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

for references in articles please use BRENDA:EC2.7.11.2
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EC Tree
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:
Caenorhabditis elegans
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Word Map
The taxonomic range for the selected organisms is: Caenorhabditis elegans
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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pyruvate dehydrogenase kinase activator protein
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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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 (lipoamide)]
ADP + [pyruvate dehydrogenase (lipoamide)] phosphate
show the reaction diagram
additional information
?
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no autophosphorylation
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?
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 (lipoamide)]
ADP + [pyruvate dehydrogenase (lipoamide)] phosphate
show the reaction diagram
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catalyzes inactivation through phosphorylation of pyruvate dehydrogenase complex EC 1.2.4.1
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ir
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
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dependent on
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetyl-CoA
dihydrolipoyl transacetylase
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pyruvate dehydrogenase-complex transacetylase core
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.74
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purified recombinant enzyme, in presence of NADH and acetyl-CoA
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PDHK2_CAEEL
401
0
45282
Swiss-Prot
Mitochondrion (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45000
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2 * 45000, recombinant wild-type, SDS-PAGE
76000
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recombinant wild-type, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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2 * 45000, recombinant wild-type, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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construction of truncated enzyme forms, the N-terminally truncated form, residues 284-402, is catalytically inactive, the C-terminally reduced form, residues 1-334, shows reduced activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and truncated form from Escherichia coli as His-tagged and maltose-binding fusion protein, respectively, to homogeneity
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of truncated enzyme forms, comprising residues 284-402 and 1-334, respectively, as maltose-binding-protein fusion proteins in Escherichia coli JM109
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functional expression in Escherichia coli as His-tagged protein
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Chen, W.; Komuniecki, P.R.; Komuniecki, R.
Nematode pyruvate dehydrogenase kinases: role of the C-terminus in binding to the dihydrolipoyl transacetylase core of the pyruvate dehydrogenase complex
Biochem. J.
339
103-109
1999
Caenorhabditis elegans, Ascaris suum (O02623)
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Manually annotated by BRENDA team