Literature summary for 2.3.1.12 extracted from

Green, T.; Grigorian, A.; Klyuyeva, A.; Tuganova, A.; Luo, M.; Popov, K.
Structural and functional insights into the molecular mechanisms responsible for the regulation of pyruvate dehydrogenase kinase 2 (2008), J. Biol. Chem., 283, 15789-15798.

Cloned(Commentary)

Cloned (Comment)	Organism
the inner lipoyl-bearing domain of dihydrolipoamide transacetylase is expressed as a GST fusion protein in Escherichia coli	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structure of pyruvate dehydrogenase kinase 2 bound to the inner lipoyl-bearing domain of dihydrolipoamide transacetylase is determined. Crystal structure reveals a pyruvate dehydrogenase kinase 2 dimer complexed with two inner lipoyl-bearing domains of dihydrolipoamide transacetylase. Comparison with apo-pyruvate dehydrogenase kinase 2 shows that dihydrolipoamide transacetylase binding causes rearrangements in PDHK2 structure that affect the dihydrolipoamidetransacetylase- and pyruvate dehydrogenase-binding sites	Homo sapiens

Crystallization (Comment)

Organism

crystal structure of pyruvate dehydrogenase kinase 2 bound to the inner lipoyl-bearing domain of dihydrolipoamide transacetylase is determined. Crystal structure reveals a pyruvate dehydrogenase kinase 2 dimer complexed with two inner lipoyl-bearing domains of dihydrolipoamide transacetylase. Comparison with apo-pyruvate dehydrogenase kinase 2 shows that dihydrolipoamide transacetylase binding causes rearrangements in PDHK2 structure that affect the dihydrolipoamidetransacetylase- and pyruvate dehydrogenase-binding sites

Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Synonyms

Synonyms	Comment	Organism
dihydrolipoyl acetyltransferase	-	Homo sapiens

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Release 2023.1 (January 2023)