Divergent allosteric patterns verify the regulatory paradigm for aspartate transcarbamylase

Journal of Molecular Biology

Volumn 294, Issue 5, 1999, Pages 1387-1400

  Wales, Melinda E ^a   Madison, Lara L ^a   Glaser, Shannon S ^a   Wild, James R ^a  

^a TEXAS A AND M UNIVERSITY   (United States)

Author keywords

Allosteric regulation; Aspartate transcarbamoylase; Co operativity; E. herbicola; Sequence alignment

Indexed keywords

ADENOSINE TRIPHOSPHATE; ASPARTATE CARBAMOYLTRANSFERASE; ASPARTIC ACID; CYTIDINE TRIPHOSPHATE; HYBRID PROTEIN; URIDINE TRIPHOSPHATE;

ALLOSTERISM; AMINO ACID SEQUENCE; ARTICLE; BINDING SITE; CONFORMATIONAL TRANSITION; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME INHIBITION; ENZYME KINETICS; ENZYME REGULATION; ENZYME SUBSTRATE COMPLEX; ENZYME SUBUNIT; ERWINIA; ESCHERICHIA COLI; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN QUATERNARY STRUCTURE;

EID: 0033579487     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.3315     Document Type: Article

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