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

BRENDA support

Refine search

Search Reference

show results
Don't show organism specific information (fast!)
Search organism in taxonomic tree (slow, choose "exact" as search mode, e.g. "mammalia" for rat,human,monkey,...)
(Not possible to combine with the first option)
Refine your search
Show additional data
do not include text mining results
include AMENDA results (Automatic Mining of Enzyme Data)
include FRENDA results (AMENDA + additional results, but less precise)

Search term:

Results 1 - 10 of 107 > >>
download as CSV
download all results as CSV
EC Number BRENDA No. Title Journal Volume Pages Year Organism PubMed ID
Show all pathways known for 2.3.1.12Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.12486210 alpha-Keto acid dehydrogenase complexes. VI. Dissociation and reconstitution of the dihydrolipoyl transacetylase of Escherichia coli J. Biol. Chem. 242 889-897 1967 Escherichia coli 5335914
Show all pathways known for 2.3.1.12Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.12486209 alpha-Keto acid dehydrogenase complexes. VII. Isolation and partial characterization of the polypeptide chains in the dihydrolipoyl transacetylase of Escherichia coli J. Biol. Chem. 242 898-901 1967 Escherichia coli 5335915
Show all pathways known for 2.3.1.12Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.12486208 alpha-Keto acid dehydrogenase complexes. IX. Effects of iodination of the tyrosyl residues on the properties of the dihydrolipoyl transacetylase of Escherichia coli J. Biol. Chem. 243 639-643 1968 Escherichia coli 4866524
Show all pathways known for 2.3.1.12Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.12486207 alpha-Keto acid dehydrogenase complexes. XII. Effects of acetylation on the activity and structure of the dihydrolipoyl transacetylase of Escherichia coli J. Biol. Chem. 244 6074-6079 1969 Escherichia coli 4900507
Show all pathways known for 2.3.1.12Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.12486206 The subunit structure of the Escherichia coli K-12 pyruvate dehydrogenase complex. The dihydrolipoamide transacetylase component Eur. J. Biochem. 20 169-178 1971 Escherichia coli 4934679
Show all pathways known for 2.3.1.12Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.1294893 alpha-Keto acid dehydrogenase complexes. XV. Purification and properties of the component enzymes of the pyruvate dehydrogenase complexes from bovine kidney and heart Arch. Biochem. Biophys. 148 327-342 1972 Bos taurus 4401694
Show all pathways known for 2.3.1.12Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.12486204 A new dihydrolipoamide transacetylase in Escherichia coli K12 Biochim. Biophys. Acta 321 143-148 1973 Escherichia coli 4584392
Show all pathways known for 2.3.1.12Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.12486203 A kinetic study of dihydrolipoyl transacetylase from bovine kidney J. Biol. Chem. 250 1921-1925 1975 Bos taurus 1089667
Show all pathways known for 2.3.1.12Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.12486202 Purification properties and subunit composition of pig heart lipoate acetyltransferase J. Biochem. 78 187-197 1975 Sus scrofa 1194249
Show all pathways known for 2.3.1.12Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.12486201 Reconstitution of the Escherichia coli pyruvate dehydrogenase complex Proc. Natl. Acad. Sci. USA 72 3068-3072 1975 Escherichia coli 1103138
Results 1 - 10 of 107 > >>
download as CSV
download all results as CSV