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FruBPase II and ADP-PFK1 are involved in the modulation of carbon flow in the metabolism of carbohydrates in Methanosarcina acetivorans

Author:
Santiago-Martínez, M. Geovanni, Marín-Hernández, Álvaro, Gallardo-Pérez, Juan Carlos, Yoval-Sánchez, Belem, Feregrino-Mondragón, R. Daniela, Rodríguez-Zavala, José S., Pardo, J. Pablo, Moreno-Sánchez, Rafael, Jasso-Chávez, Ricardo
Source:
Archives of biochemistry and biophysics 2019 v.669 pp. 39-49
ISSN:
0003-9861
Subject:
Methanosarcina acetivorans, adenosine monophosphate, adenosine triphosphate, carbohydrates, carbon, dephosphorylation, genes, messenger RNA, metabolism, metabolites, methanogens, phosphorylation, protein content, protein kinases
Abstract:
To enhance our understanding of the control of archaeal carbon central metabolism, a detailed analysis of the regulation mechanisms of both fructose1,6-bisphosphatase (FruBPase) and ADP-phosphofructokinase-1 (ADP-PFK1) was carried out in the methanogen Methanosarcina acetivorans. No correlations were found among the transcript levels of the MA_1152 and MA_3563 (frubpase type II and pfk1) genes, the FruBPase and ADP-PFK1 activities, and their protein contents. The kinetics of the recombinant FruBPase II and ADP-PFK1 were hyperbolic and showed simple mixed-type inhibition by AMP and ATP, respectively. Under physiological metabolite concentrations, the FruBPase II and ADP-PFK1 activities were strongly modulated by their inhibitors. To assess whether these enzymes were also regulated by a phosphorylation/dephosphorylation process, the recombinant enzymes and cytosolic-enriched fractions were incubated in the presence of commercial protein phosphatase or protein kinase. De-phosphorylation of ADP-PFK1 slightly decreased its activity (i.e. Vmax) and did not change its kinetic parameters and oligomeric state. Thus, the data indicated a predominant metabolic regulation of both FruBPase and ADP-PFK1 activities by adenine nucleotides and suggested high degrees of control on the respective pathway fluxes.
Agid:
6453887