Literature summary for 2.3.1.12 extracted from

Yu, X.; Hiromasa, Y.; Tsen, H.; Stoops, J.K.; Roche, T.E.; Zhou, Z.H.
Structures of the human pyruvate dehydrogenase complex cores: a highly conserved catalytic center with flexible N-terminal domains (2008), Structure, 16, 104-114.

Search for more literature for 2.3.1.12

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
additional information	a truncated version of dihydrolipoyl acetyltransferase is created lacking the N-terminal 319 amino acids	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P10515	-	-

Purification (Commentary)

Purification (Comment)	Organism
using a sephacryl S-400 HR column	Homo sapiens

Synonyms

Synonyms	Comment	Organism
dihydrolipoyl acetyltransferase	-	Homo sapiens

General Information

General Information	Comment	Organism
physiological function	structural comparison by cryo-electronmicroscopy of the human full-length and truncated dihydrolipoyl acetyltransferase cores reveal flexible linkers emanating from the edges of trimers of the internal catalytic domains. Using the secondary structure constraints revealed the 8 A cryo-electronmicroscopy and the prokaryotic truncated dihydrolipoyl acetyltransferase atomic structure as a template, a pseudo atomic model of human truncated dihydrolipoyl acetyltransferase is derived. The active sites are conserved between the truncated prokaryotic and human enzyme. Marked structural differences are apparent in the hairpin domain and in the N-terminal helix connected to the flexible linker	Homo sapiens

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Release 2023.1 (January 2023)