In the presence of CTP, UTP becomes an allosteric inhibitor of aspartate transcarbamoylase.
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Allosteric regulation of catalytic activity: Escherichia coli aspartate transcarbamoylase versus yeast chorismate mutaseReplacement of Asp-162 by Ala prevents the cooperative transition by the substrates while enhancing the effect of the allosteric activator ATP on E. coli aspartate transcarbamoylaseIntegrated allosteric regulation in the S. cerevisiae carbamylphosphate synthetase - aspartate transcarbamylase multifunctional proteinArginine 54 in the active site of escherichia coli aspartate transcarbamoylase is critical for catalysis: A site-specific mutagenesis, NMR, and X-ray crystallographic studyThe first high pH structure ofEscherichia coliaspartate transcarbamoylaseMolecular structure of Bacillus subtilis aspartate transcarbamoylase at 3.0 A resolutionDihydroorotase from the Hyperthermophile Aquifiex aeolicus Is Activated by Stoichiometric Association with Aspartate Transcarbamoylase and Forms a One-Pot Reactor for Pyrimidine Biosynthesis † ‡The Pathway of Product Release from the R State of Aspartate TranscarbamoylaseA Cooperative Escherichia coli Aspartate Transcarbamoylase without Regulatory Subunits,Metal Ion Involvement in the Allosteric Mechanism of Escherichia coli Aspartate TranscarbamoylaseA Second Allosteric Site in Escherichia coli Aspartate TranscarbamoylaseStructure and mechanisms of Escherichia coli aspartate transcarbamoylaseTime Evolution of the Quaternary Structure of Escherichia coli Aspartate Transcarbamoylase upon Reaction with the Natural Substrates and a Slow, Tight-Binding InhibitorCrystal structure of the Glu-239----Gln mutant of aspartate carbamoyltransferase at 3.1-A resolution: an intermediate quaternary structure.The contribution of individual interchain interactions to the stabilization of the T and R states of Escherichia coli aspartate transcarbamoylase.The antilymphocytic activity of brequinar sodium and its potentiation by cytidine. Effects on lymphocyte proliferation and cytokine production.Asymmetric allosteric signaling in aspartate transcarbamoylase.A single amino acid substitution in the active site of Escherichia coli aspartate transcarbamoylase prevents the allosteric transitionDirect observation in solution of a preexisting structural equilibrium for a mutant of the allosteric aspartate transcarbamoylase.Pyrimidine homeostasis is accomplished by directed overflow metabolism.Allostery and cooperativity in Escherichia coli aspartate transcarbamoylaseGenetic evidence that promoter P2 is the physiologically significant promoter for the pyrBI operon of Escherichia coli K-12Weakening of the interface between adjacent catalytic chains promotes domain closure in Escherichia coli aspartate transcarbamoylaseThe use of nucleotide analogs to evaluate the mechanism of the heterotropic response of Escherichia coli aspartate transcarbamoylase.N-phosphonacetyl-L-isoasparagine a potent and specific inhibitor of Escherichia coli aspartate transcarbamoylase.A molecular mechanism for pyrimidine and purine nucleotide control of aspartate transcarbamoylase.Structural model of the R state of Escherichia coli aspartate transcarbamoylase with substrates bound.Heterotropic interactions in aspartate transcarbamoylase: turning allosteric ATP activation into inhibition as a consequence of a single tyrosine to phenylalanine mutation.The regulatory subunit of Escherichia coli aspartate carbamoyltransferase may influence homotropic cooperativity and heterotropic interactions by a direct interaction with the loop containing residues 230-245 of the catalytic chain.From feedback inhibition to allostery: the enduring example of aspartate transcarbamoylase.Aspartate carbamoyltransferase from the thermoacidophilic archaeon Sulfolobus acidocaldarius. Cloning, sequence analysis, enzyme purification and characterization.Uncoupling conformational states from activity in an allosteric enzyme.Temperature effects on the allosteric responses of native and chimeric aspartate transcarbamoylases.Conversion of the allosteric regulatory patterns of aspartate transcarbamoylase by exchange of a single beta-strand between diverged regulatory chains.Allosteric signal transmission involves synergy between discrete structural units of the regulatory subunit of aspartate transcarbamoylase.Cell division defects of Schizosaccharomyces pombe liz1- mutants are caused by defects in pantothenate uptake.Dissecting enzyme regulation by multiple allosteric effectors: nucleotide regulation of aspartate transcarbamoylase.Domain bridging interactions. A necessary contribution to the function and structure of Escherichia coli aspartate transcarbamoylase.Stabilization of the R allosteric structure of Escherichia coli aspartate transcarbamoylase by disulfide bond formation.The role of intersubunit interactions for the stabilization of the T state of Escherichia coli aspartate transcarbamoylase.
P2860
Q24548465-02C6B3D2-8BF0-4D70-8C9F-87898BAAD75CQ24645129-502C6F84-56F0-43E4-9D93-4DC11CA8AA7FQ24795316-B66A8F29-D064-4F13-A980-B4DEF9806DA8Q27642036-BB21E1D1-60E6-4BDA-8451-4D3F2AA369FFQ27651125-44BF73F7-56DC-4508-9FAE-8DA0C699BE00Q27653076-CAA00E2C-798F-4A1D-AA8C-C65311B52CE4Q27653358-DA46C6DF-BDF2-40C2-ABBD-08E81C32F780Q27663306-B55BEDB1-0EC6-49B7-B342-68781B6BACA6Q27663832-8A9D9C5C-D62E-4281-9192-7C32F77B3B1AQ27671603-29293841-CBED-4350-AA59-A092BE97DF4EQ27679509-3C2908DA-685D-453D-A364-0FF8F0159B44Q27687456-17FC0644-4140-4957-8ECC-B27EF5841D7BQ29391897-36217A03-CD86-45BF-868C-A01962C4FA41Q30450827-086B9A65-83B8-46EB-8C9C-5B143BAECC50Q33907815-E3D6C401-1DF1-4C46-9D3A-22A1A8F4F0E6Q34299423-EF1028EC-7526-437F-A2B4-EB32F5135548Q34416097-D3E2FF1A-34C0-4950-8FC5-CF1B08CEFC2CQ34682239-713E1CFC-2C8E-49B7-8458-3359B78EE6DBQ35578709-3FA1064D-D427-414D-A87E-BDCC7F21F689Q35751186-384954EC-451D-4DA3-9A35-5E46EFD25BFCQ36085714-0931D1EB-6423-4AF3-A23F-702673A8C354Q36098519-21B1ACDE-7325-4694-A8EA-D707FFC62488Q36279037-798A5126-C642-4452-A241-4BD60B0952EEQ36281716-1F304536-15B1-447A-8C02-9A621E6A56D1Q36881613-F4BAFAF1-0BA3-4BBE-8CEA-0E6D76B00FBBQ37053198-994E4854-5A03-4885-AAB2-34C13B539F5BQ37287204-E99BB825-4A2A-48DA-87D1-CAF3CA77EF47Q37608042-D2416484-4D6C-495A-BEB3-DBC4A8733BEEQ37722721-B228AF5E-1DB3-4439-B0B4-7F2D9160C2BDQ38129478-C02844E1-9340-4AEF-B267-B9426E37F7CCQ38321683-0595AA04-6D20-41B7-8782-422A62B8EDADQ38638225-09DB256A-2FA6-4B83-ABD5-098E8A525197Q39683379-490937A4-7BA5-4190-9AC5-EFA5C426CB5AQ39683463-2D7358EF-85DF-4E25-9211-F141E99AE851Q39897141-E86AD539-4B47-46EB-B96D-F15871067351Q40762970-F6BBA692-A75A-4109-B2D2-E1E59536DB40Q41872739-8E8CE74B-CD86-422A-A775-2525996C2EB6Q43607752-EE098C6F-D2A7-40FB-A5E7-A61A5ACB8A55Q44164525-C69B1305-F14F-4601-93D3-1AA033BDFEE1Q44193826-F8FA6EB3-E03B-48BC-AE97-011482F8642E
P2860
In the presence of CTP, UTP becomes an allosteric inhibitor of aspartate transcarbamoylase.
description
1989 nî lūn-bûn
@nan
1989 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1989 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1989年の論文
@ja
1989年論文
@yue
1989年論文
@zh-hant
1989年論文
@zh-hk
1989年論文
@zh-mo
1989年論文
@zh-tw
1989年论文
@wuu
name
In the presence of CTP, UTP be ...... f aspartate transcarbamoylase.
@ast
In the presence of CTP, UTP be ...... f aspartate transcarbamoylase.
@en
type
label
In the presence of CTP, UTP be ...... f aspartate transcarbamoylase.
@ast
In the presence of CTP, UTP be ...... f aspartate transcarbamoylase.
@en
prefLabel
In the presence of CTP, UTP be ...... f aspartate transcarbamoylase.
@ast
In the presence of CTP, UTP be ...... f aspartate transcarbamoylase.
@en
P2093
P2860
P356
P1476
In the presence of CTP, UTP be ...... f aspartate transcarbamoylase.
@en
P2093
Loughrey-Chen SJ
P2860
P356
10.1073/PNAS.86.1.46
P407
P577
1989-01-01T00:00:00Z