Insights into the mechanisms of catalysis and heterotropic regulation of Escherichia coli aspartate transcarbamoylase based upon a structure of the enzyme complexed with the bisubstrate analogue N-phosphonacetyl-L-aspartate at 2.1 Å

Proteins: Structure, Function and Genetics

Volumn 37, Issue 4, 1999, Pages 729-742

  Jin, Lei ^a   Stec, Boguslaw ^b   Lipscomb, William N ^c   Kantrowitz, Evan R ^a  

^a BOSTON COLLEGE   (United States)

^b RICE UNIVERSITY   (United States)

^c HARVARD UNIVERSITY   (United States)

Author keywords

Allosteric regulatory; Cooperativity; Enzyme inhibitor complex; Tetrahedral intermediate

Indexed keywords

ASPARTATE CARBAMOYLTRANSFERASE; SPARFOSIC ACID;

ALLOSTERISM; ARTICLE; BINDING AFFINITY; BINDING SITE; CATALYSIS; ELECTRIC FIELD; ENZYME INHIBITION; ENZYME INHIBITOR COMPLEX; ENZYME MECHANISM; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN STRUCTURE;

ALLOSTERIC REGULATION; ASPARTATE CARBAMOYLTRANSFERASE; ASPARTIC ACID; CATALYSIS; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; ELECTROSTATICS; ESCHERICHIA COLI; MODELS, MOLECULAR; PHOSPHONOACETIC ACID; PROTEIN CONFORMATION; SUBSTRATE SPECIFICITY;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; NEGIBACTERIA;

EID: 0032747749     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(19991201)37:4<729::AID-PROT21>3.0.CO;2-F     Document Type: Article

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