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Information on EC 2.3.1.168 - dihydrolipoyllysine-residue (2-methylpropanoyl)transferase and Organism(s) Bos taurus
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2.3.1.168 dihydrolipoyllysine-residue (2-methylpropanoyl)transferaseIUBMB 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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Word Map
- 2.3.1.168
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branched-chain
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bcaas
-
merits
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protein-restricted
- retinal
- urine
- metformin
- women
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maple
- l-glutamate
- syrup
- agriculture
- synthesis
- medicine
The taxonomic range for the selected organisms is: Bos taurus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
dihydrolipoamide branched chain transacylase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dihydrolipoyl transacetylase
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-
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additional information
additional information
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enzyme is the E2 component of the multienzyme complex branched-chain alpha-keto acid dehydrogenase, i.e. branched-chain 2-oxo acid dehydrogenase
additional information
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enzyme is the E2 component of the multienzyme complex branched-chain alpha-keto acid dehydrogenase, i.e. branched-chain 2-oxo acid dehydrogenase
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
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
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
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
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
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2-methylpropanoyl-CoA + enzyme N6-(dihydrolipoyl)lysine = CoA + enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine
2-methylpropanoyl-CoA + enzyme N6-(dihydrolipoyl)lysine = CoA + enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine
random bi bi mechanism
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2-methylpropanoyl-CoA + enzyme N6-(dihydrolipoyl)lysine = CoA + enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine
His391 is involved in the catalytic reaction
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2-methylpropanoyl-CoA + enzyme N6-(dihydrolipoyl)lysine = CoA + enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine
the active site is located in the inner core domain
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
alkyl group transfer
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PATHWAY SOURCE
PATHWAYS
KEGG
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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.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-methylpropanoyl-CoA + dihydrolipoamide
CoA + S-2-methylpropanoyldihydrolipoamide
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identification by mass spectrometry
r
2-methylpropanoyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine
acetyl-CoA + dihydrolipoamide
CoA + S-acetyldihydrolipoamide
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low activity
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r
isobutyryl-CoA + dihydrolipoamide
CoA + S-isobutyryldihydrolipoamide
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-
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r
2-methylpropanoyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine
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-
-
?
2-methylpropanoyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine
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-
-
?
2-methylpropanoyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine
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-
-
?
2-methylpropanoyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine
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-
-
?
2-methylpropanoyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine
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-
-
?
2-methylpropanoyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine
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-
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r
2-methylpropanoyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine
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recombinant apo-E2 devoid of lipoic acid is fully active
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?
2-methylpropanoyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine
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enzyme contains 1 lipoyl residue per E2 chain of branched-chain 2-oxo acid dehydrogenase
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?
2-methylpropanoyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine
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multienzyme complex, scheme of the reaction steps
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?
isovaleryl-CoA + dihydrolipoamide
CoA + S-isovaleryldihydrolipoamide
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-
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r
isovaleryl-CoA + dihydrolipoamide
CoA + S-isovaleryldihydrolipoamide
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recombinant enzyme, i.e. E2 domain, overexpressed in Escherichia coli
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r
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-methylpropanoyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine
2-methylpropanoyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine
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-
-
?
2-methylpropanoyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine
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-
-
?
2-methylpropanoyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine
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-
-
r
2-methylpropanoyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine
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multienzyme complex, scheme of the reaction steps
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?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
CoA
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product inhibition, competitive to acyl-CoA, noncompetitive to dihydrolipoamide
additional information
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limited proteolysis by trypsin results in the complete loss of the overall activity of the enzyme complex, but does not affect dihydrolipoyllysine-residue (2-methylpropanoyl)transferase activity; NEM and thiamine diphosphate have no effect
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ODB2_BOVIN
482
0
53410
Swiss-Prot
Mitochondrion (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
84000
-
E2-trimer, sucrose density gradient centrifugation in presence of the chaotropic reagent guanidinium-HCl
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
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
additional information
-
in vitro reconstitution of the 24-meric E2 inner core requires the chaperonins GroEL and GroES
additional information
-
the 24-mer can be separated into active trimers of MW 84 kDa by incubation in 1.5 M guanidinium-HCl at 25°C, process is reversible, and removal of guanidinium-HCl leads to spontenaous reassembly to an active 24-mer
additional information
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enzyme shows the E2 structure of 3 folded domains: lipoyl-bearing, E3-binding, and inner core, typical for all E2 protein of alpha-keto acid dehydrogenases
additional information
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lipoate-free inner E2 core: 26 kDa fragment contains the active site, 22 kDa fragment B is the subunit-binding domain, fragments are gained by tryptic digest
additional information
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the 26 kDa fragment from tryptic digest is the catalytically active part of the enzyme
additional information
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assembly of 24 E2 subunits into a cubic structure, forming the core of the mammalian branched-chain alpha-keto acid dehydrogenase multienzyme complex
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant E2c, residues 161-421, fused to maltose-binding protein from Escherichia coli
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA sequence determination, overexpression of wild-type, lipol-free apo-enzyme, and mutants 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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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
E2c, completely unfolded in 4.5 M guanidinium chloride, is diluted 100fold at 25°C 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
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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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Chuang, D.T.; Hu, C.C.; Ku, L.S.; Niu, W.L.; Myers, D.E.; Cox, R.P.
Catalytic and structural properties of the dihydrolipoyl transacylase component of bovine branched-chain alpha-keto acid dehydrogenase
J. Biol. Chem.
259
9277-9284
1984
Bos taurus
Chuang, D.T.; Hu, C.W.; Ku, L.S.; Markovitz, P.J.; Cox, R.P.
Subunit structure of the dihydrolipoyl transacylase component of branched-chain alpha-keto acid dehydrogenase complex from bovine liver. Characterization of the inner transacylase core
J. Biol. Chem.
260
13779-13786
1985
Bos taurus
Hu, C.W.; Griffin, T.A.; Lau, K.S.; Cox, R.P.; Chuang, D.T.
Subunit structure of the dihydrolipoyl transacylase component of branched-chain alpha-keto acid dehydrogenase complex from bovine liver. Mapping of the lipoyl-bearing domain by limited proteolysis
J. Biol. Chem.
261
343-349
1986
Bos taurus
Chuang, D.T.; Fisher, C.W.; Lau, K.S.; Griffin, T.A.; Wynn, R.M.; Cox, R.P.
Maple syrup urine disease: domain structure, mutations and exon skipping in the dihydrolipoyl transacylase (E2) component of the branched-chain alpha-keto acid dehydrogenase complex
Mol. Biol. Med.
8
49-63
1991
Bos taurus, Homo sapiens (P11182)
Ansari, A.A.; Neckelmann, N.; Villinger, F.; Leung, P.; Danner, D.J.; Brar, S.S.; Zhao, S.; Gravanis, M.B.; Mayne, A.; Gershwin, M.E.
Epitope mapping of the branched chain alpha-ketoacid dehydrogenase dihydrolipoyl transacylase (BCKD-E2) protein that reacts with sera from patients with idiopathic dilated cardiomyopathy
J. Immunol.
153
4754-4765
1994
Bos taurus, Homo sapiens
Chuang, J.L.; Davie, J.R.; Wynn, R.M.; Chuang, D.T.
Production of recombinant mammalian holo-E2 and E3 and reconstitution of functional branched-chain alpha-keto acid dehydrogenase complex with recombinant E1
Methods Enzymol.
324
192-200
2000
Bos taurus
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