Assembly of catalytic subunits of aspartate transcarbamoylase from Escherichia coli

Journal Article · Wed Oct 01 04:00:00 EDT 1980 · Biophys. J.; (United States)

DOI:https://doi.org/10.1016/S0006-3495(80)84970-8· OSTI ID:6761074

Burns, D L; Schachman, H K

Although extensive studies have been conducted on the assembly of the allosteric enzyme, aspartate transcarbamoylase (ATCase) from isolate, intact catalytic (C) and regulatory (R) subunits, there has been little research on the formation of these subunits from individual catalytic (c) and regulatory (r) polypeptide chains. Such studies would be useful for evaluating the strengths of the interchain bonding domains within the subunits just as earlier experiments provided valuable data regarding interactions between the subunits in ATCase. The intact enzyme comprising two C trimers and three R dimers is designated as C/sub 2/R/sub 3/ or c/sub 6/r/sub 6/.

• Research Organization: Univ. of California, Berkeley
• OSTI ID: 6761074
• Journal Information: Biophys. J.; (United States), Journal Name: Biophys. J.; (United States) Vol. 32:1; ISSN BIOJA
• Country of Publication: United States
• Language: English

Related Subjects

550200* -- Biochemistry
551000 -- Physiological Systems
59 BASIC BIOLOGICAL SCIENCES
BACTERIA
BIOLOGICAL PATHWAYS
BIOSYNTHESIS
CATALYSIS
CHEMICAL REACTIONS
DYNAMIC FUNCTION STUDIES
ENZYME ACTIVITY
ENZYMES
ESCHERICHIA COLI
INTERMEDIATE STRUCTURE
LIGANDS
LYASES
MICROORGANISMS
MOLECULAR STRUCTURE
POLYMERIZATION
STRUCTURAL CHEMICAL ANALYSIS
SYNTHESIS