About: Structure at 2.9-A resolution of aspartate carbamoyltransferase complexed with the bisubstrate analogue N-(phosphonacetyl)-L-aspartate

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About: Structure at 2.9-A resolution of aspartate carbamoyltransferase complexed with the bisubstrate analogue N-(phosphonacetyl)-L-aspartate Goto Sponge NotDistinct Permalink

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scientific article published on March 1985

Attributes	Values
rdf:type	Item
description	videnskabelig artikel (da) article científic (ca) articolo scientifico (it) artigo científico (pt) bilimsel makale (tr) vedecký článok (sk) vetenskaplig artikel (sv) vědecký článek (cs) wetenschappelijk artikel (nl) wissenschaftlicher Artikel (de) научни чланак (sr) bài báo khoa học (vi) article scientifique (fr) artículu científicu espublizáu en 1985 (ast) 1985年學術文章 (zh) наукова стаття, опублікована в березні 1985 (uk) مقالة علمية نشرت في مارس 1985 (ar) scientific article published on March 1985 (en)
publication date	wds:Q37680322-DD422599-344D-4D0D-A914-46CB0228D17D
publication date	1985-03-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q37680322-2C112A09-64F7-423B-AB87-788834101AEE
language of work or name	English
cites work	wds:Q37680322-02A74F4A-7FFD-4EC9-A0E7-38A312D53C32 wds:Q37680322-04429D8A-5D76-44F5-982F-F4401665C587 wds:Q37680322-04E7DAAB-5D88-41F8-86C8-31F394DEE3DC wds:Q37680322-086253A4-E113-41B5-96AC-CBD1EA600868 wds:Q37680322-1FEB8E5C-87A0-41F2-AE73-B0ECCA7C74E2 wds:Q37680322-20DA3421-BD68-452E-AE32-60D94685F4A8 wds:Q37680322-2942EBC1-500D-43AE-B33D-F94B5CA0BD31 wds:Q37680322-331B3802-9F36-40AD-9BFB-36314E0C116B wds:Q37680322-3FCAB323-BB71-4153-BE90-5593B393108B wds:Q37680322-42B4D0FD-0564-43B2-ADC8-9DEF81659359 wds:Q37680322-4902DA92-CE99-4EA2-A7C3-CD94F68F40C4 wds:Q37680322-4F03532F-95BF-4E94-A5F0-80DDADE51850 wds:Q37680322-639931E8-75BA-41A4-82B8-0444CF475422 wds:Q37680322-700B018F-7505-4FDA-9C9C-0BD4A2C9D815 wds:Q37680322-7700FF45-B668-4819-878D-EF6536FE3CF3 wds:Q37680322-7E1A808E-E341-4103-BF22-B034092A904A wds:Q37680322-8B9943E8-6BE5-447D-84AD-C4F1AA28F8FC wds:Q37680322-9171443B-EAB1-431C-A72C-4824B07CE99F wds:Q37680322-941302DF-5415-4146-A581-FCB6EC9C1D17 wds:Q37680322-A0E41629-4567-4CEB-BFC3-6D44B7805471 wds:Q37680322-A40A6585-9D1F-4E9D-A632-CA048B9D8EB9 wds:Q37680322-AE98EFD7-FEAD-4ACD-8617-4A4760EF2BED wds:Q37680322-CB873997-D077-40CD-BF10-9A508DE61FD8 wds:Q37680322-DB899986-8346-4AAC-8BF9-0D3CDB695426 wds:Q37680322-DD0C6D2F-F555-4AB1-AF37-C52AD90FB963 wds:Q37680322-EAFF27C0-F8B0-40C7-BB23-3B698F4BCCA8 wds:Q37680322-EE155D21-2FB5-41CD-9521-56721932EB5B wds:Q37680322-F922EB51-C5DD-48D0-9B46-386DB491BCD4 wds:Q37680322-FBFC6729-44D7-4E9E-BDCE-B015D0CDD9BA
cites work	A study of the sulfhydryl groups of the catalytic subunit of Escherichia coli aspartate transcarbamylase. The use of enzyme--5-thio-2-nitrobenzoate mixed disulfides as intermediates in modifying enzyme sulfhydryl groups Structure of unligated aspartate carbamoyltransferase of Escherichia coli at 2.6-A resolution Location of amino acid alterations in mutants of aspartate transcarbamoylase: Structural aspects of interallelic complementation Aspartate transcarbamylase. Interaction with the transition state analogue N-(phosphonacetyl)-L-aspartate. The enzymology of control by feedback inhibition. Allosteric regulation of aspartate transcarbamoylase. Changes in the sedimentation coefficient promoted by the bisubstrate analog N-(phosphonacetyl)-L-aspartate Interactions of phosphate ligands with Escherichia coli aspartate carbamoyltransferase in the crystalline state Structure and function of haemoglobin. 3. A three-dimensional fourier synthesis of human deoxyhaemoglobin at 5.5 Angstrom resolution. Crystal and molecular structures of native and CTP-liganded aspartate carbamoyltransferase from Escherichia coli Three-dimensional structures of aspartate carbamoyltransferase from Escherichia coli and of its complex with cytidine triphosphate Modification of three active site lysine residues in the catalytic subunit of aspartate transcarbamylase by D- and L-bromosuccinate. Changes in the X-ray solution scattering of aspartate transcarbamylase following the allosteric transition New Structural Model of E. coli Aspartate Transcarbamylase and the Amino-acid Sequence of the Regulatory Polypeptide Chain The Purification of Aspartate Transcarbamylase of Escherichia coli and Separation of Its Protein Subunits The 5.5 A Resolution Structure of the Regulatory Enzyme, Aspartate Transcarbamylase Carbamyl phosphate: an allosteric substrate for aspartate transcarbamylase of Escherichia coli ASPARTATE TRANSCARBAMYLASE, AN ENZYME DESIGNED FOR FEEDBACK INHIBITION Pyridoxal 5'-phosphate, a fluorescent probe in the active site of aspartate transcarbamylase Crystallographic Determination of Symmetry of Aspartate Transcarbamylase Elimination of cooperativity in aspartate transcarbamylase by nitration of a single tyrosine residue Primary structure and properties of an inactive mutant aspartate transcarbamoylase Aspartate transcarbamylase from Escherichia coli. The use of pyridoxal 5'-phosphate as a probe in the active site. Gross quaternary changes in aspartate carbamoyltransferase are induced by the binding of N-(phosphonacetyl)-L-aspartate: A 3.5-A resolution study Purification and characterization of a mutant aspartate transcarbamoylase lacking enzyme activity The effect of pH on the cooperative behavior of aspartate transcarbamylase from Escherichia coli A unifying concept for the active site region in aspartate transcarbamylase Inactivation of the catalytic subunit of aspartate transcarbamylase by nitration with tetranitromethane The modification of the catalytic chain sulfhydryl group of aspartate transcarbamylase with mercurinitrophenols Regulation of the glycine cleavage system in the isolated perfused rat liver
author name string	wds:Q37680322-658676BC-F108-43FE-A6C6-22CC08108C2F wds:Q37680322-E9739854-230A-42F7-B3E0-91A7B238E4C6 wds:Q37680322-FD30821E-63A3-4531-8FD0-602FD7C43369
author name string	K L Krause K W Volz W N Lipscomb
rdfs:label	Structure at 2.9-A resolution of aspartate carbamoyltransferase complexed with the bisubstrate analogue N- (nl) Structure at 2.9-A resolution of aspartate carbamoyltransferase complexed with the bisubstrate analogue N-(phosphonacetyl)-L-aspartate (en) Structure at 2.9-A resolution of aspartate carbamoyltransferase complexed with the bisubstrate analogue N-(phosphonacetyl)-L-aspartate (ast)
skos:prefLabel	Structure at 2.9-A resolution of aspartate carbamoyltransferase complexed with the bisubstrate analogue N- (nl) Structure at 2.9-A resolution of aspartate carbamoyltransferase complexed with the bisubstrate analogue N-(phosphonacetyl)-L-aspartate (en) Structure at 2.9-A resolution of aspartate carbamoyltransferase complexed with the bisubstrate analogue N-(phosphonacetyl)-L-aspartate (ast)
name	Structure at 2.9-A resolution of aspartate carbamoyltransferase complexed with the bisubstrate analogue N- (nl) Structure at 2.9-A resolution of aspartate carbamoyltransferase complexed with the bisubstrate analogue N-(phosphonacetyl)-L-aspartate (en) Structure at 2.9-A resolution of aspartate carbamoyltransferase complexed with the bisubstrate analogue N-(phosphonacetyl)-L-aspartate (ast)
title	wds:Q37680322-F867B962-1D27-4CD4-AD25-AFFF37EF5B00
title	Structure at 2.9-A resolution of aspartate carbamoyltransferase complexed with the bisubstrate analogue N-(phosphonacetyl)-L-aspartate (en)
page(s)	wds:Q37680322-D75C64B6-CB88-4253-A991-07ED90B823CA
page(s)	1643-1647

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