2.3.1.168: dihydrolipoyllysine-residue (2-methylpropanoyl)transferase
This is an abbreviated version!
For detailed information about dihydrolipoyllysine-residue (2-methylpropanoyl)transferase, go to the full flat file.
Word Map on EC 2.3.1.168
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2.3.1.168
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branched-chain
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bcaas
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merits
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protein-restricted
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retinal
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urine
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metformin
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women
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maple
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l-glutamate
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syrup
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agriculture
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synthesis
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medicine
- 2.3.1.168
-
branched-chain
-
bcaas
-
merits
-
protein-restricted
- retinal
- urine
- metformin
- women
-
maple
- l-glutamate
- syrup
- agriculture
- synthesis
- medicine
Reaction
Synonyms
Bkd, BKDH, DBT, dihydrolipoamide branched chain transacylase, dihydrolipoyl transacetylase, DLD, E2, E2p, More
ECTree
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Subunits
Subunits on EC 2.3.1.168 - dihydrolipoyllysine-residue (2-methylpropanoyl)transferase
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additional information
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lipoyl domains and inner core in the structure of multienzyme complex, overview
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C-terminus of E2 is joined to the N-terminus of E3 in the pyruvate dehydrogenase complex, subunit organization
additional information
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lipoyl domains and inner core in the structure of multienzyme complex, overview
additional information
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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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in vitro reconstitution of the 24-meric E2 inner core requires the chaperonins GroEL and GroES
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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
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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
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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
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the 26 kDa fragment from tryptic digest is the catalytically active part of the enzyme
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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
additional information
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lipoyl domains and inner core in the structure of multienzyme complex, overview
additional information
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lipoyl domains and inner core in the structure of multienzyme complex, overview
additional information
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lipoyl domains and inner core in the structure of multienzyme complex, overview
additional information
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lipoyl domains and inner core in the structure of multienzyme complex, overview
additional information
assembly of 24 E2 subunits into a cubic structure, forming the core of the mammalian branched-chain alpha-keto acid dehydrogenase multienzyme complex
additional information
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The human pyruvate dehydrogenase complex (PDC) is organized around a 60-meric dodecahedral core comprising the C-terminal domains of E2p and a noncatalytic component, E3-binding protein (E3BP), which specifically tethers E3 dimers to the PDC. Using an in vitro reconstituted PDC, densitometry, isothermal titration calorimetry, and analytical ultracentrifugation evidence provide that there are 40 copies of E2p and 20 copies of E3BP in the E2p/E3BP core. The overall maximal stoichiometry of this in vitro assembled PDC for E2p:E3BP:E1p:E3 is 40:20:40:20.
additional information
reconstitution of the multienzyme complex branched-chain alpha-keto dehydrogenase
additional information
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lipoyl domains and inner core in the structure of multienzyme complex, overview