Written in English
|Other titles||Structure-function analyses in Escherichia coli aspartate transcarbamylase|
|Statement||by Kenneth Andrew Smith.|
|Contributions||Boston College. Dept. of Chemistry.|
|The Physical Object|
|Pagination||136 leaves :|
|Number of Pages||136|
Escherichia coli aspartate transcarbamoylase (ATCase, EC ) catalyzes the committed step of the pyrimidine nucleotide biosynthesis pathway: the condensation of carbamoyl phosphate (CP) and L-aspartate (Asp) to form N-carbamoyl-L-aspartate (CA) and phosphate (P i).The end products of the pyrimidine biosynthetic pathway, CTP and UTP in the presence of CTP, Cited by: 6. Aspartate Transcarbamylase Quaternary Structure Among the many structurally interesting proteins, aspartate transcarbamylase (ATCase) attracted special attention. It catalyzes the first committed step in pyrimidine biosynthesis and a number of metabolites alter its enzymatic activity in physiologically meaningful ways. A large collection of mutant versions of Escherichia coli aspartate transcarbamylase (carbamoylphosphate: l-aspartate carbamoyltransferase, EC Cited by: Aspartate transcarbamoylase from Escherichia coli has become a model system for the study of both homotropic and heterotropic interactions in proteins. Analysis of the X-ray structures of the enzyme in the absence and presence of substrates and substrate analogs has revealed sets of interactions that appear to stabilize either the ‘T’ of the ‘R’ states of the enzyme.
Superproduction and rapid purification of Escherichia coli aspartate transcarbamylase and its catalytic subunit under extreme derepression of the pyrimidine pathway. J Biol Chem. Nov 25; (27)– Gerhart JC, Holoubek H. The purification of aspartate transcarbamylase of Escherichia coli and separation of its protein subunits. Mammalian aspartate transcarbamylase (ATCase) is part of a kDa multidomain polypeptide, called CAD, that catalyzes the first three steps in de novo pyrimidine biosynthesis. The structural organization of the mammalian enzyme is very different from E. coli ATCase, a dodecameric, monofunctional molecule comprised of six copies of separate. R. Cunin, A. Jacobs, D. Charlier, M. Crabeel, and G. Hérve. Structure-function relationship in allosteric aspartate carbamoyltransferase from Escherichia coli I. Primary structure of a pyrI gene encoding a modified regulatory subunit. J. Mol. Biol. –13 (). PubMed CrossRef Google Scholar. 4fyw: GM Cockrell & ER Kantrowitz () Metal ion involvement in the allosteric mechanism of Escherichia coli aspartate transcarbamoylase. Biochemis WN Lipscomb & ER Kantrowitz () Structure and mechanisms of Escherichia coli aspartate transcarbamylase. Accounts of Chemical Resea
Escherichia coli aspartate transcarbamoylase (ATCase) is the textbook example of an enzyme that regulates a metabolic pathway—namely, pyrimidine nucleotide biosynthesis—by feedback control and by the cooperative binding of the substrate, l-aspartate. The catalytic and regulatory mechanisms of this enzyme have been extensively studied. Abstract. Aspartate transcarbamylase of Escherichia coli [EC ] is a member of a special class of enzymes that not only catalyzes a cellular reaction but also controls the rate of a metabolic pathway. The enzymes in this class are usually large, each composed of more than one polypeptide chain, and catalyze a reaction at or near the beginning of a metabolic pathway. Subunit Structure of Aspartate Transcarbamylase from Escherichia coli* (Received for publication, Septem ) JURG P. ROSENBUSCH$ AND Kuus WEBER Prom the Biological Laboratories, Harvard University, Cambridge, Massachusetts SUMMARY 1. The molecular weights of the catalytic and regulatory. to 5-fold. Immunochemical studies indicated very little similarity between B. subtilis and E. coli aspartate transcarbamylase or E. coli aspartate transcarbamylase catalytic subunit. Aspartate transcarbamoylase (EC ) catalyzes the first committed step in .