Information on EC 3.1.3.43 - [pyruvate dehydrogenase (acetyl-transferring)]-phosphatase

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The expected taxonomic range for this enzyme is: Eukaryota

EC NUMBER
COMMENTARY
3.1.3.43
-
RECOMMENDED NAME
GeneOntology No.
[pyruvate dehydrogenase (acetyl-transferring)]-phosphatase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
[pyruvate dehydrogenase (acetyl-transferring)] phosphate + H2O = [pyruvate dehydrogenase (acetyl-transferring)] + phosphate
show the reaction diagram
-
-
-
-
[pyruvate dehydrogenase (acetyl-transferring)] phosphate + H2O = [pyruvate dehydrogenase (acetyl-transferring)] + phosphate
show the reaction diagram
overview on mechanism and regulation of enzyme
-
[pyruvate dehydrogenase (acetyl-transferring)] phosphate + H2O = [pyruvate dehydrogenase (acetyl-transferring)] + phosphate
show the reaction diagram
mechanism, overview
-
[pyruvate dehydrogenase (acetyl-transferring)] phosphate + H2O = [pyruvate dehydrogenase (acetyl-transferring)] + phosphate
show the reaction diagram
mechanism, difference in specificity of isoforms
-
[pyruvate dehydrogenase (acetyl-transferring)] phosphate + H2O = [pyruvate dehydrogenase (acetyl-transferring)] + phosphate
show the reaction diagram
mechanism
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
hydrolysis of phosphoric ester
-
-
hydrolysis of phosphoric ester
-
-
hydrolysis of phosphoric ester
-
-
hydrolysis of phosphoric ester
-
-
hydrolysis of phosphoric ester
-
-
hydrolysis of phosphoric ester
-
-
hydrolysis of phosphoric ester
Rattus norvegicus Sprague-Dawley, Saccharomyces cerevisiae BY4741
-
-
-
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
Rattus norvegicus Sprague-Dawley
-
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
-
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Pda1p
-
alpha-subunit of the pyruvate dehydrogenase complex
Pda1p
-
alpha-subunit of the pyruvate dehydrogenase complex
-
PDH phosphatase
-
-
PDH phosphatase
O88483, O88484
-
PDP
Rattus norvegicus Sprague-Dawley
-
-
-
PDP1
-
-
PDP1
P35816
-
PDP1
Q9P0J1
isoform
PDP1
-
-
PDP1
O88483
isoform
PDP1
O88483
PDP1r regulatory subunit, PDP1c catalytic subunit
PDP1
Rattus norvegicus Sprague-Dawley
-
-
-
PDP2
-
-
PDP2
-
-
PDP2
Q9P2J9
isoform
PDP2
-
-
PDP2
O88484
isoform
PDP2
Rattus norvegicus Sprague-Dawley
-
-
-
phosphatase, pyruvate dehydrogenase
-
-
-
-
phosphopyruvate dehydrogenase phosphatase
-
-
-
-
pyruvate dehydrogenase complex
-
-
pyruvate dehydrogenase complex
-
-
-
pyruvate dehydrogenase phosphatase
-
-
-
-
pyruvate dehydrogenase phosphatase
-
-
pyruvate dehydrogenase phosphatase
-
-
pyruvate dehydrogenase phosphatase
-
-
pyruvate dehydrogenase phosphatase
Q9P0J1, Q9P2J9
-
pyruvate dehydrogenase phosphatase
-
-
pyruvate dehydrogenase phosphatase
-
-
pyruvate dehydrogenase phosphatase
O88483
-
pyruvate dehydrogenase phosphatase
O88484
-
pyruvate dehydrogenase phosphatase
Rattus norvegicus Sprague-Dawley
-
-
-
pyruvate dehydrogenase phosphatase
-
-
pyruvate dehydrogenase phosphatase
-
-
-
pyruvate dehydrogenase phosphatase isoform 1
Q9P0J1
-
pyruvate dehydrogenase phosphatase isoform 2
Q9P2J9
-
pyruvate dehydrogenase phosphatase type 1
P35816
-
pyruvate dehydrogenase phosphatase type 2
-
-
pyruvate dehydrogenase phosphate phosphatase
-
-
-
-
[pyruvate dehydrogenase (acetyl-transferring)]-phosphatase
-
-
[pyruvate dehydrogenase (acetyl-transferring)]-phosphatase
-
-
[pyruvate dehydrogenase (acetyl-transferring)]-phosphatase
-
-
[pyruvate dehydrogenase (acetyl-transferring)]-phosphatase
-
-
[pyruvate dehydrogenase (acetyl-transferring)]-phosphatase
O88483
-
[pyruvate dehydrogenase (acetyl-transferring)]-phosphatase
Rattus norvegicus Sprague-Dawley
-
-
-
[pyruvate dehydrogenase (acetyl-transferring)]-phosphatase
-
-
[pyruvate dehydrogenase (acetyl-transferring)]-phosphatase
-
-
-
[pyruvate dehydrogenase (lipoamide)]-phosphatase
-
-
-
-
[pyruvate dehydrogenase (lipoamide)]-phosphate phosphohydrolase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9073-70-5
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
overview
-
-
Manually annotated by BRENDA team
reactivation of the pyruvate dehydrogenase complex from Saccharomyces cerevisiae
-
-
Manually annotated by BRENDA team
recombinant catalytic subunit
-
-
Manually annotated by BRENDA team
isoforms PDP1, PDP2
-
-
Manually annotated by BRENDA team
two isoforms
-
-
Manually annotated by BRENDA team
Long-Evans Tokushima Otsuka (LETO) rat; Otsuka Long-Evans Tokushima Fatty (OLETF) rat, spontaneously diabetic
-
-
Manually annotated by BRENDA team
recombinant enzyme
-
-
Manually annotated by BRENDA team
Sprague-Dawley
-
-
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
Sprague-Dawley
-
-
Manually annotated by BRENDA team
strain BY4741
-
-
Manually annotated by BRENDA team
wild type strain BY4741, mutant strain yor090c lacking pyruvate dehydrogenase phosphatase
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
physiological function
-
allosteric activation of pyruvate dehydrogenase phosphatase and protein phosphatase 2Calpha leads to insulin-mimetic and insulin-sensitizing effects
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
-
-
-
?
peptide T-1
?
show the reaction diagram
-
phosphopeptide produced by tryptic digestion of phosphorylated pyruvate dehydrogenase
-
-
?
peptide T-2
?
show the reaction diagram
-
-
-
-
?
peptide T-3
?
show the reaction diagram
-
-
-
-
?
RRAS(P)VA
?
show the reaction diagram
-
-
-
-
?
[Asp8]tetradecapeptide + H2O
?
show the reaction diagram
-
-
-
-
?
[mothers against decapentaplegic]-phosphate + H2O
[mothers against decapentaplegic] + phosphate
show the reaction diagram
-
PDP1 directly dephosphorylates mothers against decapentaplegic (MAD) and inhibits signal transduction of decapentaplegic (DPP)
-
-
?
[pyruvate dehydrogenase (acetyl-transferring)] phosphate + H2O
[pyruvate dehydrogenase (acetyl-transferring)] + phosphate
show the reaction diagram
-
-
-
-
?
[pyruvate dehydrogenase (acetyl-transferring)] phosphate + H2O
[pyruvate dehydrogenase (acetyl-transferring)] + phosphate
show the reaction diagram
-
-
-
-
?
[pyruvate dehydrogenase (acetyl-transferring)] phosphate + H2O
[pyruvate dehydrogenase (acetyl-transferring)] + phosphate
show the reaction diagram
-
-
-
-
?
[pyruvate dehydrogenase (acetyl-transferring)] phosphate + H2O
[pyruvate dehydrogenase (acetyl-transferring)] + phosphate
show the reaction diagram
-
-
-
-
?
[pyruvate dehydrogenase (acetyl-transferring)] phosphate + H2O
[pyruvate dehydrogenase (acetyl-transferring)] + phosphate
show the reaction diagram
-
-
-
-
?
[pyruvate dehydrogenase (acetyl-transferring)] phosphate + H2O
[pyruvate dehydrogenase (acetyl-transferring)] + phosphate
show the reaction diagram
O88483
-
-
-
?
[pyruvate dehydrogenase (acetyl-transferring)] phosphate + H2O
[pyruvate dehydrogenase (acetyl-transferring)] + phosphate
show the reaction diagram
Rattus norvegicus Sprague-Dawley
-
-
-
-
?
[pyruvate dehydrogenase (acetyl-transferring)] phosphate + H2O
[pyruvate dehydrogenase (acetyl-transferring)] + phosphate
show the reaction diagram
-
-
-
-
?
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
show the reaction diagram
-
-
-
?
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
show the reaction diagram
-
-
-
ir
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
show the reaction diagram
-
-
-
?
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
show the reaction diagram
-
-
-
-
?
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
show the reaction diagram
-
-
-
ir
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
show the reaction diagram
-
-
-
-
?
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
show the reaction diagram
-
-
-
ir
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
show the reaction diagram
-
-
-
ir
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
show the reaction diagram
-
-
-
ir
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
show the reaction diagram
-
-
-
ir
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
show the reaction diagram
-
-
-
ir
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
show the reaction diagram
-
-
-
ir
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
show the reaction diagram
-
-
-
ir
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
show the reaction diagram
-
-
-
ir
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
show the reaction diagram
-
-
-
ir
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
show the reaction diagram
-
-
-
ir
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
show the reaction diagram
-
-
-
ir
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
show the reaction diagram
-
-
-
ir
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
show the reaction diagram
-
-
-
ir
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
show the reaction diagram
-
-
-
ir
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
show the reaction diagram
-
-
-
ir
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
show the reaction diagram
-
-
-
ir
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
show the reaction diagram
-
-
-
ir
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
show the reaction diagram
-
-
-
ir
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
show the reaction diagram
-
-
-
ir
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
show the reaction diagram
-
-
-
ir
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
show the reaction diagram
-
-
-
ir
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
show the reaction diagram
-
-
-
ir
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
show the reaction diagram
-
-
-
?
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
show the reaction diagram
-
-
-
-
?
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
show the reaction diagram
P35816
-
-
-
?
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
show the reaction diagram
-
-
-
ir
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
show the reaction diagram
-
-
-
ir
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
show the reaction diagram
-
-
-
ir
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
show the reaction diagram
-
-
-
ir
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
show the reaction diagram
-
-
-
ir
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
show the reaction diagram
-
-
-
ir
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
show the reaction diagram
-
-
-
ir
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
show the reaction diagram
-
-
-
ir
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
show the reaction diagram
-
-
-
ir
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
show the reaction diagram
-
-
-
ir
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
show the reaction diagram
-
-
-
ir
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
show the reaction diagram
-
-
-
ir
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
show the reaction diagram
-
-
-
ir
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
show the reaction diagram
-
-
-
ir
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
show the reaction diagram
-
-
-
ir
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
show the reaction diagram
-
-
-
ir
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
show the reaction diagram
-
-
-
ir
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
show the reaction diagram
-
-
-
ir
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
show the reaction diagram
-
-
-
ir
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
show the reaction diagram
-
-
-
ir
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
show the reaction diagram
-
-
-
ir
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
show the reaction diagram
-
-
-
ir
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
show the reaction diagram
-
presence of EGTA or Ca2+ and transacetylase
-
ir
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
show the reaction diagram
-
pyruvate dehydrogenase activity is only 25% in patients carrying a deletion mutation of L213 of PDP1
-
-
?
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
?
show the reaction diagram
-
-
-
-
-
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
?
show the reaction diagram
-
-
-
-
-
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
?
show the reaction diagram
-
-
-
-
-
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
?
show the reaction diagram
-
-
-
-
-
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
?
show the reaction diagram
-
-
-
-
-
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
?
show the reaction diagram
-
-
-
-
-
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
?
show the reaction diagram
-
-
-
-
-
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
?
show the reaction diagram
-
-
-
-
-
additional information
?
-
-
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
-
?
additional information
?
-
-
different conditions for binding of isoforms to substrate, both isoforms can dephosphorylate all three phosphorylation sites of substrate in a random mechanism
-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
show the reaction diagram
-
-
-
-
?
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
show the reaction diagram
-
-
-
-
?
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
?
show the reaction diagram
-
-
-
-
-
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
?
show the reaction diagram
-
-
-
-
-
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
?
show the reaction diagram
-
-
-
-
-
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
?
show the reaction diagram
-
-
-
-
-
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
?
show the reaction diagram
-
-
-
-
-
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
?
show the reaction diagram
-
-
-
-
-
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
?
show the reaction diagram
-
-
-
-
-
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
?
show the reaction diagram
-
-
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
FAD
-
noncovalently bound to PDP1r
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
activation, overview
Ca2+
-
activates, facilitates binding to substrate
Ca2+
-
required for binding of catalytic subunit
Ca2+
-
increase in Mg2+ concentration decreases the Ca2+ concentration needed for half-maximal activation of PDB1 from 3 microM to 1 microM
Ca2+
-
2 mM required for optimal phosphorylase activity
Ca2+
-
PDP1 is highly enhanced through Ca2+-dependent binding of PDP1c to the inner lipoyl domain L2 of the dihydrolipoyl acetyltransferase E2
Ca2+
P35816
the addition of 0.1 mM Ca2+ alone gives a 6fold increase in basal PDP activity; the addition of 0.1 mM Ca2+ alone gives a 6fold increase in basal PDP activity
Ca2+
-
stimulates in presence of Mg2+
Ca2+
-
Km: 0.0438 mM, fully phosphorylated pyruvate dehydrogenase complex, Km: 0.0156 mM partially phosphorylated
Ca2+
-
Km: 0.116 mM, fully phosphorylated pyruvate dehydrogenase complex, Km: 0.0266 mM, partially phosphorylated
Ca2+
-
Km: 0.001-0.003 mM; overcomes EGTA inhibition
Ca2+
-
Km: 0.001
Ca2+
-
overcomes EGTA inhibition
Ca2+
-
within toluene-permeabilized mitochondria
Ca2+
-
required to bind the phosphatase to the transacetylase
Ca2+
-
subunit pyruvate dehydrogenase phosphatase 1 regulated by
Ca2+
-
aiding the association of PDP with dihydrolipoyl acetyltransferase
Ca2+
-
cannot overcome inhibition by calmodulin antagonists
Ca2+
-
-
Co2+
-
Km: 1.4 mM
KCl
-
-
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+
-
required, PDP2 is less sensitive to Mg2+ concentration than PDP1
Mg2+
-
required, Km-value about 0.3-0.5 mM
Mg2+
-
increase in Mg2+ concentration decreases the Ca2+ concentration needed for half-maximal activation of PDB1 from 3 microM to 1 microM
Mg2+
-
required at five active site residues
Mg2+
-
Km: 3.8 mM
Mg2+
-
insulin increases sensivity to Mg2+ of pyruvate dehydrogenase phosphatase
Mg2+
-
Km: 2 mM
Mg2+
-
Km: 0.59 mM, partially and fully phosphorylated pyruvate dehydrogenase complex
Mg2+
-
Km: 4.2 mM
Mg2+
-
Km: 0.52 mM
Mg2+
-
within toluene-permeabilized mitochondria
Mg2+
-
required
Mg2+
-
dependent; Km: 0.0018 mM
Mg2+
-
Km: 0.7 mM for pyruvate dehydrogenase phosphatase 1, Km: 17.4 mM for pyruvate dehydrogenase phosphatase 2; sensivity of subunit pyruvate dehydrogenase phosphatase 1 10fold higher than of pyruvate dehydrogenase phosphatase 2
Mg2+
-
dependent
Mg2+
-
starvation of rats requires doubled Mg2+ concentration
Mg2+
-
dependent
Mg2+
-
dependent; Km: 3 mM
Mn2+
P35816
about 50% stimulation of activity in the presence of 1 mM Mn2+; about 50% stimulation of activity in the presence of 1 mM Mn2+
Mn2+
-
Km: 0.5 mM
Mn2+
-
-
Mn2+
-
required
Mn2+
-
Km: 1 mM
Mn2+
-
-
Mn2+
-
Km: 1.7 mM
Zn2+
P35816
about 70% stimulation of activity in the presence of 0.01 mM Zn2+; about 70% stimulation of activity in the presence of 0.01 mM Zn2+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
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
arsenite
-
together with NADH
Ca2+
-
antagonizes activation by Mg2+
Calmodulin
-
-
Chlorpromazine
-
-
Dihydrolipoamide
-
-
EGTA
-
with Mg2+ as cofactor
EGTA
-
inhibits binding of the phosphatase to transacetylase
F-
-
50% inhibition at 0.6 mM in the presence of Mg2+
fluphenazine
-
-
glyoxylate
-
at concentrations greater than 0.05 mM
myo-inositol cyclic 1,2-inositol phosphate phosphoglycan
-
from human plasma, antagonist of insulin, inhibits Mg2+ and spermine stimulation
-
N-ethylmaleimide
-
slight inhibition
NaCl
-
inhibits reactivation
NADH
-
0.5 mM with 10 mM Mg2+ and 0.1 mM Ca2+
p-nitrophenylphosphate
-
-
phosphate
-
-
phosphate
-
-
thioridazine
-
-
triflupromazine
-
-
Zn2+
P35816
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+
KCl
-
inhibits reactivation
additional information
O88484
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
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
-
2-tetradecylglycidate
-
together with insulin
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
Ca2+
-
stimulates PDP1 at micromolar concentrations
Ca2+
-
for isozyme PDP1c, simultaneous presence of Ca2+ and E2 component of substrate is required
cysteine
-
reverses glyoxylate inhibition
Dichloroacetate
-
together with insulin
inner lipoyl domain of dihydrolipoyl acetyltransferase
-
component of substrate complex, structural requirements for binding and activation
-
inositol phosphoglycan P-type
P35816
linear stimulation; linear stimulation
-
Insulin
-
sensivity to Mg2+ increases
-
Insulin
-
with starved rats pretreated with dichloroacetate or 2-tetradecylglycidate
-
NAD+
-
reverses NADH inhibition
protamine
-
-
putrescine
-
-
-
putrescine
-
in presence of Mg2+ and Ca2+
-
spermidine
-
-
spermidine
-
in presence of Mg2+ and Ca2+
spermine
-
reduces Km-value for Mg2+
spermine
-
activates
spermine
-
in presence of Mg2+ and Ca2+
spermine
-
pyruvate dehydrogenase phosphatase 2 sensitive to
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
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
29.3
-
p-nitrophenyl phosphate
-
pH 7.8, wild type enzyme
48.9
-
p-nitrophenyl phosphate
-
pH 7.8, D445A mutant
55.1
-
p-nitrophenyl phosphate
-
pH 7.8, N49A mutant
0.625
-
peptide T-1
-
phosphopeptide produced by tryptic digestion of phosphorylated pyruvate dehydrogenase
-
0.22
-
peptide T-2
-
-
-
0.106
-
peptide T-3
-
-
-
0.053
-
RRAS(P)VA
-
with PDPc, a member of the protein phosphatase 2C family
-
0.018
-
RRAT(P)VA
-
with PDPc, a member of the protein phosphatase 2C family
-
0.0029
-
[Pyruvate dehydrogenase (lipoamide)]-phosphate
-
with Ca2+
-
0.003
-
[Pyruvate dehydrogenase (lipoamide)]-phosphate
-
with Ca2+ and Mg2+
-
0.0076
-
[Pyruvate dehydrogenase (lipoamide)]-phosphate
-
-
-
0.029
-
[Pyruvate dehydrogenase (lipoamide)]-phosphate
-
presence of Ca2+ and transacetylase
-
0.053
-
[Pyruvate dehydrogenase (lipoamide)]-phosphate
-
-
-
0.058
-
[Pyruvate dehydrogenase (lipoamide)]-phosphate
-
-
-
0.058
-
[Pyruvate dehydrogenase (lipoamide)]-phosphate
-
presence of EGTA and transacetylase
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.000001
-
-
in white gastrocnemius muscles, wet tissue
0.0000015
-
-
in soleus muscles, wet tissue
0.000002
-
-
in red gastrocnemius muscles in food-deprived rats, wet tissue
0.0000025
-
-
in red gastrocnemius muscles, wet tissue
0.0044
-
-
in soleus muscles, in food-deprived rats, extracted mitochondrial protein
0.005
-
-
in soleus muscles, 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
0.0058
-
-
in white gastrocnemius, extracted mitochondrial protein
0.0066
-
-
in red gastrocnemius, extracted mitochondrial protein
2.3
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
-
-
-
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
PDP2, probably target for insulin activation
Manually annotated by BRENDA team
-
high level of PDP2
Manually annotated by BRENDA team
-
high level of isoform PDP1 and PDP2
Manually annotated by BRENDA team
-
high level of isoform PDP1 and PDP2
Manually annotated by BRENDA team
-
high level of isoform PDP2
Manually annotated by BRENDA team
-
PDP1, PDP2
Manually annotated by BRENDA team
-
high level of PDP2
Manually annotated by BRENDA team
-
high level of isoform PDP2
Manually annotated by BRENDA team
-
PDP1 is downregulated in obese subjects
Manually annotated by BRENDA team
-
high level of PDP1
Manually annotated by BRENDA team
-
soleus slow-twitch oxidative, RG, red gastrocnemius fast-twitch oxidative glycolytic, and WG, white gastrocnemius fast-twitch glycolytic muscles
Manually annotated by BRENDA team
O88484
; PDP1 is the predominant isoform expressed in skeletal muscle
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
-
soleus slow-twitch oxidative, RG, red gastrocnemius fast-twitch oxidative glycolytic, and WG, white gastrocnemius fast-twitch glycolytic muscles
-
Manually annotated by BRENDA team
-
lower mRNA expression compared to non diabetic control animals; mRNA expression
Manually annotated by BRENDA team
-
patients with congenital lactic acidemia
Manually annotated by BRENDA team
-
high level of isoform PDP1
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
52600
-
-
PDP1c
92000
95000
-
gel electrophoresis, SDS-PAGE
95660
-
-
calculated after cloning, PCR and sequencing
95800
-
-
matrix-assisted laser desorption-ionization mass spectrometry
96000
-
-
PDP1r
100000
-
-
gel filtration
100000
-
-
-
140000
-
-
gel filtration
150000
-
-
sedimentation equilibrium and gel filtration
150000
-
-
-
150000
-
-
sedimentation equilibrium and gel filtration
150000
-
-
estimated native molecular weight
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
50000, catalytic subunit, SDS-PAGE
?
-
SDS-PAGE and immunoblotting, PDPc protein; x * 80000, SDS-PAGE and immunoblotting, function unknown
?
-
x * 45000, immunoblotting, truncated recombinant PDPc; x * 50000, SDS-PAGE and immunoblotting, rPDPc; x * 52625, calculated after PCR, subcloning and sequencing
dimer
-
1 * 97000 + 1 * 50000, SDS-PAGE, heterodimer
dimer
-
1 * 89000 + 1 * 49000, gel electrophoresis, heterodimer
dimer
-
1 * 90000 + 1 * 50000, SDS-PAGE
heterodimer
-
isoform PDP1, composed of catalytic subunit PDP1c and regulatory subunit PDP1r of 96000 Da, overview
heterodimer
-
PDP1, 1 * 52000, catalytic subunit,+ 1 * 69000, regulatory subunit, overview
heterodimer
-
catalytic subunit beloging to the phosphatase 2C class plus regulatory subunit, a flavoprotein, overview, there are two isoforms of the catalytic subunit+++
additional information
-
overview on interactions and binding of subunits
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
needle like
-
hanging-drop method; hanging-drop method
-
PDP1c, by using the sitting-drop, vapor-diffusion method
-
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2
4
-
40% loss of activity within 8 days, 80% within 19 days
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
rabbit serum stabilizes
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C for 1 month
-
-70C, 400 mM KCl for 2 months no loss of activity
-
-35C, 4 weeks
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
partially, over 1000fold
-
400-1000fold
-
assay method
-
recombinant catalytic subunit, one-step affinity chromatographic method
-
75% purity after Ni-affinity chromatography
-
immobilized metal ion affinity chromatography (Ni2+), gel filtration; immobilized metal ion affinity chromatography (Ni2+), gel filtration
-
partially
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Escherichia coli
-
expression in S2 cells as GFP-construct; GST-fusion protein, expression in S2 cell line
-
His-tag fusion protein, expression in Escherichia coli BL21(DE3)
-
His-tagged SUMO version expressed in Escherichia coli BL21; His-tagged version expressed in Escherichia coli BL21
-
expression in Escherichia coli
-
expression in Escherichia coli BL21
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
D93A
-
loss of phosphatase activity
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; 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
D445A
-
almost complete loss of activity
D54A
-
almost complete loss of activity
N49A
-
38% of activity of wild type
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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 Decapentaplegic signalling pathways
molecular biology
-
pyruvate dehydrogenase phosphatase acts as a Smad1 phosphatase and plays a key role in TGF-b signalling pathways
medicine
-
overview, role of enzyme in diabetes and starvation
molecular biology
-
pyruvate dehydrogenase phosphatase acts as a Smad1 phosphatase and plays a key role TGF-b signalling pathways
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
molecular biology
-
pyruvate dehydrogenase complex in yeast is regulated by the PDH phosphatase Yor090cp
molecular biology
-
pyruvate dehydrogenase complex in yeast is regulated by the PDH phosphatase Yor090cp
-