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Howard Schachman

Research Profile

Chemicals & Drugs

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Escherichia coli

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Physiology

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Catalysis

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Amino Acid Sequences

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Publications

TOP 3
Algirdas Velyvis; Howard K Schachman; Lewis E Kay
Assignment of Ile, Leu, and Val methyl correlations in supra-molecular systems: an application to aspartate transcarbamoylase.
Howard K Schachman; Marvin Cassman
Retrospective. Ruth L. Kirschstein (1926-2009).
Algirdas Velyvis; Howard K Schachman; Lewis E Kay
Application of methyl-TROSY NMR to test allosteric models describing effects of nucleotide binding to aspartate transcarbamoylase.

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All Publications

2009: Algirdas Velyvis; Howard K Schachman; Lewis E Kay
Assignment of Ile, Leu, and Val methyl correlations in supra-molecular systems: an application to aspartate transcarbamoylase.
Journal of the American Chemical Society 2009;131(45):16534-43.
2009: Howard K Schachman; Marvin Cassman
Retrospective. Ruth L. Kirschstein (1926-2009).
Science (New York, N.Y.) 2009;326(5955):947.
2009: Algirdas Velyvis; Howard K Schachman; Lewis E Kay
Application of methyl-TROSY NMR to test allosteric models describing effects of nucleotide binding to aspartate transcarbamoylase.
Journal of molecular biology 2009;387(3):540-7.
2007: Algirdas Velyvis; Ying R Yang; Howard K Schachman; Lewis E Kay
A solution NMR study showing that active site ligands and nucleotides directly perturb the allosteric equilibrium in aspartate transcarbamoylase.
Proceedings of the National Academy of Sciences of the United States of America 2007;104(21):8815-20.
2006: Howard K Schachman
From "publish or perish" to "patent and prosper".
The Journal of biological chemistry 2006;281(11):6889-903.
2004: Howard K Schachman
Those wonderful early years with the Model E ultracentrifuge and David Yphantis.
Biophysical chemistry 2004;108(1-3):9-16.
2003: Howard K Schachman
On scientific freedom and responsibility.
Biophysical chemistry 2003;100(1-3):615-25.
2002: N N Kalnine; Howard K Schachman
Quantitative urea gradient gel electrophoresis for studies of dissociation and unfolding of oligomeric proteins.
Biophysical chemistry 2002;101-102():133-44.
2001: Peter Beernink; Y R Yang; R Graf; David S King; S S Shah; Howard K Schachman
Random circular permutation leading to chain disruption within and near alpha helices in the catalytic chains of aspartate transcarbamoylase: effects on assembly, stability, and function.
Protein science : a publication of the Protein Society 2001;10(3):528-37.
2001: X Ni; Howard K Schachman
In vivo assembly of aspartate transcarbamoylase from fragmented and circularly permuted catalytic polypeptide chains.
Protein science : a publication of the Protein Society 2001;10(3):519-27.
2000: James A Endrizzi; Peter Beernink; Thomas Alber; Howard K Schachman
Binding of bisubstrate analog promotes large structural changes in the unregulated catalytic trimer of aspartate transcarbamoylase: implications for allosteric regulation.
Proceedings of the National Academy of Sciences of the United States of America 2000;97(10):5077-82.
2000: Howard K Schachman
Still looking for the Ivory Tower.
Annual review of biochemistry 2000;69():1-29.
1999: Peter Beernink; James A Endrizzi; Thomas Alber; Howard K Schachman
Assessment of the allosteric mechanism of aspartate transcarbamoylase based on the crystalline structure of the unregulated catalytic subunit.
Proceedings of the National Academy of Sciences of the United States of America 1999;96(10):5388-93.
1996: R Graf; Howard K Schachman
Random circular permutation of genes and expressed polypeptide chains: application of the method to the catalytic chains of aspartate transcarbamoylase.
Proceedings of the National Academy of Sciences of the United States of America 1996;93(21):11591-6.
1996: P Zhang; Howard K Schachman
In vivo formation of allosteric aspartate transcarbamoylase containing circularly permuted catalytic polypeptide chains: implications for protein folding and assembly.
Protein science : a publication of the Protein Society 1996;5(7):1290-300.
1996: Y R Yang; Howard K Schachman
A bifunctional fusion protein containing the maltose-binding polypeptide and the catalytic chain of aspartate transcarbamoylase: assembly, oligomers, and domains.
Biophysical chemistry 1996;59(3):289-97.
1996: L B Murata; Howard K Schachman
Structural similarity between ornithine and aspartate transcarbamoylases of Escherichia coli: implications for domain switching.
Protein science : a publication of the Protein Society 1996;5(4):719-28.
1996: L B Murata; Howard K Schachman
Structural similarity between ornithine and aspartate transcarbamoylases of Escherichia coli: characterization of the active site and evidence for an interdomain carboxy-terminal helix in ornithine transcarbamoylase.
Protein science : a publication of the Protein Society 1996;5(4):709-18.
1994: B B Zhou; G L Waldrop; L Lum; Howard K Schachman
A 70-amino acid zinc-binding polypeptide fragment from the regulatory chain of aspartate transcarbamoylase causes marked changes in the kinetic mechanism of the catalytic trimer.
Protein science : a publication of the Protein Society 1994;3(6):967-74.
1994: C B Peterson; B B Zhou; D Hsieh; A N Creager; Howard K Schachman
Association of the catalytic subunit of aspartate transcarbamoylase with a zinc-containing polypeptide fragment of the regulatory chain leads to increases in thermal stability.
Protein science : a publication of the Protein Society 1994;3(6):960-6.
1993: Y R Yang; Howard K Schachman
Aspartate transcarbamoylase containing circularly permuted catalytic polypeptide chains.
Proceedings of the National Academy of Sciences of the United States of America 1993;90(24):11980-4.
1993: Howard K Schachman
What is misconduct in science?
Science (New York, N.Y.) 1993;261(5118):148-9, 183.
1993: Y R Yang; Howard K Schachman
In vivo formation of active aspartate transcarbamoylase from complementing fragments of the catalytic polypeptide chains.
Protein science : a publication of the Protein Society 1993;2(6):1013-23.
1993: V M Powers; Y R Yang; M J Fogli; Howard K Schachman
Reconstitution of active catalytic trimer of aspartate transcarbamoylase from proteolytically cleaved polypeptide chains.
Protein science : a publication of the Protein Society 1993;2(6):1001-12.
1993: B B Zhou; Howard K Schachman
Peptide-protein interaction markedly alters the functional properties of the catalytic subunit of aspartate transcarbamoylase.
Protein science : a publication of the Protein Society 1993;2(1):103-12.
1992: Robert E Cohen; M Takama; Howard K Schachman
1H NMR studies on the catalytic subunit of aspartate transcarbamoylase.
Proceedings of the National Academy of Sciences of the United States of America 1992;89(24):11881-5.
1992: Edward Eisenstein; M S Han; T S Woo; J M Ritchey; Ian R Gibbons; Y R Yang; Howard K Schachman
Negative complementation in aspartate transcarbamylase. Analysis of hybrid enzyme molecules containing different arrangements of polypeptide chains from wild-type and inactive mutant catalytic subunits.
The Journal of biological chemistry 1992;267(31):22148-55.
1992: C B Peterson; D L Burman; Howard K Schachman
Effects of replacement of active site residue glutamine 231 on activity and allosteric properties of aspartate transcarbamoylase.
Biochemistry 1992;31(36):8508-15.
1992: L E Parmentier; M H O'Leary; Howard K Schachman; W W Cleland
13C isotope effect studies of Escherichia coli aspartate transcarbamylase in the presence of the bisubstrate analog N-(phosphonoacetyl)-L-aspartate.
Biochemistry 1992;31(28):6598-602.
1992: G L Waldrop; J L Turnbull; L E Parmentier; S Lee; M H O'Leary; W W Cleland; Howard K Schachman
The contribution of threonine 55 to catalysis in aspartate transcarbamoylase.
Biochemistry 1992;31(28):6592-7.
1992: G L Waldrop; J L Turnbull; L E Parmentier; M H O'Leary; W W Cleland; Howard K Schachman
Steady-state kinetics and isotope effects on the mutant catalytic trimer of aspartate transcarbamoylase containing the replacement of histidine 134 by alanine.
Biochemistry 1992;31(28):6585-91.
1992: L E Parmentier; P M Weiss; M H O'Leary; Howard K Schachman; W W Cleland
13C and 15N isotope effects as a probe of the chemical mechanism of Escherichia coli aspartate transcarbamylase.
Biochemistry 1992;31(28):6577-84.
1992: L E Parmentier; M H O'Leary; Howard K Schachman; W W Cleland
13C isotope effects as a probe of the kinetic mechanism and allosteric properties of Escherichia coli aspartate transcarbamylase.
Biochemistry 1992;31(28):6570-6.
1992: J L Turnbull; G L Waldrop; Howard K Schachman
Ionization of amino acid residues involved in the catalytic mechanism of aspartate transcarbamoylase.
Biochemistry 1992;31(28):6562-9.
1992: C B Peterson; Howard K Schachman
Long range effects of amino acid substitutions in the catalytic chain of aspartate transcarbamoylase. Localized replacements in the carboxyl-terminal alpha-helix cause marked alterations in allosteric properties and intersubunit interactions.
The Journal of biological chemistry 1992;267(4):2443-50.
1991: D W Markby; B B Zhou; Howard K Schachman
A 70-amino acid zinc-binding polypeptide from the regulatory chain of aspartate transcarbamoylase forms a stable complex with the catalytic subunit leading to markedly altered enzyme activity.
Proceedings of the National Academy of Sciences of the United States of America 1991;88(23):10568-72.
1991: S R Wente; Howard K Schachman
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 enzyme.
The Journal of biological chemistry 1991;266(31):20833-9.
1991: C B Peterson; Howard K Schachman
Role of a carboxyl-terminal helix in the assembly, interchain interactions, and stability of aspartate transcarbamoylase.
Proceedings of the National Academy of Sciences of the United States of America 1991;88(2):458-62.
1990: J O Newell; Howard K Schachman
Amino acid substitutions which stabilize aspartate transcarbamoylase in the R state disrupt both homotropic and heterotropic effects.
Biophysical chemistry 1990;37(1-3):183-96.
1990: Edward Eisenstein; D W Markby; Howard K Schachman
Heterotropic effectors promote a global conformational change in aspartate transcarbamoylase.
Biochemistry 1990;29(15):3724-31.
1989: H L Levin; K Park; Howard K Schachman
Attenuation in the regulation of the pyrBI operon in Escherichia coli. In vivo studies of transcriptional termination.
The Journal of biological chemistry 1989;264(25):14638-45.
1989: Edward Eisenstein; D W Markby; Howard K Schachman
Changes in stability and allosteric properties of aspartate transcarbamoylase resulting from amino acid substitutions in the zinc-binding domain of the regulatory chains.
Proceedings of the National Academy of Sciences of the United States of America 1989;86(9):3094-8.
1989: W E Werner; J R Cann; Howard K Schachman
Boundary spreading in sedimentation velocity experiments on partially liganded aspartate transcarbamoylase. A ligand-mediated isomerization.
Journal of molecular biology 1989;206(1):231-7.
1989: W E Werner; Howard K Schachman
Analysis of the ligand-promoted global conformational change in aspartate transcarbamoylase. Evidence for a two-state transition from boundary spreading in sedimentation velocity experiments.
Journal of molecular biology 1989;206(1):221-30.
1989: J O Newell; D W Markby; Howard K Schachman
Cooperative binding of the bisubstrate analog N-(phosphonacetyl)-L-aspartate to aspartate transcarbamoylase and the heterotropic effects of ATP and CTP.
The Journal of biological chemistry 1989;264(5):2476-81.
1988: Howard K Schachman
Can a simple model account for the allosteric transition of aspartate transcarbamoylase?
The Journal of biological chemistry 1988;263(35):18583-6.
1988: C Kleanthous; David E Wemmer; Howard K Schachman
The role of an active site histidine in the catalytic mechanism of aspartate transcarbamoylase.
The Journal of biological chemistry 1988;263(26):13062-7.
1987: Howard K Schachman
From allostery to mutagenesis: 20 years with aspartate transcarbamoylase.
Biochemical Society transactions 1987;15(4):772-5.
1987: Y R Yang; Howard K Schachman
Hybridization as a technique for studying interchain interactions in the catalytic trimers of aspartate transcarbamoylase.
Analytical biochemistry 1987;163(1):188-95.
1987: S R Wente; Howard K Schachman
Shared active sites in oligomeric enzymes: model studies with defective mutants of aspartate transcarbamoylase produced by site-directed mutagenesis.
Proceedings of the National Academy of Sciences of the United States of America 1987;84(1):31-5.
1986: E A Robey; S R Wente; D W Markby; A Flint; Y R Yang; Howard K Schachman
Effect of amino acid substitutions on the catalytic and regulatory properties of aspartate transcarbamoylase.
Proceedings of the National Academy of Sciences of the United States of America 1986;83(16):5934-8.
1986: R S Lahue; Howard K Schachman
Communication between polypeptide chains in aspartate transcarbamoylase. Conformational changes at the active sites of unliganded chains resulting from ligand binding to other chains.
The Journal of biological chemistry 1986;261(7):3079-84.
1986: Robert E Cohen; Howard K Schachman
Kinetics of the interaction of N-(phosphonacetyl)-L-aspartate with the catalytic subunit of aspartate transcarbamoylase. A slow conformational change subsequent to binding.
The Journal of biological chemistry 1986;261(6):2623-31.
1985: J Foote; Howard K Schachman
Homotropic effects in aspartate transcarbamoylase. What happens when the enzyme binds a single molecule of the bisubstrate analog N-phosphonacetyl-L-aspartate?
Journal of molecular biology 1985;186(1):175-84.
1985: D B Wacks; Howard K Schachman
19F nuclear magnetic resonance studies of communication between catalytic and regulatory subunits in aspartate transcarbamoylase.
The Journal of biological chemistry 1985;260(21):11659-62.
1985: D B Wacks; Howard K Schachman
19F nuclear magnetic resonance studies of fluorotyrosine-labeled aspartate transcarbamoylase. Properties of the enzyme and its catalytic and regulatory subunits.
The Journal of biological chemistry 1985;260(21):11651-8.
1985: H L Levin; Howard K Schachman
Regulation of aspartate transcarbamoylase synthesis in Escherichia coli: analysis of deletion mutations in the promoter region of the pyrBI operon.
Proceedings of the National Academy of Sciences of the United States of America 1985;82(14):4643-7.
1985: Robert E Cohen; J Foote; Howard K Schachman
On conformational changes in the regulatory enzyme aspartate transcarbamoylase.
Current topics in cellular regulation 1985;26():177-90.
1985: E A Robey; Howard K Schachman
Regeneration of active enzyme by formation of hybrids from inactive derivatives: implications for active sites shared between polypeptide chains of aspartate transcarbamoylase.
Proceedings of the National Academy of Sciences of the United States of America 1985;82(2):361-5.
1984: J B Hunt; S H Neece; Howard K Schachman; Ann Ginsburg
Mercurial-promoted Zn2+ release from Escherichia coli aspartate transcarbamoylase.
The Journal of biological chemistry 1984;259(23):14793-803.
1984: R S Lahue; Howard K Schachman
The influence of quaternary structure on the active site of an oligomeric enzyme. Catalytic subunit of aspartate transcarbamoylase.
The Journal of biological chemistry 1984;259(22):13906-13.
1984: E A Robey; Howard K Schachman
Site-specific mutagenesis of aspartate transcarbamoylase. Replacement of tyrosine 165 in the catalytic chain by serine reduces enzymatic activity.
The Journal of biological chemistry 1984;259(18):11180-3.
1984: L P Vickers; J G Compton; K A Wall; J E Flatgaard; Howard K Schachman
Comparison of active mutants and wild-type aspartate transcarbamoylase of Escherichia coli.
The Journal of biological chemistry 1984;259(17):11027-35.
1984: Howard K Schachman; C. David Pauza; M Navre; M J Karels; L Wu; Y R Yang
Location of amino acid alterations in mutants of aspartate transcarbamoylase: Structural aspects of interallelic complementation.
Proceedings of the National Academy of Sciences of the United States of America 1984;81(1):115-9.
1983: R S Johnson; Howard K Schachman
Communication between catalytic and regulatory subunits in Ni(II)- and Co(II)-aspartate transcarbamoylase. Ligand-promoted structural alterations at the intersubunit bonding domains.
The Journal of biological chemistry 1983;258(6):3528-38.
1983: D D Jenness; Howard K Schachman
Genetic characterization of the folding domains of the catalytic chains in aspartate transcarbamoylase.
The Journal of biological chemistry 1983;258(5):3266-79.
1983: M Navre; Howard K Schachman
Synthesis of aspartate transcarbamoylase in Escherichia coli: transcriptional regulation of the pyrB-pyrI operon.
Proceedings of the National Academy of Sciences of the United States of America 1983;80(5):1207-11.
1983: Howard K Schachman
Assembly of aspartate transcarbamoylase in Escherichia coli.
Transactions of the New York Academy of Sciences 1983;41():199-211.
1982: S Subramani; Howard K Schachman
Linkage between reactivity of sulfhydryl groups and subunit interactions in aspartate transcarbamoylase.
The Journal of biological chemistry 1982;257(20):12219-23.
1982: D L Burns; Howard K Schachman
Ligand-promoted strengthening of interchain bonding domains in catalytic subunits of aspartate transcarbamoylase.
The Journal of biological chemistry 1982;257(20):12214-8.
1982: D L Burns; Howard K Schachman
Assembly of the catalytic trimers of aspartate transcarbamoylase from unfolded polypeptide chains.
The Journal of biological chemistry 1982;257(15):8648-54.
1982: D L Burns; Howard K Schachman
Assembly of the catalytic trimers of aspartate transcarbamoylase from folded monomers.
The Journal of biological chemistry 1982;257(15):8638-47.
1982: C. David Pauza; M J Karels; M Navre; Howard K Schachman
Genes encoding Escherichia coli aspartate transcarbamoylase: the pyrB-pyrI operon.
Proceedings of the National Academy of Sciences of the United States of America 1982;79(13):4020-4.
1981: P Hensley; Y R Yang; Howard K Schachman
On the detection of homotropic effects in enzymes of low co-operativity. Application to modified aspartate transcarbamoylase.
Journal of molecular biology 1981;152(1):131-52.
1981: C Wang; Y R Yang; C Y Hu; Howard K Schachman
Communication between subunits in aspartate transcarbamoylase. Effect of active site ligands on the tertiary structure of regulatory chains.
The Journal of biological chemistry 1981;256(13):7028-34.
1981: A Shrake; Ann Ginsburg; Howard K Schachman
Calorimetric estimate of the enthalpy change for the substrate-promoted conformational transition of aspartate transcarbamoylase from Escherichia coli.
The Journal of biological chemistry 1981;256(10):5005-15.
1981: C Y Hu; G J Howlett; Howard K Schachman
Spectral alterations associated with the ligand-promoted gross conformational change in aspartate transcarbamoylase.
The Journal of biological chemistry 1981;256(10):4998-5004.
1981: R Kim; T S Young; Howard K Schachman; S H Kim
Crystallization and preliminary X-ray diffraction studies of an inactive mutant aspartate transcarbamoylase from Escherichia coli.
The Journal of biological chemistry 1981;256(10):4691-2.
1981: S Subramani; Howard K Schachman
The mechanism of dissociation of aspartate transcarbamoylase by p-mercuribenzoate.
The Journal of biological chemistry 1981;256(3):1255-62.
1980: S Subramani; Howard K Schachman
Mechanism of disproportionation of asparate transcarbamoylase molecules lacking one regulatory subunit.
The Journal of biological chemistry 1980;255(17):8136-43.
1980: Y R Yang; Howard K Schachman
Communication between catalytic subunits in hybrid aspartate transcarbamoylase molecules: effect of ligand binding to active chains on the conformation of unliganded, inactive chains.
Proceedings of the National Academy of Sciences of the United States of America 1980;77(9):5187-91.
1980: R S Johnson; Howard K Schachman
Propagation of conformational changes in Ni(II)-substituted aspartate transcarbamoylase: effect of active-site ligands on the regulatory chains.
Proceedings of the National Academy of Sciences of the United States of America 1980;77(4):1995-9.
1980: Mark Bothwell; Howard K Schachman
A model for the assembly of aspartate transcarbamoylase from catalytic and regulatory subunits.
The Journal of biological chemistry 1980;255(5):1971-7.
1980: Mark Bothwell; Howard K Schachman
Equilibrium and kinetic studies of the association of catalytic and regulatory subunits of aspartate transcarbamoylase.
The Journal of biological chemistry 1980;255(5):1962-70.
1980: D D Jenness; Howard K Schachman
pryB mutations as suppressors of arginine auxotrophy in Salmonella typhimurium.
Journal of bacteriology 1980;141(1):33-40.
1979: Alexander N Glazer; R C Williams; G Yamanaka; Howard K Schachman
Characterization of cyanobacterial phycobilisomes in zwitterionic detergents.
Proceedings of the National Academy of Sciences of the United States of America 1979;76(12):6162-6.