfer in E. coli asparagine synthetase by using heavy atom isotope effects
    • Stoker P. W., O'Leary M. H., Boehlein S. K., Schuster S. M. and Richards N. G. J. (1996) Probing the mechanism of nitrogen transfer in E. coli asparagine synthetase by using heavy atom isotope effects. Biochemistry 35: 3024-3040
    • (1996) Biochemistry , vol.35 , pp. 3024-3040
    • Stoker, P.W.1    O'Leary, M.H.2    Boehlein, S.K.3    Schuster, S.M.4    Richards, N.G.J.5
  • 84
    • 0002416605 scopus 로고
    • The chemistry of thioamides
    • Zabicky J. (ed.). Wiley Interscience. London
    • Walter W. and Voss J. (1970) The chemistry of thioamides. In: The chemistry of amides. Zabicky J. (ed.). Wiley Interscience. London
    • (1970) The Chemistry of Amides
    • Walter, W.1    Voss, J.2
  • 85
    • 0031028212 scopus 로고    scopus 로고
    • Protein structure, dynamics and allostery in tryptophan synthase channeling
    • Pan P., Woehl E. and Dunn M. F. (1997) Protein structure, dynamics and allostery in tryptophan synthase channeling. TIBS 22: 22-27
    • (1997) TIBS , vol.22 , pp. 22-27
    • Pan, P.1    Woehl, E.2    Dunn, M.F.3
  • 86
    • 0027168789 scopus 로고
    • Substrate-induced actuation of dienelactone hydrolase: An enzyme with a naturally occuring Cys-His-Asp triad
    • Cheah E., Austin C., Ashley G. W. and Ollis D. (1993) Substrate-induced actuation of dienelactone hydrolase: an enzyme with a naturally occuring Cys-His-Asp triad. Protein Eng. 6: 575-583
    • (1993) Protein Eng. , vol.6 , pp. 575-583
    • Cheah, E.1    Austin, C.2    Ashley, G.W.3    Ollis, D.4
  • 87
    • 0028786346 scopus 로고
    • Three-dimensional structure of human lysosomal aspartylglucosaminidase
    • Oinonen C., Tikkanen R., Rouvinen J. and Peltonen L. (1995) Three-dimensional structure of human lysosomal aspartylglucosaminidase. Nature Struct. Biol. 2: 1102-1108
    • (1995) Nature Struct. Biol. , vol.2 , pp. 1102-1108
    • Oinonen, C.1    Tikkanen, R.2    Rouvinen, J.3    Peltonen, L.4
  • 88
    • 0029042511 scopus 로고
    • Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 Å resolution
    • Löwe J., Stock D., Jap B., Zwickl P., Baumeister W. and Huber R. (1995) Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 Å resolution. Science 268: 533-539
    • (1995) Science , vol.268 , pp. 533-539
    • Löwe, J.1    Stock, D.2    Jap, B.3    Zwickl, P.4    Baumeister, W.5    Huber, R.6
  • 90
    • 0029560755 scopus 로고
    • Enzymes of nucleotide synthesis
    • Smith J. L. (1995) Enzymes of nucleotide synthesis. Curr. Opin. Struct. Biol. 5: 752-757
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 752-757
    • Smith, J.L.1
  • 91
    • 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. (1997) Coupled formation of an amidotransferase interdomain 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
  • 92


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