Literature DB >> 321032

Regulation of aspartate carbamoyltransferase of Escherichia coli by the interrelationship of magnesium and nucleotides.

R I Christopherson, L R Finch.   

Abstract

Purified aspartate carbamoyltransferase from Escherichia coli K12 (carbamoylphosphate: L-aspartate carbamyltransferase, EC 2.1.3.2) shows greater activity with nucleotide effectors as the magnesium nucleotide complex than with similar amounts of the sodium nucleotide. Regulation of aspartate carbamoyltransferase activity in vivo may occur by changes in the total concentration of regulatory nucleotides or, under conditions of magnesium-limited growth, by variation of the saturation of the nucleotides with magnesium.

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Year:  1977        PMID: 321032     DOI: 10.1016/0005-2744(77)90139-5

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  3 in total

1.  Metal ion involvement in the allosteric mechanism of Escherichia coli aspartate transcarbamoylase.

Authors:  Gregory M Cockrell; Evan R Kantrowitz
Journal:  Biochemistry       Date:  2012-08-24       Impact factor: 3.162

2.  A 3.0-A resolution study of nucleotide complexes with aspartate carbamoyltransferase.

Authors:  R B Honzatko; H L Monaco; W N Lipscomb
Journal:  Proc Natl Acad Sci U S A       Date:  1979-10       Impact factor: 11.205

3.  Metal cation influence on activity and regulation of aspartate carbamoyltransferase.

Authors:  R B Honzatko; A M Lauritzen; W N Lipscomb
Journal:  Proc Natl Acad Sci U S A       Date:  1981-02       Impact factor: 11.205

  3 in total

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