Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.2.4.4 extracted from

  • Chang, C.F.; Chou, H.T.; Lin, Y.J.; Lee, S.J.; Chuang, J.L.; Chuang, D.T.; Huang, T.H.
    Structure of the subunit binding domain and dynamics of the di-domain region from the core of human branched chain alpha-ketoacid dehydrogenase complex (2006), J. Biol. Chem., 281, 28345-28353.
    View publication on PubMed
Search for more literature for 1.2.4.4

Application

Application Comment Organism
additional information NMR techniques to determine the structure of hbSBD and dynamics of several truncated constructs from the E2 component, including hbLBD (residues 1–84), hbSBD (residues 111–149), and a di-domain (hbDD) (residues 1–166) comprising hbLBD, hbSBD and the interdomain linker, the presence of the interdomain linker restricts the motional freedom of the hbSBD more significantly than hbLBD, the linker region likely exists as a soft rod rather than a flexible string in solution Homo sapiens

Cloned(Commentary)

Cloned (Comment) Organism
-
 Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
by Ni-NTA affinity chromatography Homo sapiens

Synonyms

Synonyms Comment Organism
BCKDC
-
 Homo sapiens
branched chain alpha-ketoacid dehydrogenase complex
-
 Homo sapiens
E2
-
 Homo sapiens
More
-
 Homo sapiens
More scaffold of the human branched-chain alpha-ketoacid dehydrogenase complex, contains the lipoyl-bearing domain (hbLBD), the subunit-binding domain (hbSBD) and the inner core domain that are linked to carry out E2 functions in substrate channeling and recognition Homo sapiens