Information on EC 3.1.3.52 - [3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring)]-phosphatase

for references in articles please use BRENDA:EC3.1.3.52
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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.1.3.52
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RECOMMENDED NAME
GeneOntology No.
[3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring)]-phosphatase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
[3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring)] phosphate + H2O = [3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring)] + phosphate
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
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SYSTEMATIC NAME
IUBMB Comments
[3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring)]-phosphate phosphohydrolase
A mitochondrial enzyme associated with the 3-methyl-2-oxobutanoate dehydrogenase complex. Simultaneously dephosphorylates and activates EC 1.2.4.4 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring), that has been inactivated by phosphorylation.
CAS REGISTRY NUMBER
COMMENTARY hide
87244-20-0
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88086-29-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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Simvastatin administration increases BCKDH activity state and stimulates branched-chain amino acids (BCAAs) catabolism in rats fed with the low protein diet In contrast to rats subjected to protein restriction simvastatin has no effect on liver BCKDH activity in rats fed with the standard diet
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
[3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate + H2O
[3-methyl-2-oxobutanoate 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
[3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate + H2O
[3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] + phosphate
show the reaction diagram
additional information
?
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PP2Cm interacts with the BCKD E2 subunit and competes with the BCKD kinase in a substrate-dependent and mutually exclusive manner
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
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required
additional information
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active in absence of divalent cation
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetyl-CoA
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acyl-CoA
CDP
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50% inhibition at 400 mM; inhibition is completely reversed by Mg2+
CTP
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50% inhibition at 250 mM; inhibition is completely reversed by Mg2+
guanosine 5'-(beta,gamma-imido)triphosphate
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heparin
Inhibitor protein
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isobutyryl-CoA
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isovaleryl-CoA
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nucleoside diphosphates
nucleoside triphosphates
UDP
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50% inhibition at 250 mM; inhibition is completely reversed by Mg2+
UTP
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50% inhibition at 100 mM; inhibition is completely reversed by Mg2+
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
histone H3
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stimulates at 0.036 mg/ml
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poly(L-arginine)
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stimulates 1.5-3fold at 0.0036 mg/ml
poly(L-lysine)
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stimulates 1.5-3fold at 0.0036 mg/ml
protamine
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stimulates 1.5-3fold at 0.0036 mg/ml
simvastatin
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Skeletal muscle factor
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stimulates
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00000013
Inhibitor protein
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pH 7.3, 30°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.158
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0.24
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2.328
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22.86
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 7.3
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
33000
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1 * 33000, catalytic subunit, SDS-PAGE
230000
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gel filtration, under conditions of high dilution, low MW form
460000
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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alpha,beta
additional information
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, stable for at least 6 months
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-80°C, stable for at least 2 weeks
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4°C, partially purified enzyme stable for several weeks
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a high and a low MW form
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catalytic subunit
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in HEK293 cells
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
branched-chain amino acid (BCAA) controls PP2Cm gene transcription
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PP2Cm expression is highly enriched in brain, heart, liver, kidney and diaphragm
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skeletal muscle
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A193X
single-nucleotide polymorphisms (SNPs) in human PP2Cm: mutant demonstrate basal activity against branched-chain alpha-keto dehydrogenase (BCKD) but impaired responsiveness to branched-chain-alpha-keto acids (BCKAs)
E321K
single-nucleotide polymorphisms (SNPs) in human PP2Cm: mutant demonstrate basal activity against branched-chain alpha-keto dehydrogenase (BCKD) but impaired responsiveness to branched-chain-alpha-keto acids (BCKAs). Mutant is not detected by immunoblot using human PP2Cm antibody. Therefore, it remains unclear whether this mutant is phosphatase dead due to loss-of-function mutations or unstable due to premature truncation
F359X
single-nucleotide polymorphisms (SNPs) in human PP2Cm: frameshift mutant shows no phosphatase activity at basal or after branched-chain-alpha-keto acids (BCKA) treatment. Mutant is not detected by immunoblot using human PP2Cm antibody. Therefore, it remains unclear whether this mutant is phosphatase dead due to loss-of-function mutations or unstable due to premature truncation
I167T
single-nucleotide polymorphisms (SNPs) in human PP2Cm: mutation has no an elevated activity compared to wild-type
N94K
single-nucleotide polymorphisms (SNPs) in human PP2Cm: mutation has no impact on PP2Cm activity
additional information
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motifs responsible for PP2Cm and E2 interaction: using deletion mutants it is shown that the region between the residues 46 and 61 is critical to the association of PP2Cm with the complex