Pages that link to "Q38648070"
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The following pages link to Escherichia coli aspartate transcarbamoylase: structure, energetics, and catalytic and regulatory mechanisms (Q38648070):
Displaying 31 items.
- Allosteric regulation of catalytic activity: Escherichia coli aspartate transcarbamoylase versus yeast chorismate mutase (Q24548465) (← links)
- From Genome to Structure and Back Again: A Family Portrait of the Transcarbamylases (Q26798133) (← links)
- Cooperativity in monomeric enzymes with single ligand-binding sites (Q27000989) (← links)
- Aspartate transcarbamylase from the hyperthermophilic archaeon Pyrococcus abyssi: thermostability and 1.8A resolution crystal structure of the catalytic subunit complexed with the bisubstrate analogue N-phosphonacetyl-L-aspartate (Q27640353) (← links)
- Structure of the catalytic trimer ofMethanococcus jannaschiiaspartate transcarbamoylase in an orthorhombic crystal form (Q27651925) (← links)
- Structure of the catalytic chain ofMethanococcus jannaschiiaspartate transcarbamoylase in a hexagonal crystal form: insights into the path of carbamoyl phosphate to the active site of the enzyme (Q27681138) (← links)
- Substrate-induced conformational change in a trimeric ornithine transcarbamoylase (Q27742450) (← links)
- Aspartate transcarbamoylase from Pyrococcus abyssi (Q30660152) (← links)
- The molecular basis of ornithine transcarbamylase deficiency: modelling the human enzyme and the effects of mutations (Q33682400) (← links)
- Aspartate transcarbamylase from Escherichia coli: activity and regulation (Q34339261) (← links)
- Ligation alters the pathway of urea-induced denaturation of the catalytic trimer of Escherichia coli aspartate transcarbamylase (Q36278803) (← links)
- Structural similarity between ornithine and aspartate transcarbamoylases of Escherichia coli: characterization of the active site and evidence for an interdomain carboxy-terminal helix in ornithine transcarbamoylase (Q36279754) (← links)
- Aspartate transcarbamylase from the deep-sea hyperthermophilic archaeon Pyrococcus abyssi: genetic organization, structure, and expression in Escherichia coli (Q36868923) (← links)
- 1H NMR studies on the catalytic subunit of aspartate transcarbamoylase (Q37342758) (← links)
- Role of a carboxyl-terminal helix in the assembly, interchain interactions, and stability of aspartate transcarbamoylase (Q37372000) (← links)
- Expression, purification, crystallization and preliminary X-ray diffraction analysis of the aspartate transcarbamoylase domain of human CAD. (Q37374716) (← links)
- Heterotropic interactions in aspartate transcarbamoylase: turning allosteric ATP activation into inhibition as a consequence of a single tyrosine to phenylalanine mutation (Q37608042) (← links)
- Conversion of the allosteric regulatory patterns of aspartate transcarbamoylase by exchange of a single beta-strand between diverged regulatory chains (Q39683463) (← links)
- Expression, purification, crystallization and preliminary X-ray crystallographic studies of a cold-adapted aspartate carbamoyltransferase from Moritella profunda (Q41763059) (← links)
- Dissecting enzyme regulation by multiple allosteric effectors: nucleotide regulation of aspartate transcarbamoylase (Q41872739) (← links)
- Carbamoyl phosphate biosynthesis and partition in pyrimidine and arginine pathways of Escherichia coli. In situ properties of carbamoyl-phosphate synthase, ornithine transcarbamylase and aspartate transcarbamylase in permeabilized cells (Q46204797) (← links)
- Role of Allosteric:Zinc Interdomain Region of the Regulatory Subunit in the Allosteric Regulation of Aspartate Transcarbamoylase fromEscherichia coli (Q47935642) (← links)
- Is substrate inhibition a consequence of allostery in aspartate transcarbamylase? (Q52418466) (← links)
- Functionally Linked Hydration Changes in Escherichia coli Aspartate Transcarbamylase and Its Catalytic Subunit (Q54559812) (← links)
- Domain closure in the catalytic chains of Escherichia coli aspartate transcarbamoylase influences the kinetic mechanism. (Q54610153) (← links)
- Apparent cooperativity for carbamoylphosphate in Escherichia coli aspartate transcarbamoylase only reflects cooperativity for aspartate. (Q54631902) (← links)
- Co-operative interactions between the catalytic sites in Escherichia coli aspartate transcarbamylase. Role of the C-terminal region of the regulatory chains. (Q54706019) (← links)
- Invited Lectures : Overviews Purinergic signalling: past, present and future (Q63977060) (← links)
- Solvent perturbation of the allosteric regulation of aspartate transcarbamylase (Q74768840) (← links)
- Measuring hydration changes of proteins in solution: applications of osmotic stress and structure-based calculations (Q77338396) (← links)
- CAD, A Multienzymatic Protein at the Head of de Novo Pyrimidine Biosynthesis (Q92651162) (← links)