Information on EC 2.3.1.168 - dihydrolipoyllysine-residue (2-methylpropanoyl)transferase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
2.3.1.168
-
RECOMMENDED NAME
GeneOntology No.
dihydrolipoyllysine-residue (2-methylpropanoyl)transferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2-methylpropanoyl-CoA + enzyme N6-(dihydrolipoyl)lysine = CoA + enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alkyl group transfer
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
(S)-3-methyl-2-oxopentanoate dehydrogenase (acylating)
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2-oxoisovalerate decarboxylation to isobutanoyl-CoA
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4-methyl-2-oxopentanoate dehydrogenase (acylating)
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Biosynthesis of antibiotics
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Biosynthesis of secondary metabolites
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Metabolic pathways
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NIL
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Propanoate metabolism
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Valine, leucine and isoleucine degradation
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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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
i.e. Enterococcus faecalis
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
no activity in archaebacteria
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-
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Manually annotated by BRENDA team
no activity in Desulfovibrio africanus
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-
-
Manually annotated by BRENDA team
rainbow trout
SwissProt
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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 + dihydrolipoamide
CoA + S-2-methylpropanoyldihydrolipoamide
show the reaction diagram
-
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identification by mass spectrometry
r
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
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-
?
acetyl-CoA + dihydrolipoamide
CoA + S-acetyldihydrolipoamide
show the reaction diagram
butyryl-CoA + dihydrolipoamide
CoA + S-butyryldihydrolipoamide
show the reaction diagram
-
-
-
?
isobutyryl-CoA + dihydrolipoamide
CoA + S-isobutyryldihydrolipoamide
show the reaction diagram
-
-
-
r
isocaproyl-CoA + dihydrolipoamide
CoA + S-isohexanoyldihydrolipoamide
show the reaction diagram
-
-
-
?
isovaleryl-CoA + dihydrolipoamide
CoA + S-isovaleryldihydrolipoamide
show the reaction diagram
additional information
?
-
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
2-methylpropanoyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine
show the reaction diagram
additional information
?
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enzyme is a mitochondrial autoantigen, epitope mapping is performed to define the recognition sites by sera and T cells of patients suffering idopathic dilated cardiomyopathy and dilated cardiomyopathy
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
arsenite
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strong inhibition
CoA
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product inhibition, competitive to acyl-CoA, noncompetitive to dihydrolipoamide
Mg2+
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additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.11
acetyl-CoA
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pH 7.4, 37C
2
dihydrolipoanide
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pH 7.4, 37C
0.1
isobutyryl-CoA
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pH 7.4, 37C
0.05
isovaleryl-CoA
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pH 7.4, 37C
additional information
additional information
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.173
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purified recombinant apo-enzyme
0.185
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purified native enzyme
2.38
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partially purified E2 enzyme
3.1
purified enzyme, as part of the multienzyme complex, substrate isovaleryl-CoA
additional information
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recombinant enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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assay at
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
84000
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E2-trimer, sucrose density gradient centrifugation in presence of the chaotropic reagent guanidinium-HCl
1116000
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amino acid determination and sedimentation equilibrium analysis
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24-mer
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24 * 52000, SDS-PAGE
additional information
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant apo-enzyme E2 from Escherichia coli strain XL1-Blue
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recombinant E2 fusion protein from Escherichia coli, the tag is cleaved off by factor Xa
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recombinant E2c, residues 161-421, fused to maltose-binding protein from Escherichia coli
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recombinant wild-type, apo-E2 enzyme, and mutants from Escherichia coli
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloning of full length E2 and fragments, expression in Escherichia coli JM109 as fusion protein
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DNA and amino acid sequence determination anad analysis
DNA sequence determination, overexpression of wild-type, lipol-free apo-enzyme, and mutants in Escherichia coli
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expressed as recombinant protein in Escherichia coli
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expression of apo-enzyme in Escherichia coli strain XL1-Blue, can be lipoylated in vitro
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expression of E2c, residues 161-421, fused to maltose-binding protein, which enhances the yield of the recombinant enzyme, in Escherichia coli
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gene contains a mitochondrial targeting presequence; gene E2, DNA sequence determination and analysis; pseudogene E2, DNA sequence determination and analysis, retroposon, gene corresponds to the complete mitochondrial presequence and the lipoyl-bearing domain encoded by exon I through IV of the functional gene E2
gene E2, DNA sequence determination and analysis
gene E2, DNA sequence determination and analysis; gene E2, mapping to chromosome 1p31
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H391N
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enzymatically inactive
H391Q
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enzymatically inactive
F214C
natural splicing mutant from WG-34 cells, related to the maple syrup urine disease, phenotype of homo- and heterozygous mutations in humans
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
E2c, completely unfolded in 4.5 M guanidinium chloride, is diluted 100fold at 25C and refolded in 5 mM MgATP2- and a 4fold molar excess of chaperonins GroEL and GroES at pH 7.5, full activity is recovered after 45 min, an active GroEL-E2 24-mer is formed; in vitro reconstitution of the 24-meric E2 inner core requires the chaperonins GroEL and GroES
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recombinant apo-E2 is unable to reconstitute with recombinant E1 and E3 to an active branched-chain alpha-keto dehydrogenase, but recombinant holo-E2 is able to
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reconstitution of the multienzyme complex branched-chain alpha-keto dehydrogenase
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