mitochondrial proteins, Pkp2 (Ygl059wp) and Ppp2 (Ycr079wp), are engaged in the regulation of the pyruvate dehydrogenase complex by affecting the phosphorylation state of subunit Pda1. Ppp2 is almost exclusively localized in the mitochondrial matrix and associated with the complex. Cells lacking Ppp2 but also cells with a non-functional pyruvate dehydrogenase complex due to deletion of Pda1 possess similar sensitivity toward rapamycin
within the pyruvate dehydrogenase complex, the E1 enzyme pyruvate dehydrogenase (PDH) is the main regulatory site and is subject to inhibitory phosphorylation. Total PDH content does not change significantly during hibernation in any tissue but phospho-PDH content increases in all. Heart PDH shows increased phosphorylation at the three sites S232, S293, S300 by 8.1-, 10.6- and 2.1fold, respectively. Liver also shows elevated phospho-S300 (2.5fold) and phospho-S293 (4.7fold) content. Phosphorylation of S232 and S293 increases significantly in brain and lung but only S232 phosphorylation increases in kidney and skeletal muscle
both subunits PDHA and PDHB are surface-exposed immunogenic proteins of Mycoplasma gallisepticum. The mouse anti-PDHA and anti-PDHB sera kill 48.0% and 75.1% of mycoplasmas, respectively. A combination of PDHA and PDHB antisera has a mean bactericidal rate of 65.2%. Both PDHA and PDHB adhere to DF-1 chicken embryo fibroblast cells and adherence is significantly inhibited by antisera against PDHA and PDHB. Both PDHA and PDHB are plasminogen-binding proteins
during lactate consumption, component E1 subunit alpha Ser293 and Ser300 phosphorylation levels are 33% higher compared to the phase of glucose excess. At the same time, the relative phosphorylation level of Ser232 increases steadily throughout the cultivation (66% increase overall). The intracellular pyruvate accumulates only during the period of high lactate production, while acetyl-CoA shows nearly no accumulation
high salt intake downregulates sirtuin SIRT3 level in brown adipose tissue, accompanied by decreased oxygen consumption rate, and causes a severe loss of brown adipose tissue characteristics. SIRT3 interacts with pyruvate dehydrogenase E1alpha (PDHA1) and deacetylates residue Lys83 both in vitro and in vivo under high salt intake. In parallel, high salt intake suppresses salt-induced kinase (Sik) 2 phosphorylation. Silencing Sik2 further diminishes SIRT3 activity and enhances acetylation of PDHA1 K83. Reconstruction of SIRT3 restores PDH activity and thermogenic markers expression in differentiated brown adipocytes from SIRT3 knockout mice
mitochondrial PDC E1 contributes to polar auxin transport during organ development. MAB1 encodes a mitochondrial PDC E1beta subunit that can form both a homodimer and a heterodimer with alpha-subunit IAR4. The MAB1 mutation impairs MAB1 homodimerization, reduces the abundance of IAR4 and IAR4L, weakens PDC enzymatic activity, and diminishes mitochondrial respiration. Mutation leads to significant changes in metabolites including amino acids, and an accumulation of Ala. In MAB1 mutants and seedlings where the TCA cycle is pharmacologically blocked, reduced abundance of the PIN-FORMED (PIN) auxin efflux carriers is found
mutation of promoter binding protein SPL16/GW8 leads to upregulation of pyruvate kinase, pyruvate dehydrogenase E1, dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex, acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial pyruvate carrier, 4-hydroxyphenylpyruvate dioxygenase, and dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex. SPL16 mutations have the potential to boost the grain yield of rice
nitric oxide produced by murine macrophages is responsible for TCA cycle alterations and citrate accumulation associated with polarization. Inflammatory macrophages reroute pyruvate away from pyruvate dehydrogenase in an NO-dependent and hypoxia-inducible factor Hif1alpha-independent manner, thereby promoting glutamine-based anaplerosis
recombinant subunits PdhA and PdhB show binding activity with chicken plasminogen and human fibronectin. Rabbit anti-PdhA and anti-PdhB sera have distinct mycoplasmacidal efficacy in the presence of guinea pig complement, and the adherence of Mycoplasma synoviae to DF-1 cells pretreated with plasminogen is effectively inhibited by treatment with anti-rPdhA or anti-PdhB sera
the pyruvate dehydrogenase complex PDC displays size versatility in an ionic strength-dependent manner. Yeast PDC is a salt-labile complex that dissociates into submegadalton individual components even under physiological ionic strength. The ionic strength can modulate its catalytic activity
the pyruvate dehydrogenase complex PDC displays size versatility in an ionic strength-dependent manner. Yeast PDC is a salt-labile complex that dissociates into submegadalton individual components even under physiological ionic strength. The ionic strength can modulate its catalytic activity
recombinant subunits PdhA and PdhB show binding activity with chicken plasminogen and human fibronectin. Rabbit anti-PdhA and anti-PdhB sera have distinct mycoplasmacidal efficacy in the presence of guinea pig complement, and the adherence of Mycoplasma synoviae to DF-1 cells pretreated with plasminogen is effectively inhibited by treatment with anti-rPdhA or anti-PdhB sera
both subunits PDHA and PDHB are surface-exposed immunogenic proteins of Mycoplasma gallisepticum. The mouse anti-PDHA and anti-PDHB sera kill 48.0% and 75.1% of mycoplasmas, respectively. A combination of PDHA and PDHB antisera has a mean bactericidal rate of 65.2%. Both PDHA and PDHB adhere to DF-1 chicken embryo fibroblast cells and adherence is significantly inhibited by antisera against PDHA and PDHB. Both PDHA and PDHB are plasminogen-binding proteins