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Information on EC 2.3.1.168 - dihydrolipoyllysine-residue (2-methylpropanoyl)transferase and Organism(s) Oncorhynchus mykiss and UniProt Accession Q8QHL7

for references in articles please use BRENDA:EC2.3.1.168
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EC Tree
IUBMB Comments
A multimer (24-mer) of this enzyme forms the core of the multienzyme 3-methyl-2-oxobutanoate dehydrogenase complex, and binds tightly both EC 1.2.4.4, 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) and EC 1.8.1.4, dihydrolipoyl dehydrogenase. The lipoyl group of this enzyme is reductively 2-methylpropanoylated by EC 1.2.4.4, and the only observed direction catalysed by EC 2.3.1.168 is that where this 2-methylpropanoyl is passed to coenzyme A. In addition to the 2-methylpropanoyl group, formed when EC 1.2.4.4 acts on the oxoacid that corresponds with valine, this enzyme also transfers the 3-methylbutanoyl and S-2-methylbutanoyl groups, donated to it when EC 1.2.4.4 acts on the oxo acids corresponding with leucine and isoleucine.
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This record set is specific for:
Oncorhynchus mykiss
UNIPROT: Q8QHL7
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Word Map
The taxonomic range for the selected organisms is: Oncorhynchus mykiss
The enzyme appears in selected viruses and cellular organisms
Synonyms
dihydrolipoamide branched chain transacylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dihydrolipoyl transacetylase
-
-
-
-
additional information
enzyme is the E2 component of the multienzyme complex branched-chain alpha-keto acid dehydrogenase, i.e. branched-chain 2-oxo acid dehydrogenase
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alkyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
2-methylpropanoyl-CoA:enzyme-N6-(dihydrolipoyl)lysine S-(2-methylpropanoyl)transferase
A multimer (24-mer) of this enzyme forms the core of the multienzyme 3-methyl-2-oxobutanoate dehydrogenase complex, and binds tightly both EC 1.2.4.4, 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) and EC 1.8.1.4, dihydrolipoyl dehydrogenase. The lipoyl group of this enzyme is reductively 2-methylpropanoylated by EC 1.2.4.4, and the only observed direction catalysed by EC 2.3.1.168 is that where this 2-methylpropanoyl is passed to coenzyme A. In addition to the 2-methylpropanoyl group, formed when EC 1.2.4.4 acts on the oxoacid that corresponds with valine, this enzyme also transfers the 3-methylbutanoyl and S-2-methylbutanoyl groups, donated to it when EC 1.2.4.4 acts on the oxo acids corresponding with leucine and isoleucine.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-methylpropanoyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine
show the reaction diagram
-
-
?
2-oxoglutaryl-CoA + dihydrolipoamide
CoA + S-(2-oxoglutaryl)dihydrolipoamide
show the reaction diagram
low activity
-
-
?
3-methylisovaleryl-CoA + dihydrolipoamide
CoA + S-(3-methylisovaleryl)dihydrolipoamide
show the reaction diagram
-
-
-
?
4-methylthiobutyryl-CoA + dihydrolipoamide
CoA + S-(4-methylthiobutyryl)dihydrolipoamide
show the reaction diagram
low activity
-
-
?
butyryl-CoA + dihydrolipoamide
CoA + S-butyryldihydrolipoamide
show the reaction diagram
-
-
-
?
isocaproyl-CoA + dihydrolipoamide
CoA + S-isohexanoyldihydrolipoamide
show the reaction diagram
-
-
-
?
isovaleryl-CoA + dihydrolipoamide
CoA + S-isovaleryldihydrolipoamide
show the reaction diagram
-
-
-
?
additional information
?
-
pyruvate is a poor substrate
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.1
purified enzyme, as part of the multienzyme complex, substrate isovaleryl-CoA
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
rainbow trout
SwissProt
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?
Q8QHL7_ONCMY
495
0
54368
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
54000
x * 54000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 54000, SDS-PAGE
additional information
reconstitution of the multienzyme complex branched-chain alpha-keto dehydrogenase
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination anad analysis
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
reconstitution of the multienzyme complex branched-chain alpha-keto dehydrogenase
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hakozaki, M.; Ono, K.; Suzuki, T.; Hata, H.; Mori, T.; Kochi, H.
Characterization of rainbow trout branched-chain alpha-keto acid dehydrogenase complex: inter-domain segments of the E2 component affect the overall activity
Comp. Biochem. Physiol. B Biochem. Mol. Biol.
132
433-442
2002
Gallus gallus (Q98UJ6), Oncorhynchus mykiss (Q8QHL7)
Manually annotated by BRENDA team