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

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.1.3.43
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RECOMMENDED NAME
GeneOntology No.
[pyruvate dehydrogenase (acetyl-transferring)]-phosphatase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
[pyruvate dehydrogenase (acetyl-transferring)] phosphate + H2O = [pyruvate dehydrogenase (acetyl-transferring)] + phosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
additional information
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
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Automatic Mining of ENzyme DAta
bat
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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1003334 A+, 1003655 A+, 1009111 A+, 1009114 A+, 1009115 A+, 1009120 A+, 1009121 A+, 1009122 A+, 1009257 A+, 1023678 A+, 1048209 A+, 1097857 A+, 1097861 A+, 1249437 A+, 1370923 A+, 1482112 A+, 1482132 A+, 1482198 A+, 1482208 A+, 1482227 A+, 1482230 A+, 1482274 A+, 1482284 A+, 1482294 A+, 1482296 A+, 1482315 A+, 1482354 A+, 2169487 A+, 2169545 A+, 2169639 A+, 2247104 A+, 2351116 A+, 2351118 A+, 2469542 A+, 2550875 A+, 2553077 A+, 2603422 A+, 2603435 A+, 2603547 A+, 2603552 A+, 2603567 A+, 288401 A+, 348932 A+, 348937 A+, 348940 A+, 348946 A+, 348953 A+, 348965 A+, 348995 A+, 393963 A+, 393989 A+, 486171 A+, 486181 A+, 486186 A+, 486198 A+, 486199 A+, 486237 A+, 661057 A+, 662098 A+, 663062 A+, 664920 A+, 665596 A+, 672520 A+, 678579 A+, 687613 A+, 696036 A+, 724375 A+, 725205 A+, 725521 A+, 802196 A+, 859000 A+, 859003 A+, 859004 A+, 859008 A+, 859011 A+, 859012 A+, 859013 A+, 859014 A+, 859028 A+, 859031 A+, 859049 A+, 859063 A+, 859097 A+, 859106 A+, 859107 A+, 859111 A+, 859113 A+, 859114 A+, 859115 A+, 859116 A+, 859117 A+, 859118 A+, 859130 A+, 859132 A+, 859148 A+, 859159 A+, 859179 A+, 859183 A+, 859184 A+, 859195 A+, 859196 A+, 859198 A+, 859199 A+, 859201 A+, 859202 A+, 859208 A+, 859212 A+, 859214 A+, 859216 A+, 859229 A+, 859233 A+, 859237 A+, 859244 A+, 859246 A+, 859261 A+, 859272 A+, 859276 A+, 859278 A+, 859279 A+, 859310 A+, 859313 A+, 486240 A++, 653730 A++, 94912 A++, 94915 A++, 94920 A++, 348921 A+++, 348933 A+++, 348934 A+++, 348943 A+++, 348948 A+++, 348956 A+++, 348961 A+++, 486166 A+++, 486167 A+++, 486201 A+++, 486236 A+++, 654734 A+++, 736448 A+++, 859010 A+++, 859025 A+++, 859046 A+++, 859048 A+++, 859074 A+++, 859080 A+++, 859081 A+++, 859087 A+++, 859096 A+++, 859124 A+++, 859126 A+++, 859127 A+++, 859134 A+++, 859217 A+++, 859317 A+++, 859323 A+++, 859335 A+++, 859340 A+++
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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1003263 A+, 1003284 A+, 1003327 A+, 1003387 A+, 1003415 A+, 1003480 A+, 1003504 A+, 1003589 A+, 1009092 A+, 1009132 A+, 1009135 A+, 1009267 A+, 1097865 A+, 1167900 A+, 1167904 A+, 1332558 A+, 1427488 A+, 1482108 A+, 1482118 A+, 1482147 A+, 1482152 A+, 1482153 A+, 1482163 A+, 1482171 A+, 1482172 A+, 1482179 A+, 1482189 A+, 1482202 A+, 1482235 A+, 1482273 A+, 1482289 A+, 1482339 A+, 2169495 A+, 2169514 A+, 2169519 A+, 2169522 A+, 2169525 A+, 2169529 A+, 2169545 A+, 2169554 A+, 2169572 A+, 2243952 A+, 2243969 A+, 2244017 A+, 2244051 A+, 2262675 A+, 2499678 A+, 2603430 A+, 2603441 A+, 2603459 A+, 2603460 A+, 2603473 A+, 2603492 A+, 2603514 A+, 2603515 A+, 2603526 A+, 2603529 A+, 2603622 A+, 348926 A+, 349035 A+, 392509 A+, 730476 A+, 804292 A+, 804422 A+, 859016 A+, 859042 A+, 859050 A+, 859060 A+, 859061 A+, 859088 A+, 859091 A+, 859095 A+, 859109 A+, 859140 A+, 859144 A+, 859147 A+, 859153 A+, 859154 A+, 859163 A+, 859164 A+, 859175 A+, 859211 A+, 859215 A+, 859219 A+, 859243 A+, 859273 A+, 859281 A+, 859305 A+, 886027 A+, 94900 A+, 94904 A+, 94906 A+, 94908 A+, 1003262 A++, 1003459 A++, 1003461 A++, 1003464 A++, 1003604 A++, 1315578 A++, 2169481 A++, 2169509 A++, 2194197 A++, 2243931 A++, 2243944 A++, 2243971 A++, 2603463 A++, 2603542 A++, 681438 A++, 858999 A++, 94897 A++, 94899 A++, 94915 A++, 94918 A++, 1003462 A++, 2169502 A++, 2169506 A++, 2244002 A++, 2244087 A++, 642132 A++, 650946 A++, 670107 A++, 677467 A++, 859005 A++, 859231 A++, 94883 A++, 348941 A+++, 486180 A+++, 710828 A+++, 859023 A+++, 859030 A+++, 859044 A+++, 859070 A+++, 859084 A+++, 859092 A+++, 859093 A+++, 859094 A+++, 859142 A+++, 859171 A+++, 859189 A+++, 859203 A+++, 859234 A+++, 859239 A+++, 859306 A+++, 654462 A++++, 859002 A++++, 94907 A++++, 94916 A++++
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Automatic Mining of ENzyme DAta
Rattus norvegicus Sprague-Dawley
Sprague-Dawley
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
strain BY4741
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
yeasts
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Automatic Mining of ENzyme DAta
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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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
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allosteric activation of pyruvate dehydrogenase phosphatase and protein phosphatase 2Calpha leads to insulin-mimetic and insulin-sensitizing effects
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
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?
peptide T-1
?
show the reaction diagram
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phosphopeptide produced by tryptic digestion of phosphorylated pyruvate dehydrogenase
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?
peptide T-2
?
show the reaction diagram
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?
peptide T-3
?
show the reaction diagram
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-
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?
RRAS(P)VA
?
show the reaction diagram
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-
?
[Asp8]tetradecapeptide + H2O
?
show the reaction diagram
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?
[mothers against decapentaplegic]-phosphate + H2O
[mothers against decapentaplegic] + phosphate
show the reaction diagram
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PDP1 directly dephosphorylates mothers against decapentaplegic (MAD) and inhibits signal transduction of decapentaplegic (DPP)
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?
[pyruvate dehydrogenase (acetyl-transferring)] phosphate + H2O
[pyruvate dehydrogenase (acetyl-transferring)] + phosphate
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
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
[pyruvate dehydrogenase (acetyl-transferring)] phosphate + H2O
[pyruvate dehydrogenase (acetyl-transferring)] + phosphate
show the reaction diagram
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-
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-
?
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
?
show the reaction diagram
[pyruvate dehydrogenase (lipoamide)]-phosphate + H2O
[pyruvate dehydrogenase (lipoamide)] + phosphate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
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noncovalently bound to PDP1r
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
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Km: 1.4 mM
Zn2+
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
COMMENTARY hide
LITERATURE
IMAGE
(R)-dehydrolipoic acid
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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
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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
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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
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together with NADH
Ca2+
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antagonizes activation by Mg2+
Calmodulin
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chlorpromazine
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Dihydrolipoamide
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fluphenazine
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glyoxylate
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at concentrations greater than 0.05 mM
myo-inositol cyclic 1,2-inositol phosphate phosphoglycan
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from human plasma, antagonist of insulin, inhibits Mg2+ and spermine stimulation
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N-ethylmaleimide
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slight inhibition
NaCl
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inhibits reactivation
p-nitrophenylphosphate
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phosphate
ruthenium red
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thioridazine
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triflupromazine
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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
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(1S)-1,5-anhydro-1-{[(1R,2R,3R,4S,5S,6S)-2,3,4,5-tetrahydroxy-6-methoxycyclohexyl]methyl}-D-galactitol
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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
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i.e. C-INS-2, the C-glycoside of INS-2
2-tetradecylglycidate
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together with insulin
4-O-beta-D-galactosaminyl-3-O-methyl-D-chiro-inositol
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i.e. INS-2, allosteric activation, docking study using crystal structure of the enzyme PDHP1, PDB ID 2PNQ, and mechanism, overview
cysteine
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reverses glyoxylate inhibition
Dichloroacetate
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together with insulin
inner lipoyl domain of dihydrolipoyl acetyltransferase
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component of substrate complex, structural requirements for binding and activation
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inositol phosphoglycan P-type
linear stimulation; linear stimulation
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Insulin
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malate
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NAD+
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reverses NADH inhibition
protamine
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putrescine
spermidine
spermine
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
29.3 - 55.1
p-nitrophenyl phosphate
0.625
peptide T-1
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phosphopeptide produced by tryptic digestion of phosphorylated pyruvate dehydrogenase
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0.22
peptide T-2
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0.106
peptide T-3
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0.053
RRAS(P)VA
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with PDPc, a member of the protein phosphatase 2C family
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0.018
RRAT(P)VA
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with PDPc, a member of the protein phosphatase 2C family
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0.0029 - 0.058
[Pyruvate dehydrogenase (lipoamide)]-phosphate
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.000001
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in white gastrocnemius muscles, wet tissue
0.0000015
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in soleus muscles, wet tissue
0.000002
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in red gastrocnemius muscles in food-deprived rats, wet tissue
0.0000025
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in red gastrocnemius muscles, wet tissue
0.0044
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in soleus muscles, in food-deprived rats, extracted mitochondrial protein
0.005
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in soleus muscles, extracted mitochondrial protein
0.0051
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in white gastrocnemius, in food-deprived rats, extracted mitochondrial protein
0.0057
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in red gastrocnemius, in food-deprived rats, extracted mitochondrial protein
0.0058
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in white gastrocnemius, extracted mitochondrial protein
0.0066
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in red gastrocnemius, extracted mitochondrial protein
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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Automatic Mining of ENzyme DAta
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lower mRNA expression compared to non diabetic control animals; mRNA expression
Manually annotated by BRENDA team
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high level of isoform PDP1
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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inner surface of the inner membrane
Manually annotated by BRENDA team
additional information
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extramitochondrial
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Manually annotated by BRENDA team