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 232 > >>
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 2.6.1.1Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.1759587 Aspartate aminotransferase is potently inhibited by copper complexes Exploring copper complex-binding proteome J. Inorg. Biochem. 170 46-54 2017 Rattus norvegicus 28219031
Show all pathways known for 2.6.1.1Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.1759824 Aspartate aminotransferase Rv3722c governs aspartate-dependent nitrogen metabolism in Mycobacterium tuberculosis Nat. Commun. 11 1960 2020 Mycobacterium tuberculosis 32327655
Show all pathways known for 2.6.1.1Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.1759824 Aspartate aminotransferase Rv3722c governs aspartate-dependent nitrogen metabolism in Mycobacterium tuberculosis Nat. Commun. 11 1960 2020 Mycobacterium tuberculosis H37Rv 32327655
Show all pathways known for 2.6.1.1Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.1758821 Biochemical characterization and structure-based mutational analysis provide insight into the binding and mechanism of action of novel aspartate aminotransferase inhibitors Biochemistry 57 6604-6614 2018 Homo sapiens 30365304
Show all pathways known for 2.6.1.1Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.1759006 Chemoenzymatic synthesis of L-3,4-dimethoxyphenyl-alanine and its analogues using aspartate aminotransferase as a key catalyst Catal. Commun. 120 28-32 2019 Escherichia coli -
Show all pathways known for 2.6.1.1Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.1759136 Conversion of cysteine to 3-mercaptopyruvic acid by bacterial aminotransferases Enzyme Microb. Technol. 99 38-48 2017 Cupriavidus necator 28193330
Show all pathways known for 2.6.1.1Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.1759136 Conversion of cysteine to 3-mercaptopyruvic acid by bacterial aminotransferases Enzyme Microb. Technol. 99 38-48 2017 Shimwellia blattae 28193330
Show all pathways known for 2.6.1.1Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.1759136 Conversion of cysteine to 3-mercaptopyruvic acid by bacterial aminotransferases Enzyme Microb. Technol. 99 38-48 2017 Escherichia coli 28193330
Show all pathways known for 2.6.1.1Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.1759136 Conversion of cysteine to 3-mercaptopyruvic acid by bacterial aminotransferases Enzyme Microb. Technol. 99 38-48 2017 Advenella mimigardefordensis 28193330
Show all pathways known for 2.6.1.1Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.1759136 Conversion of cysteine to 3-mercaptopyruvic acid by bacterial aminotransferases Enzyme Microb. Technol. 99 38-48 2017 Advenella mimigardefordensis DPN7 28193330
Results 1 - 10 of 232 > >>
download as CSV
download all results as CSV