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Information on EC 2.7.11.2 - [pyruvate dehydrogenase (acetyl-transferring)] kinase and Organism(s) Sus scrofa

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IUBMB Comments
The enzyme has no activating compound but is specific for its substrate. It is a mitochondrial enzyme associated with the pyruvate dehydrogenase complex in mammals. Phosphorylation inactivates EC 1.2.4.1, pyruvate dehydrogenase (acetyl-transferring).
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This record set is specific for:
Sus scrofa
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The taxonomic range for the selected organisms is: Sus scrofa
The enzyme appears in selected viruses and cellular organisms
Synonyms
pyruvate dehydrogenase kinase, pyruvate dehydrogenase kinase 4, pdh kinase, pdhk2, pdhk1, pdk-4, pyruvate dehydrogenase kinase-4, pdhk4, pyruvate dehydrogenase kinase 2, pdk-2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
kinase (phosphorylating), pyruvate dehydrogenase
-
-
-
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pyruvate dehydrogenase kinase
-
-
-
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pyruvate dehydrogenase kinase (phosphorylating)
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-
-
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pyruvate dehydrogenase kinase 4
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pyruvate dehydrogenase kinase activator protein
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phopho group transfer
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phospho group transfer
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:[pyruvate dehydrogenase (acetyl-transferring)] phosphotransferase
The enzyme has no activating compound but is specific for its substrate. It is a mitochondrial enzyme associated with the pyruvate dehydrogenase complex in mammals. Phosphorylation inactivates EC 1.2.4.1, pyruvate dehydrogenase (acetyl-transferring).
CAS REGISTRY NUMBER
COMMENTARY hide
9074-01-5
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + [pyruvate dehydrogenase (acetyl-transferring)]
ADP + [pyruvate dehydrogenase (acetyl-transferring)] phosphate
show the reaction diagram
-
-
-
?
ATP + [pyruvate dehydrogenase (lipoamide)]
ADP + [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
ATP + [pyruvate dehydrogenase (acetyl-transferring)]
ADP + [pyruvate dehydrogenase (acetyl-transferring)] phosphate
show the reaction diagram
-
-
-
?
ATP + [pyruvate dehydrogenase (lipoamide)]
ADP + [pyruvate dehydrogenase (lipoamide)] phosphate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K+
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2.2fold activation at 20 mM K+, not pH- and buffer concentration-dependent
additional information
-
no activation by Na+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Cl-
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40% inhibition at 80 mM, K+-independent inhibition
HPO42-
-
noncompetitive to ATP in the range of 1-10 mM; within physiological range, only in the presence of K+, not in its absence
pyruvate
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-
SO42-
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with the same effect as HPO42-
additional information
-
increase of ionic strength inhibits, changes of osmolarity of assay medium do not affect activity
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dihydrolipoyl transacetylase
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rate-limiting in the holo-complex
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01 - 0.025
ATP
additional information
additional information
-
changes in ionic strength
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
10
HPO42-
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pH 7.8, 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.9 - 2.7
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purified enzyme, in presence of dihydrolipoyl transacetylase, reconstituted enzyme complex
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
assay at
7.2 - 8
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broad, at 0.15 M buffer concentration
additional information
-
optimal activity within a range of 0.03 M and 0.05 M buffer concentrations
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.2 - 9
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about half-maximal activity at pH 6.2 and 9
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.19
theoretical
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
longissimus dorsal muscle
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
regulation and controlling of the pyruvate dehydrogenase complex activity in skeletal muscles by phosphorylation
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
C1IHT9_PIG
407
0
46170
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
136000
-
pyruvate dehydrogenase, gel filtration
46170
theoretical
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
subunit composition and complex structure
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
a cDNA library is constructed, the pGEM-T and pMD18-T vectors are used
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
PDK4 activity is increased in most tissues while starvation, exercise and diabetes mellitus
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kerbey, A.L.; Randle, P.J.
Pyruvate dehydrogenase kinase activity of pig heart pyruvate dehydrogenase (E1 component of pyruvate dehydrogenase complex)
Biochem. J.
231
523-529
1985
Bos taurus, Sus scrofa
Manually annotated by BRENDA team
Pawelczyk, T.; Olson, M.S.
Regulation of pyruvate dehydrogenase kinase activity from pig kidney cortex
Biochem. J.
288
369-373
1992
Sus scrofa
-
Manually annotated by BRENDA team
Lan, J.; Lei, M.G.; Zhang, Y.B.; Wang, J.H.; Feng, X.T.; Xu, D.Q.; Gui, J.F.; Xiong, Y.Z.
Characterization of the porcine differentially expressed PDK4 gene and association with meat quality
Mol. Biol. Rep.
36
2003-2010
2009
Sus scrofa (C1IHT9), Sus scrofa
Manually annotated by BRENDA team