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Information on EC 3.1.3.43 - [pyruvate dehydrogenase (acetyl-transferring)]-phosphatase
for references in articles please use BRENDA:EC3.1.3.43
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EC Tree 3 Hydrolases
3.1 Acting on ester bonds
3.1.3 Phosphoric-monoester hydrolases
3.1.3.43 [pyruvate dehydrogenase (acetyl-transferring)]-phosphatase
IUBMB Comments
A mitochondrial enzyme associated with EC 1.2.4.1 pyruvate dehydrogenase (acetyl-transferring), in the pyruvate dehydrogenase complex.
The enzyme appears in viruses and cellular organisms
- 3.1.3.43
- acetyl-coa
- acetyltransferase
- biliary
-
lipoylated
- cirrhosis
- dihydrolipoamide
- thiamin
- acidosis
-
multienzyme
-
dihydrolipoyl
- dichloroacetate
- autoimmune
-
tricarboxylic
- pdc-e2
- autoantibody
-
lipoic
- autoantigens
- pyrophosphate
- transacetylase
-
antimitochondrial
-
branched-chain
- alpha-ketoglutarate
- 2-oxoglutarate
- lipoate
- leigh
- pdha1
- carnitine
- e1alpha
- cholangitis
- tpp
-
ketogenic
-
subcomplexes
-
warburg
- azotobacter
-
alpha-keto
-
intramitochondrial
-
immunodominant
- vinelandii
- acetylcarnitine
-
acidemia
- alpha-ketoacids
-
autoreactive
- 2-oxoacid
-
pentagonal
- coash
-
phosphorylation-dephosphorylation
- succinyltransferase
-
icosahedral
- melas
- medicine
- molecular biology
-
alpha2beta2
Reaction Schemes
showSynonyms
pyruvate dehydrogenase complex, pyruvate dehydrogenase phosphatase, pdh phosphatase, pyruvate dehydrogenase phosphate phosphatase, pyruvate dehydrogenase phosphatase 1, pda1p, pyruvate dehydrogenase phosphatase 2, pyruvate dehydrogenase phosphatase isoform 1, yor090cp, phosphopyruvate dehydrogenase phosphatase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Pda1p
PDC
PDH phosphatase
PDP
PDP1
PDP2
phosphatase, pyruvate dehydrogenase
-
-
-
-
phosphopyruvate dehydrogenase phosphatase
-
-
-
-
pyruvate dehydrogenase complex
pyruvate dehydrogenase phosphatase
pyruvate dehydrogenase phosphatase 1
pyruvate dehydrogenase phosphate phosphatase
-
-
-
-
Yor090cp
[pyruvate dehydrogenase (acetyl-transferring)]-phosphatase
[pyruvate dehydrogenase (lipoamide)]-phosphatase
-
-
-
-
[pyruvate dehydrogenase (lipoamide)]-phosphate phosphohydrolase
-
-
-
-
pyruvate dehydrogenase phosphatase
-
-
-
-
[pyruvate dehydrogenase (acetyl-transferring)]-phosphatase
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
[pyruvate dehydrogenase (acetyl-transferring)] phosphate + H2O = [pyruvate dehydrogenase (acetyl-transferring)] + phosphate
[pyruvate dehydrogenase (acetyl-transferring)] phosphate + H2O = [pyruvate dehydrogenase (acetyl-transferring)] + phosphate
-
-
-
-
[pyruvate dehydrogenase (acetyl-transferring)] phosphate + H2O = [pyruvate dehydrogenase (acetyl-transferring)] + phosphate
mechanism, overview
-
[pyruvate dehydrogenase (acetyl-transferring)] phosphate + H2O = [pyruvate dehydrogenase (acetyl-transferring)] + phosphate
mechanism, difference in specificity of isoforms
-
[pyruvate dehydrogenase (acetyl-transferring)] phosphate + H2O = [pyruvate dehydrogenase (acetyl-transferring)] + phosphate
overview on mechanism and regulation of enzyme
-
[pyruvate dehydrogenase (acetyl-transferring)] phosphate + H2O = [pyruvate dehydrogenase (acetyl-transferring)] + phosphate
mechanism
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
additional information
hydrolysis of phosphoric ester
-
-
-
-
additional information
-
PDP activity and protein content is higher in fast-twitch oxidative glycolytic muscles, food deprivation decreases PDP activity in all muscle types, PDP2 declines in fast-twitch oxidative glycolytic muscle
additional information
PDP1 belongs to the PPM family of protein serine/threonine phosphatases
additional information
-
PDP activity and protein content is higher in fast-twitch oxidative glycolytic muscles, food deprivation decreases PDP activity in all muscle types, PDP2 declines in fast-twitch oxidative glycolytic muscle
-
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SYSTEMATIC NAME
IUBMB Comments
[pyruvate dehydrogenase (acetyl-transferring)]-phosphate phosphohydrolase
A mitochondrial enzyme associated with EC 1.2.4.1 pyruvate dehydrogenase (acetyl-transferring), in the pyruvate dehydrogenase complex.
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CAS REGISTRY NUMBER
COMMENTARY
9073-70-5
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
peptide T-1
?
-
Substrates: phosphopeptide produced by tryptic digestion of phosphorylated pyruvate dehydrogenase
Products: -
Products: -
?
[mothers against decapentaplegic]-phosphate + H2O
[mothers against decapentaplegic] + phosphate
-
Substrates: PDP1 directly dephosphorylates mothers against decapentaplegic (MAD) and inhibits signal transduction of decapentaplegic (DPP)
Products: -
Products: -
?
[Pda1]-phosphate + H2O
[Pda1] + phosphate
-
Substrates: enzyme acts on residue S313 of pyruvate dehydrogenase complex E1alpha subunit Pda1
Products: -
Products: -
?
[pyruvate dehydrogenase (acetyl-transferring)] phosphate + H2O
[pyruvate dehydrogenase (acetyl-transferring)] + phosphate
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
[pyruvate dehydrogenase (acetyl-transferring)] phosphate + H2O
[pyruvate dehydrogenase (acetyl-transferring)] + phosphate
Substrates: -
Products: -
Products: -
?
[pyruvate dehydrogenase (acetyl-transferring)] phosphate + H2O
[pyruvate dehydrogenase (acetyl-transferring)] + phosphate
-
Substrates: -
Products: -
Products: -
?
[pyruvate dehydrogenase (acetyl-transferring)] phosphate + H2O
[pyruvate dehydrogenase (acetyl-transferring)] + phosphate
-
Substrates: -
Products: -
Products: -
?
[pyruvate dehydrogenase (acetyl-transferring)] phosphate + H2O
[pyruvate dehydrogenase (acetyl-transferring)] + phosphate
Substrates: -
Products: -
Products: -
?
[pyruvate dehydrogenase (acetyl-transferring)] phosphate + H2O
[pyruvate dehydrogenase (acetyl-transferring)] + phosphate
-
Substrates: -
Products: -
Products: -
?
[pyruvate dehydrogenase (acetyl-transferring)] phosphate + H2O
[pyruvate dehydrogenase (acetyl-transferring)] + phosphate
-
Substrates: -
Products: -
Products: -
?
[pyruvate dehydrogenase (acetyl-transferring)] phosphate + H2O
[pyruvate dehydrogenase (acetyl-transferring)] + phosphate
Substrates: -
Products: -
Products: -
?
[pyruvate dehydrogenase (acetyl-transferring)] phosphate + H2O
[pyruvate dehydrogenase (acetyl-transferring)] + phosphate
-
Substrates: -
Products: -
Products: -
?
[pyruvate dehydrogenase (acetyl-transferring)] phosphate + H2O
[pyruvate dehydrogenase (acetyl-transferring)] + phosphate
-
Substrates: -
Products: -
Products: -
?
[pyruvate dehydrogenase (acetyl-transferring)] phosphate + H2O
[pyruvate dehydrogenase (acetyl-transferring)] + phosphate
-
Substrates: -
Products: -
Products: -
?
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
?
-
Substrates: -
Products: -
Products: -
?
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
?
-
94880, 94881, 94884, 94886, 94887, 94888, 94889, 94890, 94893, 94901, 94902, 94905, 94909, 94910, 94911, 94913, 94915, 94917, 94918, 94920
Substrates: -
Products: -
Products: -
?
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
?
-
Substrates: -
Products: -
Products: -
?
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
?
-
Substrates: -
Products: -
Products: -
?
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
?
-
Substrates: -
Products: -
Products: -
?
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
?
-
Substrates: -
Products: -
Products: -
?
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
?
-
Substrates: -
Products: -
Products: -
?
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
?
Substrates: -
Products: -
Products: -
?
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
?
-
Substrates: -
Products: -
Products: -
?
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
?
-
Substrates: -
Products: -
Products: -
?
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
-
Substrates: -
Products: -
Products: -
ir
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
-
94880, 94881, 94884, 94886, 94887, 94888, 94889, 94890, 94893, 94901, 94902, 94905, 94909, 94911, 94913, 94915, 94917, 94918, 94920
Substrates: -
Products: -
Products: -
ir
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
-
Substrates: -
Products: -
Products: -
?
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
-
Substrates: presence of EGTA or Ca2+ and transacetylase
Products: -
Products: -
ir
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
-
Substrates: -
Products: -
Products: -
?
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
Substrates: -
Products: -
Products: -
?
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
-
Substrates: -
Products: -
Products: -
ir
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
-
Substrates: -
Products: -
Products: -
?
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
-
Substrates: pyruvate dehydrogenase activity is only 25% in patients carrying a deletion mutation of L213 of PDP1
Products: -
Products: -
?
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
-
Substrates: -
Products: -
Products: -
ir
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
-
Substrates: -
Products: -
Products: -
?
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
-
Substrates: -
Products: -
Products: -
ir
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
-
Substrates: -
Products: -
Products: -
ir
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
-
Substrates: -
Products: -
Products: -
ir
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
Substrates: -
Products: -
Products: -
ir
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
-
Substrates: -
Products: -
Products: -
ir
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
-
Substrates: -
Products: -
Products: -
?
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
-
Substrates: -
Products: -
Products: -
ir
additional information
?
-
-
Substrates: dephosphorylation of substrate and substrate mutants R234Q, R234G occurs at similar rates at phosphorylation sites 1 and 2, the rate of dephosphorylation of site 3 is about 50% of wild type in substrate mutant R234Q
Products: -
Products: -
?
additional information
?
-
-
Substrates: different conditions for binding of isoforms to substrate, both isoforms can dephosphorylate all three phosphorylation sites of substrate in a random mechanism
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
[pyruvate dehydrogenase (acetyl-transferring)] phosphate + H2O
[pyruvate dehydrogenase (acetyl-transferring)] + phosphate
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
[pyruvate dehydrogenase (acetyl-transferring)] phosphate + H2O
[pyruvate dehydrogenase (acetyl-transferring)] + phosphate
-
Substrates: -
Products: -
Products: -
?
[pyruvate dehydrogenase (acetyl-transferring)] phosphate + H2O
[pyruvate dehydrogenase (acetyl-transferring)] + phosphate
Substrates: -
Products: -
Products: -
?
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
?
-
Substrates: -
Products: -
Products: -
?
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
?
-
94880, 94881, 94884, 94886, 94887, 94888, 94889, 94890, 94893, 94901, 94902, 94905, 94909, 94910, 94911, 94913, 94915, 94917, 94918, 94920
Substrates: -
Products: -
Products: -
?
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
?
-
Substrates: -
Products: -
Products: -
?
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
?
-
Substrates: -
Products: -
Products: -
?
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
?
-
Substrates: -
Products: -
Products: -
?
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
?
-
Substrates: -
Products: -
Products: -
?
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
?
-
Substrates: -
Products: -
Products: -
?
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
?
Substrates: -
Products: -
Products: -
?
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
?
-
Substrates: -
Products: -
Products: -
?
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
?
-
Substrates: -
Products: -
Products: -
?
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
-
Substrates: -
Products: -
Products: -
?
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
-
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
KCl
Mg2+
Mn2+
Ca2+
-
Km: 0.0438 mM, fully phosphorylated pyruvate dehydrogenase complex, Km: 0.0156 mM partially phosphorylated
Ca2+
-
increase in Mg2+ concentration decreases the Ca2+ concentration needed for half-maximal activation of PDB1 from 3 microM to 1 microM
Ca2+
the addition of 0.1 mM Ca2+ alone gives a 6fold increase in basal PDP activity
Ca2+
PDP1 is highly enhanced through Ca2+-dependent binding of PDP1c to the inner lipoyl domain L2 of the dihydrolipoyl acetyltransferase E2
Ca2+
-
Km: 0.116 mM, fully phosphorylated pyruvate dehydrogenase complex, Km: 0.0266 mM, partially phosphorylated
Mg2+
-
Km: 0.59 mM, partially and fully phosphorylated pyruvate dehydrogenase complex
Mg2+
-
increase in Mg2+ concentration decreases the Ca2+ concentration needed for half-maximal activation of PDB1 from 3 microM to 1 microM
Mg2+
-
two molecules per active site of each isoform, regulation of enzyme activity via effector-altered sensitivities to Mg2+-level
Mg2+
-
required, Km-value of PDP1 is 2 mM in absence and 0.4 mM in presence of spermine, Km-value of PDP2 is 16 mM in absence and 3 mM in presence of spermine
Mg2+
-
insulin increases sensivity to Mg2+ of pyruvate dehydrogenase phosphatase
Mg2+
sensivity of subunit pyruvate dehydrogenase phosphatase 1 10fold higher than of pyruvate dehydrogenase phosphatase 2
Mg2+
Km: 0.7 mM for pyruvate dehydrogenase phosphatase 1, Km: 17.4 mM for pyruvate dehydrogenase phosphatase 2
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(R)-dehydrolipoic acid
-
30% inhibition at 5 mM on phosphorylation at site 1 of E1, 20% inhibition at 5 mM on phosphorylation at site 2 of E1, 25% inhibition at 5 mM on phosphorylation at site 3 of E1
(R)-lipoic acid
-
30% inhibition at 5 mM on phosphorylation at site 1 of E1, 20% inhibition at 5 mM on phosphorylation at site 2 of E1, 25% inhibition at 5 mM on phosphorylation at site 3 of E1
(S)-lipoic acid
-
30% inhibition at 5 mM on phosphorylation at site 1 of E1, 20% inhibition at 5 mM on phosphorylation at site 2 of E1, 25% inhibition at 5 mM on phosphorylation at site 3 of E1
myo-inositol cyclic 1,2-inositol phosphate phosphoglycan
-
from human plasma, antagonist of insulin, inhibits Mg2+ and spermine stimulation
-
Zn2+
about 20% decrease of activity in the presence of 0.01 mM Zn2+; about 20% decrease of activity in the presence of 0.01 mM Zn2+
additional information
obesity results in a 46% decrease in PDP activity while PDP isoform content is unchanged, 8 weeks of endurance training lead to a significant 1.4-2.2fold increase in isoform PDP1 activity of all muscle examined from obese rats; obesity results in a 46% decrease in PDP activity while PDP isoform content is unchanged, isoform PDP2 protein content is not affected by obesity or training
-
additional information
obesity results in a 46% decrease in PDP activity while PDP isoform content is unchanged, 8 weeks of endurance training lead to a significant 1.4-2.2fold increase in isoform PDP1 activity of all muscle examined from obese rats; obesity results in a 46% decrease in PDP activity while PDP isoform content is unchanged, isoform PDP2 protein content is not affected by obesity or training
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1S)-1,5-anhydro-1-{[(1R,2R,3R,4S,5S,6S)-2,3,4,5-tetrahydroxy-6-methoxycyclohexyl]methyl}-D-galactitol
-
i.e. C-INS-2-OH the deaminated analogue of C-INS-2
(1S)-2-amino-1,5-anhydro-2-deoxy-1-{[(1R,2R,3R,4S,5S,6S)-2,3,4,5-tetrahydroxy-6-methoxycyclohexyl]methyl}-D-galactitol
-
i.e. C-INS-2, the C-glycoside of INS-2
4-O-beta-D-galactosaminyl-3-O-methyl-D-chiro-inositol
-
i.e. INS-2, allosteric activation, docking study using crystal structure of the enzyme PDHP1, PDB ID 2PNQ, and mechanism, overview
inner lipoyl domain of dihydrolipoyl acetyltransferase
-
component of substrate complex, structural requirements for binding and activation
-
Ca2+
-
for isozyme PDP1c, simultaneous presence of Ca2+ and E2 component of substrate is required
Insulin
-
with starved rats pretreated with dichloroacetate or 2-tetradecylglycidate
-
additional information
-
overview on interactions of Ca2+, Mg2+, spermine, and enzyme subunits
-
additional information
-
Pkp2p (Ygl059wp) and Ppp2p (Ycr079wp), but not Yhr076w, are engaged in the regulation of the pyruvate dehydrogenase complex by affecting the phosphorylation state of subunit Pda1p
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.625
peptide T-1
-
phosphopeptide produced by tryptic digestion of phosphorylated pyruvate dehydrogenase
-
0.029
[Pyruvate dehydrogenase (lipoamide)]-phosphate
-
presence of Ca2+ and transacetylase
-
0.058
[Pyruvate dehydrogenase (lipoamide)]-phosphate
-
presence of EGTA and transacetylase
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0044
-
in soleus muscles, in food-deprived rats, extracted mitochondrial protein
0.0051
-
in white gastrocnemius, in food-deprived rats, extracted mitochondrial protein
0.0057
-
in red gastrocnemius, in food-deprived rats, extracted mitochondrial protein
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
94880, 94886, 94887, 94888, 94889, 94890, 94893, 94902, 94905, 94909, 94910, 94911, 94913, 94915, 94917, 94918, 94920, 652240, 667592, 698844
-
-
brenda
reactivation of the pyruvate dehydrogenase complex from Saccharomyces cerevisiae
-
-
brenda
-
-
-
brenda
Otsuka Long-Evans Tokushima Fatty (OLETF) rat, spontaneously diabetic
-
-
brenda
wild type strain BY4741, mutant strain yor090c lacking pyruvate dehydrogenase phosphatase
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
the enzyme is overexpressed in pancreatic adenocarcinoma samples compared with normal pancreatic samples
brenda
the enzyme is overexpressed in pancreatic adenocarcinoma samples compared with normal pancreatic samples
brenda
-
pyruvate dehydrogenase subunit PDHA1 and pyruvate dehydrogenase phosphatase PDP1 are frequently amplified and overexpressed at both the gene and protein levels in prostate tumors
brenda
-
-
94880, 94881, 94884, 94886, 94887, 94888, 94889, 94890, 94893, 94901, 94909, 94910, 94913, 94918, 698844
brenda
-
-
brenda
-
soleus slow-twitch oxidative, RG, red gastrocnemius fast-twitch oxidative glycolytic, and WG, white gastrocnemius fast-twitch glycolytic muscles
brenda
PDP1 is the predominant isoform expressed in skeletal muscle
brenda
-
soleus slow-twitch oxidative, RG, red gastrocnemius fast-twitch oxidative glycolytic, and WG, white gastrocnemius fast-twitch glycolytic muscles
-
brenda
-
lower mRNA expression compared to non diabetic control animals
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
-
94881, 94884, 94886, 94888, 94889, 94890, 94893, 94901, 94909, 94910, 94911, 94913, 94917, 94920, 698844
brenda
-
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug target
promising diagnostic and therapeutic target for anti-pancreatic adenocarcinoma treatment
malfunction
metabolism
physiological function
malfunction
high expression of PDP1 correlates with poor overall and disease-free survival of pancreatic adenocarcinoma (PDAC) patients. PDP1 promotes the proliferation, colony formation, and invasion of PDAC cells in vitro and facilitated orthotopic tumor growth in vivo. PDP1 accelerates intracellular ATP production, leading to sufficient energy to support rapid cancer progression. mTOR activation is responsible for the PDP1-induced tumor cell proliferation and invasion in PDAC. AMPK is downregulated by PDP1 overexpression, resulting in mTOR activation and cancer progression
malfunction
silencing of PDP1 down-regulates HIF transcriptional activity and the expression of HIF-dependent genes, including that of PDK1, the kinase that phosphorylates and inactivates PDH, opposing the effects of PDP1
malfunction
defective pyruvate dehydrogenase phosphatase (PDP) leads to pyruvate dehydrogenase complex (PDC) deficiency and congenital lactic acidosis
metabolism
-
the enzyme is involved in the regulation of pyruvate dehydrogenase performing its activating dephosphorylation, together with phosphorylation and inactivation by pyruvate dehydrogenase kinase, PDK. Pyruvate dehydrogenase phosphatase PDP1 activity and expression is positively correlated with citrate synthase activity, regulation, overview
metabolism
the PDP1/PDH/HIF-1/PDK1 axis is part of a homeostatic loop which, under hypoxia, preserves cellular acetyl-CoA production to a level sufficient to sustain chromatin acetylation and transcription of hypoxia-inducible genes
physiological function
-
allosteric activation of pyruvate dehydrogenase phosphatase and protein phosphatase 2Calpha leads to insulin-mimetic and insulin-sensitizing effects
physiological function
-
in embryonic stem cells, Pdp1 expression is 27fold decreased on differentiation day 8 compared to differentiation day 0, accompanied by suppressed mitochondrial indices, including ATP levels, membrane potential, reactive oxygen species and mitochondrial Ca2+. Pdp1 overexpression significantly enhances the mitochondrial indices and pyruvate dehydrogenase activity and reduces the expression of cardiac differentiation marker mRNA and the cardiac differentiation rate. A knockdown of the Pdp1 gene promotes the expression of cardiac differentiation marker mRNA and the cardiac differentiation rate
physiological function
-
Ptc6 interacts with pyruvate dehydrogenase complex E1alpha subunit Pda1. A Ptc6 deletion mutant exhibits a marked increase in Pda1 S313 phosphorylation
physiological function
overexpression of small RNA miR-195 results in enhanced apoptosis, decreased mitochondrial membrane potential and cellular ATP content upon hydrogen peroxide stimulation. The effects can be partially rescued by PDPR or flavin adenine dinucleotide-dependent oxidoreductase domain containing protein FOXRED1. In preeclamptic patients, lowered circulating levels of miR-195 are found at early-to-mid gestation and term pregnancy, and marked increases in FOXRED1 and PDPR expression are observed in the placenta when compared with gestational week-matched controls
physiological function
-
forced expression of pyruvate dehydrogenase phosphatase catalytic subunit PDP2 in CD4+ cells reduces the in vitro Th17 T-cell differentiation, whereas shRNA-based suppression of PDP2 expression increases in vitro Th17 differentiation and augments experimental autoimmune encephalomyelitis
physiological function
-
glycolysis and lactate production in in vitro Th17-polarized T-cells is reduced and the expression of pyruvate dehydrogenase phosphatase catalytic subunit and Pdh enzyme activity are increased in Th17 cells from animals deficient for inducible cAMP early repressor/cAMP response element modulator ICER/CREM. ICER binds to the Pdp2 promoter and suppresses its expression
physiological function
the enzyme plays an important physiological role in energy metabolism
physiological function
PDP1 is a key hormone-regulated metabolic enzyme that dephosphorylates and activates pyruvate dehydrogenase (PDH), thereby stimulating the conversion of pyruvate into acetyl-CoA. PDP1 is a regulator of HIF-dependent transcription and provides a direct link between glucose metabolism, epigenetic regulation and the hypoxic response that may operate in cancer cells
physiological function
pyruvate dehydrogenase phosphatase (PDP) regulates pyruvate dehydrogenase complex (PDC)
Show AA Sequence and Transmembrane Helices (1412 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100000
150000
50000
52000
-
PDP1, 1 * 52000, catalytic subunit,+ 1 * 69000, regulatory subunit, overview
69000
-
PDP1, 1 * 52000, catalytic subunit,+ 1 * 69000, regulatory subunit, overview
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
heterodimer
heterodimer
-
catalytic subunit beloging to the phosphatase 2C class plus regulatory subunit, a flavoprotein, overview, there are two isoforms of the catalytic subunit+++
heterodimer
-
isoform PDP1, composed of catalytic subunit PDP1c and regulatory subunit PDP1r of 96000 Da, overview
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
phosphoprotein
-
Tyr-94 and Tyr-381phosphorylation through FGFR1 inhibit the enzyme activity by blocking lipoic acid binding
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method at 25°C, crystal structure is determined at 2.1 A resolution. The crystals belong to space group P3(2)21, with unit-cell parameters a = b = 75.3, c = 173.2 A
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E93X
the nonsense mutation in the PDP1 gene shows a complete absence of isoform PDP1 protein in mitochondria, PDP2 can compensate for loss of PDP1 protein in a null patient
Y94F
-
phosphorylation-deficient mutant. Expression of the mutant in H-1299 cells leads to decreased proliferation under hypoxia and increased oxidative phosphorylation
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
immobilized metal ion affinity chromatography (Ni2+), gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
an oncogene BRAFV600E-induced senescence is accompanied by induction of the pyruvate dehydrogenase phosphatase 2
-
controlled cortical impact (CCI) induces a significant increase in PDP1 mRNA expression in ipsilateral cerebral cortex at 4 h and 24 h post CCI that return to basal level 72 h post CCI. PDP1 mRNA level increases transiently in ipsilateral hippocampal dentate gyrus and CA1-3 subfields 4 h post CCI
-
inducible cAMP early repressor ICER binds to the Pdp2 promoter and suppresses its expression
-
overexpressed in pancreatic adenocarcinoma samples compared with normal pancreatic samples
PDP1 mRNA expression in thalamus and other subcortical regions decrease persistently post controlled cortical impact
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
molecular biology
medicine
-
starvation and streptozotocin-induced diabetes cause decrease in isoform PDP2 activity and protein amount in heart and kidney, refeeding and insulin treatment resp. restore
medicine
-
pyruvate dehydrogenase phosphatase regulatory subunit expression at baseline and post-training are both correlated with whole body insulin sensitivity
medicine
-
pyruvate dehydrogenase subunit PDHA1 and pyruvate dehydrogenase phosphatase PDP1 are frequently amplified and overexpressed at both the gene and protein levels in prostate tumors
medicine
-
pyruvate dehydrogenase phosphatase catalytic subunit PDP2 expression is decreased in memory Th17 T-cells from patients with systemic lupus erythematosus and forced expression of PDP2 in CD4+ T-cells from patients with systemic lupus erythematosus suppresses Th17 differentiation
molecular biology
-
pyruvate dehydrogenase phosphatase acts as a Smad1 phosphatase and plays a key role Decapentaplegic signalling pathways
molecular biology
-
pyruvate dehydrogenase phosphatase acts as a Smad1 phosphatase and plays a key role TGF-b signalling pathways
molecular biology
-
pyruvate dehydrogenase complex in yeast is regulated by the PDH phosphatase Yor090cp
molecular biology
-
pyruvate dehydrogenase phosphatase acts as a Smad phosphatase and plays a key role in decapentaplegic signalling pathways, reduced Smad1 dephosphorylation after neutralisation of PDP1 or PDP2 with SiRNA
molecular biology
-
pyruvate dehydrogenase phosphatase acts as a Smad1 phosphatase and plays a key role in TGF-b signalling pathways
molecular biology
-
pyruvate dehydrogenase complex in yeast is regulated by the PDH phosphatase Yor090cp
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Rahmatullah, M.; Roche, T.E.
Component requirements for NADH inhibition and spermine stimulation of pyruvate dehydrogenase phosphatase activity
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Bos taurus
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Pyruvate dehydrogenase
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18
77-95
1987
Bos taurus, Neurospora crassa
-
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Miernyk, J.A.; Randall, D.D.
Some properties of pea mitochondrial phospho-pyruvate dehydrogenase-phosphatase
Plant Physiol.
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1987
Lathyrus oleraceus
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Thomas, A.P.; Diggle, T.A.; Denton, R.M.
Sensitivity of pyruvate dehydrogenase phosphate phosphatase to magnesium ions. Similar effects of spermine and insulin
Biochem. J.
238
83-91
1986
Rattus norvegicus, Sus scrofa
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Reed, L.J.; Damuni, Z.; Merryfield, M.L.
Regulation of mammalian pyruvate and branched-chain alpha-keto acid dehydrogenase complexes by phosphorylation-dephosphorylation
Curr. Top. Cell. Regul.
27
41-49
1985
Bos taurus
brenda
Beatty, S.M.; Hamilton, G.A.
Inhibition of pyruvate dehydrogenase and pyruvate dehydrogenase phosphate phosphatase by glyoxylate
Bioorg. Chem.
13
14-23
1985
Rattus norvegicus
-
brenda
Damuni, Z.; Humphreys, J.S.; Reed, L.J.
Stimulation of pyruvate dehydrogenase phosphatase activity by polyamines
Biochem. Biophys. Res. Commun.
124
95-99
1984
Bos taurus
brenda
Pettit, F.H.; Teague, W.M.; Reed, L.J.
Pyruvate dehydrogenase phosphatase from bovine heart
Methods Enzymol.
90
402-407
1982
Bos taurus
brenda
Teague, W.M.; Pettit, F.H.; Wu, T.L.; Silberman, S.R.; Reed, L.J.
Purification and properties of pyruvate dehydrogenase phosphatase from bovine heart and kidney
Biochemistry
21
5585-5592
1982
Bos taurus
brenda
Pratt, M.L.; Maher, J.F.; Roche, T.E.
Purification of bovine kidney and heart pyruvate dehydrogenase phosphatase on Sepharose derivatized with the pyruvate dehydrogenase complex
Eur. J. Biochem.
125
349-355
1982
Bos taurus
brenda
Kerbey, A.L.; Randle, P.J.
Role of multi-site phosphorylation in regulation of pig heart pyruvate dehydrogenase phosphatase
FEBS Lett.
108
485-488
1979
Bos taurus, Sus scrofa
brenda
Roche, T.E.; Cate, R.L.
Purification of porcine liver pyruvate dehydrogenase complex and characterization of its catalytic and regulatory properties
Arch. Biochem. Biophys.
183
664-677
1977
Sus scrofa
brenda
Severson, D.L.; Denton, R.M.; Pask, H.T.; Randle, P.J.
Calcium and magnesium ions as effectors of adipose-tissue pyruvate dehydrogenase phosphate phosphatase
Biochem. J.
140
225-237
1974
Rattus norvegicus, Sus scrofa
brenda
Linn, T.C.; Pelley, J.W.; Pettit, F.H.; Hucho, F.; Randall, D.D.; Reed, L.J.
alpha-Keto acid dehydrogenase complexes. XV. Purification and properties of the component enzymes of the pyruvate dehydrogenase complexes from bovine kidney and heart
Arch. Biochem. Biophys.
148
327-342
1972
Bos taurus
brenda
Siess, E.A.; Wieland, O.H.
Purification and characterization of pyruvate-dehydrogenase phosphatase from pig-heart muscle
Eur. J. Biochem.
26
96-105
1972
Sus scrofa
brenda
McCormack, J.G.; Bromidge, E.S.; Dawes, N.J.
Characterization of the effects of Ca2+ on the intramitochondrial Ca2+-sensitive dehydrogenases within intact rat-kidney mitochondria
Biochim. Biophys. Acta
934
282-292
1988
Rattus norvegicus
brenda
Holness, M.J.; Sugden, M.C.
Is there a role for pyruvate dehydrogenase-phosphatase in the re-activation of hepatic pyruvate dehydrogenase complex after re-feeding?
Biochem. Soc. Trans.
16
773-774
1988
Rattus norvegicus
brenda
Larner, J.; Huang, L.C.; Schwartz, C.F.W.; Oswald, A.S.; Shen, T.Y.; Kinter, M.; Tang, G.; Zeller, K.
Rat liver insulin mediator which stimulates pyruvate dehydrogenase phosphatase contains galactosamine and D-chiroinositol
Biochem. Biophys. Res. Commun.
151
1416-1426
1988
Rattus norvegicus
brenda
Midgley, P.J.W.; Rutter, G.A.; Thomas, A.P.; Denton, R.M.
The control of pyruvate dehydrogenase phosphate phosphatase by Ca2+ and Mg2+ ions
Biochem. Soc. Trans.
15
835-836
1987
Rattus norvegicus
-
brenda
Midgley P.J.W.; Rutter, G.A.; Thomas, A.P.; Denton, R.M.
Effects of Ca2+ and Mg2+ on the activity of pyruvate dehydrogenase phosphate phosphatase within toluene-permeabilized mitochondria
Biochem. J.
241
371-377
1987
Rattus norvegicus
brenda
Holness, M.J.; Sugden, M.C.
Regulation of renal and hepatic pyruvate dehydrogenase complex on carbohydrate re-feeding after starvation
Biochem. J.
241
421-425
1987
Rattus norvegicus
brenda
Uhlinger, D.J.; Yang, C.Y.; Reed, L.J.
Phosphorylation-dephosphorylation of pyruvate dehydrogenase from bakersyeast
Biochemistry
25
5673-5677
1986
Bos taurus
brenda
Mullinax, T.R.; Stepp, L.R.; Brown, J.R.; Reed, L.J.
Synthetic peptide substrates for mammalian pyruvate dehydrogenase kinase and pyruvate dehydrogenase phosphatase
Arch. Biochem. Biophys.
243
655-659
1985
Bos taurus
brenda
Kerbey, A.L.; Randle, P.J.; Kearns, A.
Dephosphorylation of pig heart pyruvate dehydrogenase phosphate complexes by pig heart pyruvate dehydrogenase phosphate phosphatase
Biochem. J.
195
51-59
1981
Sus scrofa
brenda
Baxter, M.A.; Coore, H.G.
Specificity of lactating rat mammary-gland pyruvate dehydrogenase phosphate phosphatase for the phosphorylated residues of the alpha-subunit
Biochem. Soc. Trans.
7
949-950
1979
Rattus norvegicus, Sus scrofa
brenda
Davis, P.F.; Pettit, F.H.; Reed, L.J.
Peptides derived from pyruvate dehydrogenase as substrates for pyruvate dehydrogenase kinase and phosphatase
Biochem. Biophys. Res. Commun.
75
541-549
1977
Bos taurus
brenda
Siess, E.A.; Wieland, O.H.
Cellular distribution of pyruvate dehydrogenase phophatase. Activity in normal, hyperinsulinized and diabetic rats
FEBS Lett.
65
163-168
1976
Rattus norvegicus
brenda
Stansbie, D.; Denton, R.M.; Bridges, B.J.; Pask, H.T.; Randle, P.J.
Regulation of pyruvate dehydrogenase and pyruvate dehydrogenase phosphate phosphatase activity in rat epididymal fat-pads
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154
225-236
1976
Rattus norvegicus
brenda
Kerbey, A.L.; Randle, P.J.; Cooper, R.H.; Whitehouse, S.; Pask, H.T.; Denton, R.M.
Regulation of pyruvate dehydrogenase in rat heart. Mechanism of regulation of proportions of dephosphorylated and phosphorylated enzyme by oxidation of fatty acids and ketone bodies and of effects of diabetes: role of coenzyme A, acetyl-coenzyme A and reduced and oxidized nicotinamide-adenine dinucleotide
Biochem. J.
154
327-348
1976
Rattus norvegicus
brenda
Schuster, S.M.; Olson, M.S.
The regulation of pyruvate dehydrogenase in isolated beef heart mitochondria
J. Biol. Chem.
249
7159-7165
1974
Bos taurus
brenda
Pettit, F.H.; Roche, T.E.; Reed, L.J.
Function of Calcium ions in pyruvate dehydrogenase phosphatase activity
Biochem. Biophys. Res. Commun.
49
563-571
1972
Bos taurus
brenda
Yan, J.; Lawson, J.E.; Reed, L.J.
Role of the regulatory subunit of bovine pyruvate dehydrogenase phosphatase
Proc. Natl. Acad. Sci. USA
93
4953-4956
1996
Bos taurus
brenda
Huang, B.; Gudi, R.; Wu, P.; Harris, R.A.; Hamilton, J.; Popov, K.M.
Isoenzymes of pyruvate dehydrogenase phosphatase. DNA-derived amino acid sequences, expression, and regulation
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273
17680-17688
1998
Rattus norvegicus (O88483)
brenda
Chen, G.; Wang, L.; Liu, S.; Chuang, C.; Roche, T.E.
Activated function of the pyruvate dehydrogenase phosphatase through Ca2+-facilitated binding to the inner lipoyl domain of the dihydrolipoyl acetyltransferase
J. Biol. Chem.
271
28064-28070
1996
Bos taurus
brenda
Simonot, C.; Lerme, F.; Louisot, P.; Gateau-Roesch, O.
Sub-mitochondrial localization of the catalytic subunit of pyruvate dehydrogenase phosphatase
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401
158-162
1997
Mus musculus
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Lawson, J.E.; Niu, X.D.; Browning, K.S.; Trong, H.L.; Yan, J.; Reed, L.J.
Molecular cloning and expression of the catalytic subunit of bovine pyruvate dehydrogenase phosphatase and sequence similarity with protein phosphatase 2C
Biochemistry
32
8987-8993
1993
Bos taurus
brenda
Cockburn, B.N.; Coore, H.G.
Starvation reduces pyruvate dehydrogenase phosphate phosphatase activity in rat kidney
Mol. Cell. Biochem.
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131-136
1995
Rattus norvegicus
brenda
Bak, C.I.; Huh, J.W.; Hong, S.; Song, B.J.
Noncompetitive, Ca(2+)-independent inhibition of pyruvate dehydrogenase phosphatase by fluphenazine
Biochem. Mol. Biol. Int.
47
1029-1037
1999
Bos taurus
brenda
Galasko, G.T.F.; Abe, S.; Lilley, K.; Zhang, C.; Larner, J.
Circulating factors and insulin resistance. II. The action of the novel myo-inositol cyclic 1,2-inositol phosphate phosphoglycan insulin antagonist from human plasma in regulating pyruvate dehydrogenase phosphatase
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81
1051-1057
1996
Bos taurus
brenda
Ito, M.; Kobashi, H.; Naito, E.; Saijo, T.; Takeda, E.; Huq, A.H.M.M.; Kuroda, Y.
Decrease of pyruvate dehydrogenase phosphatase activity in patients with congenital lactic acidemia
Clin. Chim. Acta
209
1-7
1992
Homo sapiens
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Lawson, J.E.; Park, S.H.; Mattison, A.R.; Yan, J.; Reed, L.J.
Cloning, expression, and properties of the regulatory subunit of bovine pyruvate dehydrogenase phosphatase
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272
31625-31629
1997
Bos taurus
brenda
Song, H.; Thissen, J.; Komuniecki, R.
Novel regulation of pyruvate dehydrogenase phosphatase activity from mitochondria of the parasitic nematode, Ascaris suum
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48
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1991
Ascaris suum
brenda
Roche, T.E.; Baker, J.C.; Yan, X.; Hiromasa, Y.; Gong, X.; Peng, T.; Dong, J.; Turkan, A.; Kasten, S.A.
Distinct regulatory properties of pyruvate dehydrogenase kinase and phosphatase isoforms
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2001
Mammalia
brenda
Roche, T.E.; Hiromasa, Y.; Turkan, A.; Gong, X.; Peng, T.; Yan, X.; Kasten, S.A.; Bao, H.; Dong, J.
Essential roles of lipoyl domains in the activated function and control of pyruvate dehydrogenase kinases and phosphatase isoform 1
Eur. J. Biochem.
270
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2003
Mammalia
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Jacobia, S.J.; Korotchkina, L.G.; Patel, M.S.
Differential effects of two mutations at arginine-234 in the alpha subunit of human pyruvate dehydrogenase
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395
121-128
2001
Homo sapiens
brenda
Patel, M.S.; Korotchkina, L.G.
The biochemistry of the pyruvate dehydrogenase complex
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31
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2003
Mammalia
-
brenda
Karpova, T.; Danchuk, S.; Kolobova, E.; Popov, K.M.
Characterization of the isozymes of pyruvate dehydrogenase phosphatase: implications for the regulation of pyruvate dehydrogenase activity
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1652
126-135
2003
Rattus norvegicus
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Karpova, T.; Danchuk, S.; Huang, B.; Popov, K.M.
Probing a putative active site of the catalytic subunit of pyruvate dehydrogenase phosphatase 1 (PDP1c) by site-directed mutagenesis
Biochim. Biophys. Acta
1700
43-51
2004
Rattus norvegicus
brenda
Huang, B.; Wu, P.; Popov, K.M.; Harris, R.A.
Starvation and diabetes reduce the amount of pyruvate dehydrogenase phosphatase in rat heart and kidney
Diabetes
52
1371-1376
2003
Rattus norvegicus
brenda
Turkan, A.; Gong, X.; Peng, T.; Roche, T.E.
Structural requirements within the lipoyl domain for the Ca2+-dependent binding and activation of pyruvate dehydrogenase phosphatase isoform 1 or its catalytic subunit
J. Biol. Chem.
277
14976-14985
2002
Bos taurus
brenda
Soo Choi, W.; Yan, J.; McCarthy, D.B.; Hee Park, S.; Reed, L.J.
One-step purification of the recombinant catalytic subunit of pyruvate dehydrogenase phosphatase
Protein Expr. Purif.
20
128-131
2000
Bos taurus
brenda
Korotchkina, L.G.; Sidhu, S.; Patel, M.S.
R-lipoic acid inhibits mammalian pyruvate dehydrogenase kinase
Free Radic. Res.
38
1083-1092
2004
Rattus norvegicus
brenda
Turkan, A.; Hiromasa, Y.; Roche, T.E.
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
43
15073-15085
2004
Bos taurus
brenda
Chen, H.B.; Shen, J.; Ip, Y.T.; Xu, L.
Identification of phosphatases for Smad in the BMP/DPP pathway
Genes Dev.
20
648-653
2006
Drosophila melanogaster, Homo sapiens
brenda
Maj, M.C.; MacKay, N.; Levandovskiy, V.; Addis, J.; Baumgartner, E.R.; Baumgartner, M.R.; Robinson, B.H.; Cameron, J.M.
Pyruvate dehydrogenase phosphatase deficiency: identification of the first mutation in two brothers and restoration of activity by protein complementation
J. Clin. Endocrinol. Metab.
90
4101-4107
2005
Homo sapiens
brenda
Bajotto, G.; Murakami, T.; Nagasaki, M.; Tamura, T.; Tamura, N.; Harris, R.A.; Shimomura, Y.; Sato, Y.
Downregulation of the skeletal muscle pyruvate dehydrogenase complex in the otsuka long-evans tokushima fatty rat both before and after the onset of diabetes mellitus
Life Sci.
75
2117-2130
2004
Rattus norvegicus
brenda
Piccinini, M.; Mostert, M.; Alberto, G.; Ramondetti, C.; Novi, R.F.; Dalmasso, P.; Rinaudo, M.T.
Down-regulation of pyruvate dehydrogenase phosphatase in obese subjects is a defect that signals insulin resistance
Obes. Res.
13
678-686
2005
Homo sapiens
brenda
Krause-Buchholz, U.; Gey, U.; Wuenschmann, J.; Becker, S.; Roedel, G.
YIL042c and YOR090c encode the kinase and phosphatase of the Saccharomyces cerevisiae pyruvate dehydrogenase complex
FEBS Lett.
580
2553-2560
2006
Saccharomyces cerevisiae
brenda
Leblanc, P.J.; Harris, R.A.; Peters, S.J.
Skeletal muscle fiber type comparison of pyruvate dehydrogenase phosphatase activity and isoform expression in fed and food-deprived rats
Am. J. Physiol. Endocrinol. Metab.
292
E571-E576
2007
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
brenda
Hill, C.S.
Turning off Smads: identification of a Smad phosphatase
Dev. Cell
10
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2006
Drosophila melanogaster, Mammalia
brenda
Vassylyev, D.G.; Symersky, J.
Crystal structure of pyruvate dehydrogenase phosphatase 1 and its functional implications
J. Mol. Biol.
370
417-426
2007
Rattus norvegicus (O88483)
brenda
Gey, U.; Czupalla, C.; Hoflack, B.; Roedel, G.; Krause-Buchholz, U.
Yeast pyruvate dehydrogenase complex is regulated by a concerted activity of two kinases and two phosphatases
J. Biol. Chem.
283
9759-9767
2008
Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4741
brenda
Leblanc, P.J.; Mulligan, M.; Antolic, A.; Macpherson, L.; Inglis, J.G.; Martin, D.; Roy, B.D.; Peters, S.J.
Skeletal muscle type comparison of pyruvate dehydrogenase phosphatase activity and isoform expression: effects of obesity and endurance training
Am. J. Physiol. Regul. Integr. Comp. Physiol.
295
R1224-R1230
2008
Rattus norvegicus (O88483), Rattus norvegicus (O88484)
brenda
Cameron, J.M.; Maj, M.; Levandovskiy, V.; Barnett, C.P.; Blaser, S.; Mackay, N.; Raiman, J.; Feigenbaum, A.; Schulze, A.; Robinson, B.H.
Pyruvate dehydrogenase phosphatase 1 (PDP1) null mutation produces a lethal infantile phenotype
Hum. Genet.
125
319-326
2009
Homo sapiens (Q9P2J9), Homo sapiens (Q9P0J1), Homo sapiens
brenda
McLean, P.; Kunjara, S.; Greenbaum, A.L.; Gumaa, K.; Lopez-Prados, J.; Martin-Lomas, M.; Rademacher, T.W.
Reciprocal control of pyruvate dehydrogenase kinase and phosphatase by inositol phosphoglycans. Dynamic state set by "push-pull" system
J. Biol. Chem.
283
33428-33436
2008
Bos taurus, Bos taurus (P35816)
brenda
Kato, J.; Kato, M.
Crystallization and preliminary crystallographic studies of the catalytic subunits of human pyruvate dehydrogenase phosphatase isoforms 1 and 2
Acta Crystallogr. Sect. F
66
342-345
2010
Homo sapiens (Q9P2J9), Homo sapiens (Q9P0J1), Homo sapiens
brenda
Hans, S.K.; Camara, F.; Altiti, A.; Martin-Montalvo, A.; Brautigan, D.L.; Heimark, D.; Larner, J.; Grindrod, S.; Brown, M.L.; Mootoo, D.R.
Synthesis of C-glycoside analogues of beta-galactosamine-(1-4)-3-O-methyl-D-chiro-inositol and assay as activator of protein phosphatases PDHP and PP2Calpha
Bioorg. Med. Chem.
18
1103-1110
2010
Rattus norvegicus
brenda
Love, L.; LeBlanc, P.; Inglis, J.; Bradley, N.; Choptiany, J.; Heigenhauser, G.; Peters, S.
The relationship between human skeletal muscle pyruvate dehydrogenase phosphatase activity and muscle aerobic capacity
J. Appl. Physiol.
111
427-434
2011
Homo sapiens
brenda
Shan, C.; Kang, H.B.; Elf, S.; Xie, J.; Gu, T.L.; Aguiar, M.; Lonning, S.; Hitosugi, T.; Chung, T.W.; Arellano, M.; Khoury, H.J.; Shin, D.M.; Khuri, F.R.; Boggon, T.J.; Fan, J.
Tyr-94 phosphorylation inhibits pyruvate dehydrogenase phosphatase 1 and promotes tumor growth
J. Biol. Chem.
289
21413-21422
2014
Homo sapiens
brenda
Kaplon, J.; Zheng, L.; Meissl, K.; Chaneton, B.; Selivanov, V.A.; Mackay, G.; van der Burg, S.H.; Verdegaal, E.M.; Cascante, M.; Shlomi, T.; Gottlieb, E.; Peeper, D.S.
A key role for mitochondrial gatekeeper pyruvate dehydrogenase in oncogene-induced senescence
Nature
498
109-112
2013
Homo sapiens
brenda
Xing, G.; Ren, M.; O'Neill, J.T.; Sharma, P.; Verma, A.; Watson, W.D.
Pyruvate dehydrogenase phosphatase1 mRNA expression is divergently and dynamically regulated between rat cerebral cortex, hippocampus and thalamus after traumatic brain injury: a potential biomarker of TBI-induced hyper- and hypo-glycaemia and neuronal vulnerability
Neurosci. Lett.
525
140-145
2012
Rattus norvegicus
brenda
Heo, H.; Kim, H.; Youm, J.; Cho, S.; Song, I.; Lee, S.; Ko, T.; Kim, N.; Ko, K.; Rhee, B.; Han, J.
Mitochondrial pyruvate dehydrogenase phosphatase 1 regulates the early differentiation of cardiomyocytes from mouse embryonic stem cells
Exp. Mol. Med.
48
e254
2016
Mus musculus
brenda
Guo, X.; Niemi, N.; Coon, J.; Pagliarini, D.
Integrative proteomics and biochemical analyses define Ptc6p as the Saccharomyces cerevisiae pyruvate dehydrogenase phosphatase
J. Biol. Chem.
292
11751-11759
2017
Saccharomyces cerevisiae
brenda
Wang, H.; Zhang, L.; Guo, X.; Bai, Y.; Li, Y.X.; Sha, J.; Peng, C.; Wang, Y.L.; Liu, M.
MiR-195 modulates oxidative stress-induced apoptosis and mitochondrial energy production in human trophoblasts via flavin adenine dinucleotide-dependent oxidoreductase domain-containing protein 1 and pyruvate dehydrogenase phosphatase regulatory subunit
J. Hypertens.
36
306-318
2018
Homo sapiens (Q8NCN5), Homo sapiens
brenda
Barberio, M.D.; Huffman, K.M.; Giri, M.; Hoffman, E.P.; Kraus, W.E.; Hubal, M.J.
Pyruvate dehydrogenase phosphatase regulatory gene expression correlates with exercise training insulin sensitivity changes
Med. Sci. Sports Exerc.
48
2387-2397
2016
Homo sapiens
brenda
Chen, J.; Guccini, I.; Mitri, D.; Brina, D.; Revandkar, A.; Sarti, M.; Pasquini, E.; Alajati, A.; Pinton, S.; Losa, M.; Civenni, G.; Catapano, C.; Sgrignani, J.; Cavalli, A.; DAntuono, R.; Asara, J.; Morandi, A.; Chiarugi, P.; Crotti, S.; Agostini, M.
Compartmentalized activities of the pyruvate dehydrogenase complex sustain lipogenesis in prostate cancer
Nat. Genet.
50
219-228
2018
Homo sapiens
brenda
Kono, M.; Yoshida, N.; Maeda, K.; Skinner, N.E.; Pan, W.; Kyttaris, V.C.; Tsokos, M.G.; Tsokos, G.C.
Pyruvate dehydrogenase phosphatase catalytic subunit 2 limits Th17 differentiation
Proc. Natl. Acad. Sci. USA
115
9288-9293
2018
Homo sapiens, Mus musculus
brenda
Guo, Y.; Qiu, W.; Roche, T.; Hackert, M.
Crystal structure of the catalytic subunit of bovine pyruvate dehydrogenase phosphatase
Acta Crystallogr. F Struct. Biol. Commun.
76
292-301
2020
Bos taurus (P35816)
brenda
Li, Y.; Shen, J.; Cheng, C.S.; Gao, H.; Zhao, J.; Chen, L.
Overexpression of pyruvate dehydrogenase phosphatase 1 promotes the progression of pancreatic adenocarcinoma by regulating energy-related AMPK/mTOR signaling
Cell Biosci.
10
95
2020
Homo sapiens (Q9P0J1)
brenda
Karagiota, A.; Kanoura, A.; Paraskeva, E.; Simos, G.; Chachami, G.
Pyruvate dehydrogenase phosphatase 1 (PDP1) stimulates HIF activity by supporting histone acetylation under hypoxia
FEBS J.
290
2165-2179
2023
Homo sapiens (Q9P0J1)
brenda
Bedoyan, J.K.; Hecht, L.; Zhang, S.; Tarrant, S.; Bergin, A.; Demirbas, D.; Yang, E.; Shin, H.K.; Grahame, G.J.; DeBrosse, S.D.; Hoppel, C.L.; Kerr, D.S.; Berry, G.T.
A novel null mutation in the pyruvate dehydrogenase phosphatase catalytic subunit gene (PDP1) causing pyruvate dehydrogenase complex deficiency
JIMD Rep.
48
26-35
2019
Homo sapiens (Q9P0J1)
brenda
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