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Information on EC 3.1.3.43 - [pyruvate dehydrogenase (acetyl-transferring)]-phosphatase and Organism(s) Bos taurus and UniProt Accession P35816

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IUBMB Comments
A mitochondrial enzyme associated with EC 1.2.4.1 pyruvate dehydrogenase (acetyl-transferring), in the pyruvate dehydrogenase complex.
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Bos taurus
UNIPROT: P35816
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The taxonomic range for the selected organisms is: Bos taurus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
pyruvate dehydrogenase complex, pyruvate dehydrogenase phosphatase, pdh phosphatase, pyruvate dehydrogenase phosphate phosphatase, pyruvate dehydrogenase phosphatase 1, pda1p, pyruvate dehydrogenase phosphatase 2, yor090cp, phosphopyruvate dehydrogenase phosphatase, pyruvate dehydrogenase phosphatase isoform 1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pyruvate dehydrogenase phosphatase type 1
-
PDP1
-
-
PDP2
-
-
phosphatase, pyruvate dehydrogenase
-
-
-
-
phosphopyruvate dehydrogenase phosphatase
-
-
-
-
pyruvate dehydrogenase phosphatase
pyruvate dehydrogenase phosphatase type 2
-
-
pyruvate dehydrogenase phosphate phosphatase
-
-
-
-
[pyruvate dehydrogenase (lipoamide)]-phosphatase
-
-
-
-
[pyruvate dehydrogenase (lipoamide)]-phosphate phosphohydrolase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
[pyruvate dehydrogenase (acetyl-transferring)] phosphate + H2O = [pyruvate dehydrogenase (acetyl-transferring)] + phosphate
show the reaction diagram
mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
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.
CAS REGISTRY NUMBER
COMMENTARY hide
9073-70-5
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + 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
-
-
-
-
?
RRAT(P)VA + H2O
RRATVA + phosphate
show the reaction diagram
-
-
-
-
?
[Asp8]tetradecapeptide + H2O
?
show the reaction diagram
-
-
-
-
?
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
?
show the reaction diagram
-
-
-
-
?
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
?
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
the addition of 0.1 mM Ca2+ alone gives a 6fold increase in basal PDP activity
Mn2+
about 50% stimulation of activity in the presence of 1 mM Mn2+
Zn2+
about 70% stimulation of activity in the presence of 0.01 mM Zn2+
Zn2+
about 70% stimulation of activity in the presence of 0.01 mM Zn2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Zn2+
about 20% decrease of activity in the presence of 0.01 mM Zn2+
arsenite
-
together with NADH
chlorpromazine
-
-
dihydrolipoamide
-
-
F-
-
-
fluphenazine
-
-
myo-inositol cyclic 1,2-inositol phosphate phosphoglycan
-
from human plasma, antagonist of insulin, inhibits Mg2+ and spermine stimulation
-
p-nitrophenylphosphate
-
-
phosphate
-
-
thioridazine
-
-
triflupromazine
-
-
Zn2+
about 20% decrease of activity in the presence of 0.01 mM Zn2+
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
inositol phosphoglycan P-type
linear stimulation
-
inner lipoyl domain of dihydrolipoyl acetyltransferase
-
component of substrate complex, structural requirements for binding and activation
-
inositol phosphoglycan P-type
linear stimulation
-
NAD+
-
reverses NADH inhibition
protamine
-
-
putrescine
spermidine
spermine
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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 - 0.058
[Pyruvate dehydrogenase (lipoamide)]-phosphate
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.3
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PDP1_BOVIN
538
0
61184
Swiss-Prot
other Location (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
140000
-
gel filtration
150000
45000
-
x * 45000, immunoblotting, truncated recombinant PDPc
49000
-
1 * 89000 + 1 * 49000, gel electrophoresis, heterodimer
50000
52625
-
x * 52625, calculated after PCR, subcloning and sequencing
89000
-
1 * 89000 + 1 * 49000, gel electrophoresis, heterodimer
90000
-
1 * 90000 + 1 * 50000, SDS-PAGE
95660
-
calculated after cloning, PCR and sequencing
95800
-
matrix-assisted laser desorption-ionization mass spectrometry
97000
-
1 * 97000 + 1 * 50000, SDS-PAGE, heterodimer
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
needle like
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C for 1 month
-
-70°C, 400 mM KCl for 2 months no loss of activity
-
4°C
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
400-1000fold
-
assay method
-
recombinant catalytic subunit, one-step affinity chromatographic method
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
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
J. Biol. Chem.
263
8106-8110
1988
Bos taurus
Manually annotated by BRENDA team
Reed, L.J.; Yeaman, S.J.
Pyruvate dehydrogenase
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
18
77-95
1987
Bos taurus, Neurospora crassa
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Pettit, F.H.; Teague, W.M.; Reed, L.J.
Pyruvate dehydrogenase phosphatase from bovine heart
Methods Enzymol.
90
402-407
1982
Bos taurus
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Uhlinger, D.J.; Yang, C.Y.; Reed, L.J.
Phosphorylation-dephosphorylation of pyruvate dehydrogenase from bakersyeast
Biochemistry
25
5673-5677
1986
Bos taurus
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
J. Clin. Endocrinol.
81
1051-1057
1996
Bos taurus
Manually annotated by BRENDA team
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
J. Biol. Chem.
272
31625-31629
1997
Bos taurus
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team