Roles of nucleotide substructures in the regulation of cystathionine β-synthase domain-containing pyrophosphatase

• Published in: Biochimica et biophysica acta. General subjects Vol. 1863; no. 8; pp. 1263 - 1269
• Main Authors: Anashkin, Viktor A., Aksenova, Vera A., Vorobyeva, Natalya N., Baykov, Alexander A.
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.08.2019
• Subjects: active sites; Adenine; Adenine Nucleotides - chemistry; Adenosine; adenosine diphosphate; adenosine monophosphate; adenosine triphosphate; Allosteric regulation; bacteria; cAMP; CBS domain; cyclic AMP; cystathionine; cystathionine beta-synthase; Cystathionine beta-Synthase - chemistry; Cystathionine beta-Synthase - metabolism; Desulfitobacterium; Enzyme Activation; enzyme activity; fluorescence; Fluorescence Resonance Energy Transfer; Fructose-1-phosphate; inorganic pyrophosphatase; Ligands; moieties; phosphates; Protein Binding; proteins; Pyrophosphatases - chemistry; Pyrophosphatases - metabolism; ribose; Adenosine; Adenine; PPi; CBS-PPase; CBS-protein; CBS domain; cAMP; Fructose-1-phosphate; cpPPase; Fru-1-P; Allosteric regulation; CBS; Mant-AMP; Pi; FRET; dhPPase; PPase

Regulatory cystathionine β-synthase (CBS) domains are ubiquitous in proteins, yet their mechanism of regulation remains largely obscure. Inorganic pyrophosphatase which contains regulatory CBS domains as internal inhibitors (CBS-PPase) is activated by ATP and inhibited by AMP and ADP; nucleotide bin...