Can a simple model account for the allosteric transition of aspartate transcarbamoylase?SCHACHMAN, H. K.The Journal of biological chemistry (Print). 1988, Vol 263, Num 35, pp 18583-18586, issn 0021-9258Article

Aspartate transcarbamoylase containing circularly permuted catalytic polypeptide chainsYANG, Y. R; SCHACHMAN, H. K.Proceedings of the National Academy of Sciences of the United States of America. 1993, Vol 90, Num 24, pp 11980-11984, issn 0027-8424Article

Shared active sites in oligomeric enzymes: model studies with defective mutants of aspartate transcarbamoylase produced by site-directed mutagenesisWENTE, S. R; SCHACHMAN, H. K.Proceedings of the National Academy of Sciences of the United States of America. 1987, Vol 84, Num 1, pp 31-35, issn 0027-8424Article

¹⁹F nuclear magnetic resonance studies of fluorotyrosine-labeled aspartate transcarbamoylase: properties of the enzyme and its catalytic and regulatory subunitsWACKS, D. B; SCHACHMAN, H. K.The Journal of biological chemistry (Print). 1985, Vol 260, Num 21, pp 11651-11658, issn 0021-9258Article

The influence of quaternary structure on the active site of an oligomeric enzyme: catalytic subunit of aspartate transcarbamoylaseLAHUE, R. S; SCHACHMAN, H. K.The Journal of biological chemistry (Print). 1984, Vol 259, Num 22, pp 13906-13913, issn 0021-9258Article

Long range effects of amino acid substitutions in the catalytic chain of aspartate transcarbamoylase : localized replacements in the carboxyl-terminal α-helix cause marked alterations in allosteric properties and intersubunit interactionsPETERSON, C. B; SCHACHMAN, H. K.The Journal of biological chemistry (Print). 1992, Vol 267, Num 4, pp 2443-2450, issn 0021-9258Article

¹H NMR studies on the catalytic subunit of aspartate transcarbamoylaseCOHEN, R. E; TAKAMA, M; SCHACHMAN, H. K et al.Proceedings of the National Academy of Sciences of the United States of America. 1992, Vol 89, Num 24, pp 11881-11885, issn 0027-8424Article

Amino acid substitutions withic stabilize aspartate transcarbamoylase in the R state disrupt both homotropic and heterotropic effectsNEWELL, J. O; SCHACHMAN, H. K.Biophysical chemistry. 1990, Vol 37, Num 1-3, pp 183-196, issn 0301-4622, 14 p.Article

Regeneration of active enzyme by formation of hybrids from inactive derivatives: implications for active sites shared between polypeptide chains of aspartate transcarbamoylaseROBEY, E. A; SCHACHMAN, H. K.Proceedings of the National Academy of Sciences of the United States of America. 1985, Vol 82, Num 2, pp 361-365, issn 0027-8424Article

Role of a carboxyl-terminal helix in the assembly, interchain interactions, and stability of aspartate transcarbamoylasePETERSON, C. B; SCHACHMAN, H. K.Proceedings of the National Academy of Sciences of the United States of America. 1991, Vol 88, Num 2, pp 458-462, issn 0027-8424, 5 p.Article

Different amino acid substitutions at the same position in the nucleotide-binding site of aspartate transcarbamoylase have diverse effects on the allosteric properties of the enzymeWENTE, S. R; SCHACHMAN, H. K.The Journal of biological chemistry (Print). 1991, Vol 266, Num 31, pp 20833-20839, issn 0021-9258Article

Site-specific mutagenesis of aspartate transcarbamoylase: replacement of tyrosine 165 in the catalytic chain by serine reduces enzymatic activityROBEY, E. A; SCHACHMAN, H. K.The Journal of biological chemistry (Print). 1984, Vol 259, Num 18, pp 11180-11183, issn 0021-9258Article

Changes in stability and allosteric properties of aspartate transcarbamoylase resulting from amino acid substitutions in the zinc-binding domain of the regulatory chainsEISENSTEIN, E; MARKBY, D. W; SCHACHMAN, H. K et al.Proceedings of the National Academy of Sciences of the United States of America. 1989, Vol 86, Num 9, pp 3094-3098, issn 0027-8424Article

Attenuation in the regulation of the pyrBI operon in Escherichia coli: in vivo studies of transcriptional terminationLEVIN, H. L; KYEONG PARK; SCHACHMAN, H. K et al.The Journal of biological chemistry (Print). 1989, Vol 264, Num 25, pp 14638-14645, issn 0021-9258, 8 p.Article

On conformational changes in the regulatory enzyme aspartate transcarbamoylaseCOHEN, R. E; FOOTE, J; SCHACHMAN, H. K et al.Current topics in cellular regulation. 1985, Vol 26, pp 177-190, issn 0070-2137Article

Effects of replacement of active site residue glutamine 231 on activity and allosteric properties of aspartate transcarbamoylasePETERSON, C. B; BURMAN, D. L; SCHACHMAN, H. K et al.Biochemistry (Easton). 1992, Vol 31, Num 36, pp 8508-8515, issn 0006-2960Article

Steady-state kinetics and isotope effects on the mutant catalytic trimer of aspartate transcarbamoylase containing the replacement of histidine 134 by alanineWALDROP, G. L; TURNBULL, J. L; PARMENTIER, L. E et al.Biochemistry (Easton). 1992, Vol 31, Num 28, pp 6585-6591, issn 0006-2960Article

The contribution of threonine 55 to catalysis in aspartate transcarbamoylaseWALDROP, G. L; TURNBULL, J. L; PARMENTIER, L. E et al.Biochemistry (Easton). 1992, Vol 31, Num 28, pp 6592-6597, issn 0006-2960Article

¹³C isotope effect studies of Escherichia coli aspartate transcarbamylase in the presence of the bisubstrate analog N-(phosphonoacetyl)-L-aspartateO'LEARY, M. H; SCHACHMAN, H. K et al.Biochemistry (Easton). 1992, Vol 31, Num 28, pp 6598-6602, issn 0006-2960Article

¹³C isotope effects as a probe of the kinetic mechanism and allosteric properties of Escherichia coli aspartate transcarbamylasePARMENTIER, L. E; O'LEARY, M. H; SCHACHMAN, H. K et al.Biochemistry (Easton). 1992, Vol 31, Num 28, pp 6570-6576, issn 0006-2960Article

Comparison of active mutants and wild-type aspartate transcarbamoylase of Escherichia coliVICKERS, L. P; COMPTON, J. G; WALL, K. A et al.The Journal of biological chemistry (Print). 1984, Vol 259, Num 17, pp 11027-11035, issn 0021-9258Article

¹³C and ¹⁵N isotope effects as a probe of the chemical mechanism of Escherichia coli aspartate transcarbamylasePARMENTIER, L. E; WEISS, P. M; O'LEARY, M. H et al.Biochemistry (Easton). 1992, Vol 31, Num 28, pp 6577-6584, issn 0006-2960Article

Negative complementation in aspartate transcarbamylase : analysis of bybrid enzyme molecules containing different arrangements of polypeptide chains from wild-type and inactive mutant catalytic subunitsEISENSTEIN, E; HAN, M. S; WOO, T. S et al.The Journal of biological chemistry (Print). 1992, Vol 267, Num 31, pp 22148-22155, issn 0021-9258Article

Location of amino acid alterations in mutants of aspartate transcarbamoylase: structural aspects of interallelic complementationSCHACHMAN, H. K; PAUZA, C. D; NAVRE, M et al.Proceedings of the National Academy of Sciences of the United States of America. Biological sciences. 1984, Vol 81, Num 1, pp 115-119, issn 0273-1134Article

Mercurial-promoted Zn²⁺ release from Escherichia coli aspartate transcarbamoylaseHUNT, J. B; NEECE, S. H; SCHACHMAN, H. K et al.The Journal of biological chemistry (Print). 1984, Vol 259, Num 23, pp 14793-14803, issn 0021-9258Article