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Literature summary for 1.2.4.4 extracted from

  • Naik, M.T.; Chang, Y.C.; Huang, T.H.
    Folding kinetics of the lipoic acid-bearing domain of human mitochondrial branched chain alpha-ketoacid dehydrogenase complex (2002), FEBS Lett., 530, 133-138.
    View publication on PubMed
Search for more literature for 1.2.4.4

Cloned(Commentary)

Cloned (Comment) Organism
expression of C-terminally His-tagged lipoic acid-bearing domain of enzyme complex component E2 with an extra methionine at the N-terminus and a glutamic acid and leucine at the C-terminus in Escherichia coli strain BL21(DE3) Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
 Homo sapiens 5739
-

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged lipoic acid-bearing domain of enzyme complex component E2 by nickel affinity chromatography and gel filtration to over 95% purity Homo sapiens

Renatured (Commentary)

Renatured (Comment) Organism
denaturating of the lipoic acid-bearing domain of enzyme complex component E2 by 8 M urea, refolding by 10fold dilution, folding kinetics of the reversible 2-step mechanism Homo sapiens

Subunits

Subunits Comment Organism
More structure analysis, folding kinetics of the lipoic acid-bearing domain of enzyme complex component E2, a reversible 2-step mechanism for interconversion of the enzyme from native to denatured state without stable or kinetic intermediates, overview Homo sapiens

Synonyms

Synonyms Comment Organism
BCKD
-
 Homo sapiens
branched chain alpha-ketoacid dehydrogenase complex
-
 Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
22
-
 assay at Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Homo sapiens