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Volumn 1388, Issue 2, 1998, Pages 489-499

The function of Glu338 in the catalytic triad of the carbamoyl phosphate synthetase amidotransferase domain

Author keywords

Amidotransferase; Carbamoyl phosphate synthetase; Catalytic triad; Glutaminase; Multifunctional protein CAD; Pyrimidine biosynthesis

Indexed keywords

CARBAMOYL PHOSPHATE SYNTHASE; GLUTAMIC ACID; GLYCINE; HISTIDINE; AMMONIA; GLUTAMINASE; GLUTAMINE; HYBRID PROTEIN;

EID: 0032505925     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(98)00212-X     Document Type: Article
Times cited : (13)

References (55)
  • 1
    • 0015233939 scopus 로고
    • Copurification of carbamyl phosphate synthetase and aspartate transcarbamylase from mouse spleen
    • Hoogenraad N., Levine R., Kretchmer N. Copurification of carbamyl phosphate synthetase and aspartate transcarbamylase from mouse spleen. Biochem. Biophys. Res. Commun. 44:1971;981-988.
    • (1971) Biochem. Biophys. Res. Commun. , vol.44 , pp. 981-988
    • Hoogenraad, N.1    Levine, R.2    Kretchmer, N.3
  • 2
    • 0015212198 scopus 로고
    • Initial steps in pyrimidine synthesis in Ehrlich ascites carcinoma
    • Shoaf W., Jones M. Initial steps in pyrimidine synthesis in Ehrlich ascites carcinoma. Biochem. Biophys. Res. Commun. 45:1971;796-802.
    • (1971) Biochem. Biophys. Res. Commun. , vol.45 , pp. 796-802
    • Shoaf, W.1    Jones, M.2
  • 3
    • 0015895748 scopus 로고
    • Uridylic acid synthesis in Ehrlich ascites carcinoma: Properties of the multienzyme complex catalyzing the initial steps of pyrimidine biosynthesis in rat liver
    • Shoaf W.T., Jones M.E. Uridylic acid synthesis in Ehrlich ascites carcinoma: properties of the multienzyme complex catalyzing the initial steps of pyrimidine biosynthesis in rat liver. Biochemistry. 12:1973;4039-4051.
    • (1973) Biochemistry , vol.12 , pp. 4039-4051
    • Shoaf, W.T.1    Jones, M.E.2
  • 4
    • 0016782393 scopus 로고
    • Aggregation states and catalytic properties of the multienzyme complex catalyzing the initial steps of pyrimidine biosynthesis in rat liver
    • Mori M., Ishida H., Tatibana M. Aggregation states and catalytic properties of the multienzyme complex catalyzing the initial steps of pyrimidine biosynthesis in rat liver. Biochemistry. 14:1975;2622-2630.
    • (1975) Biochemistry , vol.14 , pp. 2622-2630
    • Mori, M.1    Ishida, H.2    Tatibana, M.3
  • 5
    • 0017739096 scopus 로고
    • Purification from hamster cells of the multifunctional protein that initiates de novo synthesis of pyrimidine nucleotides
    • Coleman P., Suttle D., Stark G. Purification from hamster cells of the multifunctional protein that initiates de novo synthesis of pyrimidine nucleotides. J. Biol. Chem. 252:1977;6379-6385.
    • (1977) J. Biol. Chem. , vol.252 , pp. 6379-6385
    • Coleman, P.1    Suttle, D.2    Stark, G.3
  • 6
    • 1842841202 scopus 로고
    • Controlled proteolysis of the multifunctional protein that initiates pyrimidine biosynthesis in mammalian cells: Evidence for discrete structural domains
    • Mally M.I., Grayson D.R., Evans D.R. Controlled proteolysis of the multifunctional protein that initiates pyrimidine biosynthesis in mammalian cells: evidence for discrete structural domains. Proc. Natl. Acad. Sci. USA. 78:1981;6647-6651.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 6647-6651
    • Mally, M.I.1    Grayson, D.R.2    Evans, D.R.3
  • 7
    • 0019888069 scopus 로고
    • Organization of a multifunctional protein in pyrimidine biosynthesis. Analyses of active, tryptic fragments
    • Davidson J.N., Rumsby P.C., Tamaren J. Organization of a multifunctional protein in pyrimidine biosynthesis. Analyses of active, tryptic fragments. J. Biol. Chem. 256:1981;5220-5225.
    • (1981) J. Biol. Chem. , vol.256 , pp. 5220-5225
    • Davidson, J.N.1    Rumsby, P.C.2    Tamaren, J.3
  • 8
    • 0021099393 scopus 로고
    • The isolation and characterization of the aspartate transcarbamylase domain of the multifunctional protein CAD
    • Grayson D.R., Evans D.R. The isolation and characterization of the aspartate transcarbamylase domain of the multifunctional protein CAD. J. Biol. Chem. 258:1983;4123-4129.
    • (1983) J. Biol. Chem. , vol.258 , pp. 4123-4129
    • Grayson, D.R.1    Evans, D.R.2
  • 9
    • 0022381631 scopus 로고
    • Immunochemical analysis of the domain structure of CAD, the multifunctional protein that initiates pyrimidine biosynthesis in mammalian cells
    • Grayson D.R., Lee L., Evans D.R. Immunochemical analysis of the domain structure of CAD, the multifunctional protein that initiates pyrimidine biosynthesis in mammalian cells. J. Biol. Chem. 260:1985;15840-15849.
    • (1985) J. Biol. Chem. , vol.260 , pp. 15840-15849
    • Grayson, D.R.1    Lee, L.2    Evans, D.R.3
  • 10
    • 0023042261 scopus 로고
    • The dihydroorotase domain of the multifunctional protein CAD. Subunit structure, zinc content, and kinetics
    • Kelly R.E., Mally M.I., Evans D.R. The dihydroorotase domain of the multifunctional protein CAD. Subunit structure, zinc content, and kinetics. J. Biol. Chem. 261:1986;6073-6083.
    • (1986) J. Biol. Chem. , vol.261 , pp. 6073-6083
    • Kelly, R.E.1    Mally, M.I.2    Evans, D.R.3
  • 11
    • 0026703031 scopus 로고
    • The structural organization of the hamster multifunctional protein CAD. Controlled proteolysis, domains, and linkers
    • Kim H., Kelly R.E., Evans D.R. The structural organization of the hamster multifunctional protein CAD. Controlled proteolysis, domains, and linkers. J. Biol. Chem. 267:1992;7177-7184.
    • (1992) J. Biol. Chem. , vol.267 , pp. 7177-7184
    • Kim, H.1    Kelly, R.E.2    Evans, D.R.3
  • 12
    • 0028278175 scopus 로고
    • Cloning, expression, and functional interactions of the amidotransferase domain of mammalian CAD carbamyl phosphate synthetase
    • Guy H.I., Evans D.R. Cloning, expression, and functional interactions of the amidotransferase domain of mammalian CAD carbamyl phosphate synthetase. J. Biol. Chem. 269:1994;7702-7708.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7702-7708
    • Guy, H.I.1    Evans, D.R.2
  • 13
    • 0021175813 scopus 로고
    • Sequence of the small subunit of yeast carbamyl phosphate synthetase and identification of its catalytic domain
    • Nyunoya H., Lusty C.J. Sequence of the small subunit of yeast carbamyl phosphate synthetase and identification of its catalytic domain. J. Biol. Chem. 259:1984;9790-9798.
    • (1984) J. Biol. Chem. , vol.259 , pp. 9790-9798
    • Nyunoya, H.1    Lusty, C.J.2
  • 14
    • 0021798245 scopus 로고
    • Evolution of glutamine amidotransferase genes. nucleotide sequences of the pabA genes from Salmonella typhimurium, Klebsiella aerogenes and Serratia marcescens
    • Kaplan J., Merkel W., Nichols B. Evolution of glutamine amidotransferase genes. nucleotide sequences of the pabA genes from Salmonella typhimurium, Klebsiella aerogenes and Serratia marcescens. J. Mol. Biol. 183:1985;327-340.
    • (1985) J. Mol. Biol. , vol.183 , pp. 327-340
    • Kaplan, J.1    Merkel, W.2    Nichols, B.3
  • 15
    • 0025367324 scopus 로고
    • Mammalian carbamyl phosphate synthetase (CPS). DNA sequence and evolution of the CPS domain of the Syrian hamster multifunctional protein CAD
    • Simmer J.P., Kelly R.E., Rinker A.G. Jr., Scully J.L., Evans D.R. Mammalian carbamyl phosphate synthetase (CPS). DNA sequence and evolution of the CPS domain of the Syrian hamster multifunctional protein CAD. J. Biol. Chem. 265:1990;10395-10402.
    • (1990) J. Biol. Chem. , vol.265 , pp. 10395-10402
    • Simmer, J.P.1    Kelly, R.E.2    Rinker A.G., Jr.3    Scully, J.L.4    Evans, D.R.5
  • 16
    • 0025753826 scopus 로고
    • Molecular cloning of a cDNA encoding the amino end of the mammalian multifunctional protein CAD and analysis of the 5′-flanking region of the CAD gene
    • Bein K., Simmer J., Evans D. Molecular cloning of a cDNA encoding the amino end of the mammalian multifunctional protein CAD and analysis of the 5′-flanking region of the CAD gene. J. Biol. Chem. 266:1991;3791-3799.
    • (1991) J. Biol. Chem. , vol.266 , pp. 3791-3799
    • Bein, K.1    Simmer, J.2    Evans, D.3
  • 17
    • 0028950283 scopus 로고
    • Substructure of the amidotransferase domain of mammalian carbamyl phosphate synthetase
    • Guy H.I., Evans D.R. Substructure of the amidotransferase domain of mammalian carbamyl phosphate synthetase. J. Biol. Chem. 270:1995;2190-2197.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2190-2197
    • Guy, H.I.1    Evans, D.R.2
  • 18
    • 0022272452 scopus 로고
    • Glutamine amidotransferases
    • Zalkin H. Glutamine amidotransferases. Methods Enzymol. 113:1985;263-264.
    • (1985) Methods Enzymol. , vol.113 , pp. 263-264
    • Zalkin, H.1
  • 19
    • 0021911947 scopus 로고
    • Identification of a trpG-related glutamine amide transfer domain in Escherichia coli GMP synthetase
    • Zalkin H., Argos P., Narayana S.V., Tiedeman A.A., Smith J.M. Identification of a trpG-related glutamine amide transfer domain in Escherichia coli GMP synthetase. J. Biol. Chem. 260:1985;3350-3354.
    • (1985) J. Biol. Chem. , vol.260 , pp. 3350-3354
    • Zalkin, H.1    Argos, P.2    Narayana, S.V.3    Tiedeman, A.A.4    Smith, J.M.5
  • 20
    • 0015501734 scopus 로고
    • Identification of a reactive cysteine residue at the glutamine binding site of carbamyl phosphate synthetase
    • Pinkus L.M., Meister A. Identification of a reactive cysteine residue at the glutamine binding site of carbamyl phosphate synthetase. J. Biol. Chem. 247:1972;6119-6127.
    • (1972) J. Biol. Chem. , vol.247 , pp. 6119-6127
    • Pinkus, L.M.1    Meister, A.2
  • 21
    • 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., Meister A. Selective inactivation of the glutamine binding site of Escherichia coli carbamyl phosphate synthetase by 2-amino-4-oxo-5-chloropentanoic acid. Biochemistry. 5:1966;3552-3557.
    • (1966) Biochemistry , vol.5 , pp. 3552-3557
    • Khedouri, E.1    Anderson, P.M.2    Meister, A.3
  • 22
    • 0021962151 scopus 로고
    • Study of anthranilate synthase function by replacement of cysteine 84 using site-directed mutagenesis
    • Paluh J.L., Zalkin H., Betsch D., Weith H.L. Study of anthranilate synthase function by replacement of cysteine 84 using site-directed mutagenesis. J. Biol. Chem. 260:1985;1889-1894.
    • (1985) J. Biol. Chem. , vol.260 , pp. 1889-1894
    • Paluh, J.L.1    Zalkin, H.2    Betsch, D.3    Weith, H.L.4
  • 23
    • 0024489532 scopus 로고
    • Mechanism and regulation of the glutamine-dependent carbamyl phosphate synthetase of Escherichia coli
    • Meister A. Mechanism and regulation of the glutamine-dependent carbamyl phosphate synthetase of Escherichia coli. Adv. Enzymol. Relat. Areas Mol. Biol. 62:1989;315-374.
    • (1989) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.62 , pp. 315-374
    • Meister, A.1
  • 24
    • 0022977619 scopus 로고
    • Catalytic domains of carbamyl phosphate synthetase. Glutamine-hydrolyzing site of Escherichia coli carbamyl phosphate synthetase
    • Rubino S.D., Nyunoya H., Lusty C.J. Catalytic domains of carbamyl phosphate synthetase. Glutamine-hydrolyzing site of Escherichia coli carbamyl phosphate synthetase. J. Biol. Chem. 261:1986;11320-11327.
    • (1986) J. Biol. Chem. , vol.261 , pp. 11320-11327
    • Rubino, S.D.1    Nyunoya, H.2    Lusty, C.J.3
  • 25
    • 0025896093 scopus 로고
    • Alterations in the energetics of the carbamoyl phosphate synthetase reaction by site-directed modification of the essential sulfhydryl group
    • Mullins L.S., Lusty C.J., Raushel F.M. Alterations in the energetics of the carbamoyl phosphate synthetase reaction by site-directed modification of the essential sulfhydryl group. J. Biol. Chem. 266:1991;8236-8240.
    • (1991) J. Biol. Chem. , vol.266 , pp. 8236-8240
    • Mullins, L.S.1    Lusty, C.J.2    Raushel, F.M.3
  • 26
    • 0015932719 scopus 로고
    • Interaction of Escherichia coli carbamyl phosphate synthetase with glutamine
    • Wellner V.P., Anderson P.M., Meister A. Interaction of Escherichia coli carbamyl phosphate synthetase with glutamine. Biochemistry. 12:1973;2061-2066.
    • (1973) Biochemistry , vol.12 , pp. 2061-2066
    • Wellner, V.P.1    Anderson, P.M.2    Meister, A.3
  • 27
    • 0026505954 scopus 로고
    • Mutational analysis of carbamyl phosphate synthetase. Substitution of Glu841 leads to loss of functional coupling between the two catalytic domains of the synthetase subunit
    • Guillou F., Liao M., Garcia-Espana A., Lusty C.J. Mutational analysis of carbamyl phosphate synthetase. Substitution of Glu841 leads to loss of functional coupling between the two catalytic domains of the synthetase subunit. Biochemistry. 31:1992;1656-1664.
    • (1992) Biochemistry , vol.31 , pp. 1656-1664
    • Guillou, F.1    Liao, M.2    Garcia-Espana, A.3    Lusty, C.J.4
  • 28
    • 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., Evans D.R. 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. 266:1991;3387-3395.
    • (1991) J. Biol. Chem. , vol.266 , pp. 3387-3395
    • Chaparian, M.G.1    Evans, D.R.2
  • 29
    • 0026443991 scopus 로고
    • Detection of an enzyme bound gamma-glutamyl acyl ester of carbamyl phosphate synthetase of Escherichia coli
    • Lusty C.J. Detection of an enzyme bound gamma-glutamyl acyl ester of carbamyl phosphate synthetase of Escherichia coli. FEBS Lett. 314:1992;135-138.
    • (1992) FEBS Lett. , vol.314 , pp. 135-138
    • Lusty, C.J.1
  • 30
    • 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., Zalkin H. Replacement by site-directed mutagenesis indicates a role for histidine 170 in the glutamine amide transfer function of anthranilate synthase. J. Biol. Chem. 260:1985;14844-14849.
    • (1985) J. Biol. Chem. , vol.260 , pp. 14844-14849
    • Amuro, N.1    Paluh, J.L.2    Zalkin, H.3
  • 31
    • 0025858242 scopus 로고
    • Role of the four conserved histidine residues in the amidotransferase domain of carbamoyl phosphate synthetase
    • Miran S.G., Chang S.H., Raushel F.M. Role of the four conserved histidine residues in the amidotransferase domain of carbamoyl phosphate synthetase. Biochemistry. 30:1991;7901-7907.
    • (1991) Biochemistry , vol.30 , pp. 7901-7907
    • Miran, S.G.1    Chang, S.H.2    Raushel, F.M.3
  • 32
    • 0024433662 scopus 로고
    • A cysteine-histidine-aspartate catalytic triad is involved in glutamine amide transfer function in purF-type glutamine amidotransferases
    • Mei B., Zalkin H. A cysteine-histidine-aspartate catalytic triad is involved in glutamine amide transfer function in purF-type glutamine amidotransferases. J. Biol. Chem. 264:1989;16613-16619.
    • (1989) J. Biol. Chem. , vol.264 , pp. 16613-16619
    • Mei, B.1    Zalkin, H.2
  • 33
    • 0027538266 scopus 로고
    • Overview of multienzyme systems in biosynthetic pathways
    • Zalkin H. Overview of multienzyme systems in biosynthetic pathways. Biochem. Soc. Trans. 21:1993;203-207.
    • (1993) Biochem. Soc. Trans. , vol.21 , pp. 203-207
    • Zalkin, H.1
  • 35
    • 84977303841 scopus 로고
    • The geometry of the reactive site and of the peptide groups in trypsin, trypsinogen and its complexes with inhibitors
    • Marquart M., Walter J., Deisenhofer J., Bode W., Huber R. The geometry of the reactive site and of the peptide groups in trypsin, trypsinogen and its complexes with inhibitors. Acta Crystallogr. B39:1983;480-490h.
    • (1983) Acta Crystallogr. , vol.39 , pp. 480-490h
    • Marquart, M.1    Walter, J.2    Deisenhofer, J.3    Bode, W.4    Huber, R.5
  • 36
    • 0027933713 scopus 로고
    • Structure of the complex of L-benzylsuccinate with wheat serine carboxypeptidase II at 2.0-Å resolution
    • Bullock T., Branchad B., Remington S. Structure of the complex of L-benzylsuccinate with wheat serine carboxypeptidase II at 2.0-Å resolution. Biochemistry. 33:1994;11127-11134.
    • (1994) Biochemistry , vol.33 , pp. 11127-11134
    • Bullock, T.1    Branchad, B.2    Remington, S.3
  • 37
    • 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., Klem T., Deras M., Davisson V., Smith J. 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.1    Klem, T.2    Deras, M.3    Davisson, V.4    Smith, J.5
  • 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., 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
  • 40
    • 0022382162 scopus 로고
    • Superproduction and rapid purification of Escherichia coli aspartate transcarbamylase and its catalytic subunit under extreme derepression of the pyrimidine pathway
    • Nowlan S.F., Kantrowitz E.R. Superproduction and rapid purification of Escherichia coli aspartate transcarbamylase and its catalytic subunit under extreme derepression of the pyrimidine pathway. J. Biol. Chem. 260:1985;14712-14716.
    • (1985) J. Biol. Chem. , vol.260 , pp. 14712-14716
    • Nowlan, S.F.1    Kantrowitz, E.R.2
  • 41
    • 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. 262:1987;4382-4386.
    • (1987) J. Biol. Chem. , vol.262 , pp. 4382-4386
    • Rubino, S.D.1    Nyunoya, H.2    Lusty, C.J.3
  • 42
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel T.A., Roberts J.D., Zakour R.A. Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol. 154:1987;367-382.
    • (1987) Methods Enzymol. , vol.154 , pp. 367-382
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.A.3
  • 44
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 45
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.1
  • 46
    • 0019321916 scopus 로고
    • Catalytic synergy in the multifunctional protein that initiates pyrimidine biosynthesis in Syrian hamster cells
    • Mally M.I., Grayson D.R., Evans D.R. Catalytic synergy in the multifunctional protein that initiates pyrimidine biosynthesis in Syrian hamster cells. J. Biol. Chem. 255:1980;11372-11380.
    • (1980) J. Biol. Chem. , vol.255 , pp. 11372-11380
    • Mally, M.I.1    Grayson, D.R.2    Evans, D.R.3
  • 47
    • 0001038349 scopus 로고
    • The separation of pre-column o-phthalaldehyde derivatized amino acids by high performance liquid chromatography
    • Hodgin J.C. The separation of pre-column o-phthalaldehyde derivatized amino acids by high performance liquid chromatography. J. Liq. Chromatogr. 2:1979;1047-1059.
    • (1979) J. Liq. Chromatogr. , vol.2 , pp. 1047-1059
    • Hodgin, J.C.1
  • 48
    • 0018128935 scopus 로고
    • A new and specific assay for ammonia and glutamine sensitive to 100 pmol
    • Kalb V. Jr., Donohue T., Corrigan M., Bernlohr R. A new and specific assay for ammonia and glutamine sensitive to 100 pmol. Anal. Biochem. 90:1978;47-57.
    • (1978) Anal. Biochem. , vol.90 , pp. 47-57
    • Kalb V., Jr.1    Donohue, T.2    Corrigan, M.3    Bernlohr, R.4
  • 50
    • 0003565404 scopus 로고
    • Halsted Press, a Division of John Wiley and Sons, New York
    • K. Hiromi, Kinetics of Fast Enzyme Reactions, Halsted Press, a Division of John Wiley and Sons, New York, 1979, pp. 226-230.
    • (1979) Kinetics of Fast Enzyme Reactions , pp. 226-230
    • Hiromi, K.1
  • 51
    • 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., Liao M. Substitution of Glu841 by lysine in the carbamate domain of carbamyl phosphate synthetase alters the catalytic properties of the glutaminase subunit. Biochemistry. 32:1993;1278-1284.
    • (1993) Biochemistry , vol.32 , pp. 1278-1284
    • Lusty, C.J.1    Liao, M.2
  • 52
    • 0031554904 scopus 로고    scopus 로고
    • Crystal structure of the wild-type human procathepsin B at 2.5 Å resolution reveals the native active site of a papain-like cysteine protease zymogen
    • Podobnik M., Kuhelj R., Turk V., Turk D. Crystal structure of the wild-type human procathepsin B at 2.5 Å resolution reveals the native active site of a papain-like cysteine protease zymogen. J. Mol. Biol. 27:1997;774-788.
    • (1997) J. Mol. Biol. , vol.27 , pp. 774-788
    • Podobnik, M.1    Kuhelj, R.2    Turk, V.3    Turk, D.4
  • 53
    • 0027931861 scopus 로고
    • Cloning and expression of the mammalian multifunctional protein CAD in Escherichia coli. Characterization of the recombinant protein and a deletion mutant lacking the major interdomain linker
    • Guy H.I., Evans D.R. Cloning and expression of the mammalian multifunctional protein CAD in Escherichia coli. Characterization of the recombinant protein and a deletion mutant lacking the major interdomain linker. J. Biol. Chem. 269:1994;23808-23816.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23808-23816
    • Guy, H.I.1    Evans, D.R.2
  • 54
    • 0030744665 scopus 로고    scopus 로고
    • Trapping an activated conformation of mammalian carbamyl-phosphate synthetase
    • Guy H.I., Evans D.R. Trapping an activated conformation of mammalian carbamyl-phosphate synthetase. J. Biol. Chem. 272:1997;19906-19912.
    • (1997) J. Biol. Chem. , vol.272 , pp. 19906-19912
    • Guy, H.I.1    Evans, D.R.2
  • 55
    • 0027174079 scopus 로고
    • P-Aminobenzoate synthesis in Escherichia coli: Mutational analysis of three conserved amino acid residues of the amidotransferase PabA
    • Roux B., Walsh C.T. p-Aminobenzoate synthesis in Escherichia coli: mutational analysis of three conserved amino acid residues of the amidotransferase PabA. Biochemistry. 32:1993;3763-3768.
    • (1993) Biochemistry , vol.32 , pp. 3763-3768
    • Roux, B.1    Walsh, C.T.2


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