Replacement 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 transcarbamoylase

Protein Science

Volumn 11, Issue 5, 2002, Pages 1074-1081

  Fetler, L ^a,b,d   Tauc, P ^d   Baker, D P ^c,d   Macol, C P ^c,d   Kantrowitz, E R ^c,d   Vachette, P ^a,d  

^a DIF   (France)

^b CNRS   (France)

^c Ecole Normale Superieure de Cachan   (France)

^d BOSTON COLLEGE   (United States)

Author keywords

Allostery; Aspartate transcarbamoylase; Cooperativity; Quaternary structural changes; Small angle X ray scattering

Indexed keywords

ADENOSINE TRIPHOSPHATE; ALANINE; ASPARTATE CARBAMOYLTRANSFERASE; ASPARTIC ACID; MUTANT PROTEIN; SPARFOSIC ACID;

ALLOSTERISM; ARTICLE; BINDING AFFINITY; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; ENZYME ACTIVITY; ESCHERICHIA COLI; MEASUREMENT; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN INTERACTION; REACTION ANALYSIS; X RAY CRYSTALLOGRAPHY;

ESCHERICHIA COLI;

EID: 0036229568     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.4500102     Document Type: Article

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