Formation of a Complex of the Catalytic Subunit of Pyruvate Dehydrogenase Phosphatase Isoform 1 (PDP1c) and the L2 Domain Forms a Ca2+Binding Site and Captures PDP1c as a Monomer†

Biochemistry ◽  
2004 ◽  
Vol 43 (47) ◽  
pp. 15073-15085 ◽  
Author(s):  
Ali Turkan ◽  
Yasuaki Hiromasa ◽  
Thomas E. Roche
Keyword(s):  
Binding Site ◽  
Pyruvate Dehydrogenase ◽  
Catalytic Subunit ◽  
Pyruvate Dehydrogenase Phosphatase

One-Step Purification of the Recombinant Catalytic Subunit of Pyruvate Dehydrogenase Phosphatase

2000 ◽  
Vol 20 (1) ◽  
pp. 128-131 ◽  
Author(s):  
Wahn Soo Choi ◽  
Jiangong Yan ◽  
Diane B. McCarthy ◽  
Seung Hee Park ◽  
Lester J. Reed
Keyword(s):  
Pyruvate Dehydrogenase ◽  
Catalytic Subunit ◽  
One Step ◽  
Pyruvate Dehydrogenase Phosphatase

scholarly journals Crystal structure of the catalytic subunit of bovine pyruvate dehydrogenase phosphatase

2020 ◽  
Vol 76 (7) ◽  
pp. 292-301
Author(s):  
Youzhong Guo ◽  
Weihua Qiu ◽  
Thomas E. Roche ◽  
Marvin L. Hackert
Keyword(s):  
Crystal Structure ◽  
Pyruvate Dehydrogenase ◽  
Pyruvate Dehydrogenase Complex ◽  
Ion Pairs ◽  
Catalytic Subunit ◽  
Regulatory Subunit ◽  
Amino Acid Residues ◽  
Cell Parameters ◽  
Twofold Symmetry Axis ◽  
Pyruvate Dehydrogenase Phosphatase

Mammalian pyruvate dehydrogenase (PDH) activity is tightly regulated by phosphorylation and dephosphorylation, which is catalyzed by PDH kinase isomers and PDH phosphatase isomers, respectively. PDH phosphatase isomer 1 (PDP1) is a heterodimer consisting of a catalytic subunit (PDP1c) and a regulatory subunit (PDP1r). Here, the crystal structure of bovine PDP1c determined at 2.1 Å resolution is reported. The crystals belonged to space group P3221, with unit-cell parameters a = b = 75.3, c = 173.2 Å. The structure was solved by molecular-replacement methods and refined to a final R factor of 21.9% (R free = 24.7%). The final model consists of 402 of a possible 467 amino-acid residues of the PDP1c monomer, two Mn2+ ions in the active site, an additional Mn2+ ion coordinated by His410 and His414, two MnSO4 ion pairs at special positions near the crystallographic twofold symmetry axis and 226 water molecules. Several new features of the PDP1c structure are revealed. The requirements are described and plausible bases are deduced for the interaction of PDP1c with PDP1r and other components of the pyruvate dehydrogenase complex.

Sub-mitochondrial localization of the catalytic subunit of pyruvate dehydrogenase phosphatase

FEBS Letters ◽  
1997 ◽  
Vol 401 (2-3) ◽  
pp. 158-162 ◽  
Author(s):  
Cédric Simonot ◽  
Fabienne Lerme ◽  
Pierre Louisot ◽  
Odile Gateau-Roesch
Keyword(s):  
Pyruvate Dehydrogenase ◽  
Catalytic Subunit ◽  
Mitochondrial Localization ◽  
Pyruvate Dehydrogenase Phosphatase

scholarly journals Pyruvate dehydrogenase phosphatase catalytic subunit 2 limits Th17 differentiation

2018 ◽  
Vol 115 (37) ◽  
pp. 9288-9293 ◽  
Author(s):  
Michihito Kono ◽  
Nobuya Yoshida ◽  
Kayaho Maeda ◽  
Nicole E. Skinner ◽  
Wenliang Pan ◽  
...  
Keyword(s):  
T Cells ◽  
Lupus Erythematosus ◽  
Pyruvate Dehydrogenase ◽  
Th17 Cells ◽  
Active Form ◽  
Lactate Production ◽  
Catalytic Subunit ◽  
Th17 Differentiation ◽  
Pyruvate Dehydrogenase Phosphatase

Th17 cells favor glycolytic metabolism, and pyruvate dehydrogenase (PDH) is the key bifurcation enzyme, which in its active dephosphorylated form advances the oxidative phosphorylation from glycolytic pathway. The transcriptional factor, inducible cAMP early repressor/cAMP response element modulator (ICER/CREM), has been shown to be induced in Th17 cells and to be overexpressed in CD4+ T cells from the patients with systemic lupus erythematosus (SLE). We found that glycolysis and lactate production in in vitro Th17-polarized T cells was reduced and that the expression of pyruvate dehydrogenase phosphatase catalytic subunit 2 (PDP2), an enzyme that converts the inactive PDH to its active form, and PDH enzyme activity were increased in Th17 cells from ICER/CREM-deficient animals. ICER was found to bind to the Pdp2 promoter and suppress its expression. Furthermore, forced expression of PDP2 in CD4+ cells reduced the in vitro Th17 differentiation, whereas shRNA-based suppression of PDP2 expression increased in vitro Th17 differentiation and augmented experimental autoimmune encephalomyelitis. At the translational level, PDP2 expression was decreased in memory Th17 cells from patients with SLE and forced expression of PDP2 in CD4+ T cells from lupus-prone MRL/lpr mice and patients with SLE suppressed Th17 differentiation. These data demonstrate the direct control of energy production during Th17 differentiation in health and disease by the transcription factor ICER/CREM at the PDH metabolism bifurcation level.

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