About: A mutation in the catalytic cistron of aspartate carbamoyltransferase affecting catalysis, regulatory response and holoenzyme assembly

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About: A mutation in the catalytic cistron of aspartate carbamoyltransferase affecting catalysis, regulatory response and holoenzyme assembly Goto Sponge NotDistinct Permalink

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scientific article published in Nature

Attributes	Values
rdf:type	Item
description	artículu científicu (ast) wetenschappelijk artikel (nl) article publié dans la revue scientifique Nature (fr) scientific article published in Nature (en) im Juli 1981 veröffentlichter wissenschaftlicher Artikel (de) наукова стаття, опублікована в Nature в липні 1981 (uk)
publication date	wds:Q59019375-2B95B36F-11B0-47BB-AA9C-88FCE6240C7C
publication date	1981-07-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q59019375-6670BDC3-8D7B-4CEE-8B82-20C5503ADCF0
language of work or name	English
exact match	wds:Q59019375-F93F38CD-1236-49E1-9A63-F0C96C2C9F5D
exact match	https://scigraph.springernature.com/pub.10.1038/292373a0
cites work	wds:Q59019375-009C61EF-D238-4360-B569-6671E91B9D5F wds:Q59019375-1DD350F7-D371-4BBE-BF52-2BB26E231F9D wds:Q59019375-1FFE3B11-0DD4-4E13-BF14-7A6E206F1034 wds:Q59019375-32B27A07-435C-455E-BAE7-A444177F7D7E wds:Q59019375-52ED5A88-DE9E-4310-8B5F-A9454F1BD298 wds:Q59019375-5BBD1E37-1F67-4486-98A8-2447B643A6BD wds:Q59019375-6A5BDDD6-CC63-4C83-9256-721B17366C42 wds:Q59019375-7FFDAA31-A5B1-4F27-A396-0237CB75D6E1 wds:Q59019375-9A06B6EB-C773-48E5-8862-50A7CF1C665E wds:Q59019375-A88F99C4-30C3-4013-B168-5CD3F51441C7 wds:Q59019375-AEAFDDBA-DA92-4A24-B055-5EC05ADFA32F wds:Q59019375-AF67407F-BE90-4D7A-B9FB-E14E3533DD98 wds:Q59019375-C1D5858D-2E21-4CB9-82AE-5A0DE7CCCF2D wds:Q59019375-C5999628-4AFF-4C07-8C68-CFB1A5B082B8 wds:Q59019375-E13ADD30-A7C7-4F23-9C7D-63C93F50C258 wds:Q59019375-E4216D89-0F30-4823-8CDC-6220F9495D0C wds:Q59019375-F29D4885-578B-4283-88BE-3386837B72CB wds:Q59019375-F5EA9EDF-AD0A-4668-8242-AFD5CB75D7CD wds:Q59019375-F69A442E-16DA-47D9-8798-4FB31644A95B wds:Q59019375-FABF9274-D391-4DF4-AA8B-B26BC3C99664
cites work	ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL Distinct Subunits for the Regulation and Catalytic Activity of Aspartate Transcarbamylase* Coordination of the synthesis of the enzymes in the pyrimidine pathway of E. coli Allosteric Interactions in Aspartate Transcarbamylase. II. Evidence for Different Conformational States of the Protein in the Presence and Absence of Specific Ligands BACTERIOPHAGE-INDUCED MUTATION IN ESCHERICHIA COLI Construction and characterization of new cloning vehicle. II. A multipurpose cloning system New Structural Model of E. coli Aspartate Transcarbamylase and the Amino-acid Sequence of the Regulatory Polypeptide Chain Binding of cytidine triphosphate to aspartate transcarbamylase Carbamyl phosphate: an allosteric substrate for aspartate transcarbamylase of Escherichia coli Mutation of gene encoding regulatory polypeptide of aspartate carbamoyltransferase The stimulation of Escherichia coli aspartate transcarbamylase activity by adenosine triphosphate. Relation with the other regulatory conformational changes; a model Crystallographic Determination of Symmetry of Aspartate Transcarbamylase 5 Aspartate transcarbamoylase (Escherichia coli): Preparation of subunits The isolation and partial characterization of a new restriction endonuclease from Providencia stuartii Regulatory divergence of aspartate transcarbamoylases within the enterobacteriaceae Role for zinc in the quaternary structure of aspartate transcarbamylase from Escherichia coli Binding of nucleotides AMP and ATP to yeast phosphofructokinase:evidence for distinct catalytic and regulatory subunits An aspartate transcarbamylase lacking catalytic subunit interactions. II. Regulatory subunits are responsible for the lack of co-operative interactions between catalytic sites. Drastic feedback inhibition does not restore these interactions Biosynthesis of an aspartate transcarbamylase lacking co-operative interactions. I. Disconnection of homotropic and heterotropic interactions under the influence of 2-thiouracil Interaction of tetraiodofluorescein with a modified form of aspartate transcarbamylase
author name string	wds:Q59019375-3E06592D-77BE-4875-A9EF-DE47145B2B8C wds:Q59019375-5341A568-5E01-474E-B704-ED813635CCD2 wds:Q59019375-7A04ED8A-9F7D-4C87-8627-1D9B20D23B99 wds:Q59019375-B68B4445-18A6-4FFA-89E2-328DDD41488C
author name string	J R Wild W D Roof G A O'Donovan K F Foltermann
rdfs:label	A mutation in the catalytic cistron of aspartate carbamoyltransferase affecting catalysis, regulatory response and holoenzyme assembly (en) A mutation in the catalytic cistron of aspartate carbamoyltransferase affecting catalysis, regulatory response and holoenzyme assembly (nl)
skos:prefLabel	A mutation in the catalytic cistron of aspartate carbamoyltransferase affecting catalysis, regulatory response and holoenzyme assembly (en) A mutation in the catalytic cistron of aspartate carbamoyltransferase affecting catalysis, regulatory response and holoenzyme assembly (nl)
name	A mutation in the catalytic cistron of aspartate carbamoyltransferase affecting catalysis, regulatory response and holoenzyme assembly (en) A mutation in the catalytic cistron of aspartate carbamoyltransferase affecting catalysis, regulatory response and holoenzyme assembly (nl)
title	wds:Q59019375-7D0E4482-2DB6-4B55-9BFA-4F76D199015A
title	A mutation in the catalytic cistron of aspartate carbamoyltransferase affecting catalysis, regulatory response and holoenzyme assembly (en)
page(s)	wds:Q59019375-03535313-F756-4C13-B07A-FAA0A960256D
page(s)	373-375
instance of	wds:Q59019375-111C8F8F-E18D-45DD-8152-ECF5CA990AE0
instance of	scholarly article
PubMed ID	wds:Q59019375-F1EAF864-F98B-4FA5-860A-6F5ABE31A67F
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/7019722
PubMed ID	7019722
published in	wds:Q59019375-533009AF-9936-4EB4-AF09-9BDDFB469EC0
published in	Nature
issue	wds:Q59019375-15725482-CBA8-4EFE-A6A7-B37D022D488B
volume	wds:Q59019375-BBD1BEFA-A5A2-4F84-96E4-A1EFF3431493
issue	5821
volume	292
DOI	wds:Q59019375-0FFE2350-C94C-4D17-801E-44BB05D7BBE3
DOI	http://dx.doi.org/10.1038/292373A0
DOI	10.1038/292373A0
Dimensions Publication ID	wds:Q59019375-7B4AD938-B3E0-4473-942B-1BCDB790AE76
Dimensions Publication ID	1050731190
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q59019375
is cites work of	Genetic characterization of the folding domains of the catalytic chains in aspartate transcarbamoylase Linkage map of Escherichia coli K-12, edition 7 Evolutionary divergence of genes for ornithine and aspartate carbamoyl-transferases--complete sequence and mode of regulation of the Escherichia coli argF gene; comparison of argF with argI and pyrB. Nucleotide sequence of the structural gene (pyrB) that encodes the catalytic polypeptide of aspartate transcarbamoylase of Escherichia coli Mutation of gene encoding regulatory polypeptide of aspartate carbamoyltransferase The organization and regulation of the pyrBI operon in E. coli includes a rho-independent attenuator sequence In vivo formation of hybrid aspartate transcarbamoylases from native subunits of divergent members of the family Enterobacteriaceae
is cites work of	wds:Q33627756-4A2F4159-28BB-4482-8927-7B31C052BCDC wds:Q35437492-9066234F-C24C-444D-9C69-BE7948BBA442 wds:Q37609995-B4B23BCC-62E6-4B32-B9A1-EF97EE0B4490 wds:Q48406786-19C5BE27-C863-472D-8D32-669E2DE5A87F wds:Q50211762-1942F71E-A4EA-4798-9049-70161574528D

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