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 43 > >>
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 1.14.11.17Display the word mapDisplay the reaction diagram Show all sequences 1.14.11.17765270 Strongly coupled redox-linked conformational switching at the active site of the non-heme iron-dependent dioxygenase, TauD J. Phys. Chem. B 123 7785-7793 2019 Escherichia coli 31433947
Show all pathways known for 1.14.11.17Display the word mapDisplay the reaction diagram Show all sequences 1.14.11.17765270 Strongly coupled redox-linked conformational switching at the active site of the non-heme iron-dependent dioxygenase, TauD J. Phys. Chem. B 123 7785-7793 2019 Escherichia coli K12 31433947
Show all pathways known for 1.14.11.17Display the word mapDisplay the reaction diagram Show all sequences 1.14.11.17765089 The Irving-Williams series and the 2-His-1-carboxylate facial triad a thermodynamic study of Mn2+, Fe2+, and Co2+ binding to taurine/?-ketoglutarate dioxygenase (TauD) J. Biol. Inorg. Chem. 23 785-793 2018 Escherichia coli 29923040
Show all pathways known for 1.14.11.17Display the word mapDisplay the reaction diagram Show all sequences 1.14.11.17765089 The Irving-Williams series and the 2-His-1-carboxylate facial triad a thermodynamic study of Mn2+, Fe2+, and Co2+ binding to taurine/?-ketoglutarate dioxygenase (TauD) J. Biol. Inorg. Chem. 23 785-793 2018 Escherichia coli K12 29923040
Show all pathways known for 1.14.11.17Display the word mapDisplay the reaction diagram Show all sequences 1.14.11.17764972 Structural origin of the large redox-linked reorganization in the 2-oxoglutarate dependent oxygenase, TauD J. Am. Chem. Soc. 141 15318-15326 2019 Escherichia coli 31475523
Show all pathways known for 1.14.11.17Display the word mapDisplay the reaction diagram Show all sequences 1.14.11.17764972 Structural origin of the large redox-linked reorganization in the 2-oxoglutarate dependent oxygenase, TauD J. Am. Chem. Soc. 141 15318-15326 2019 Escherichia coli K12 31475523
Show all pathways known for 1.14.11.17Display the word mapDisplay the reaction diagram Show all sequences 1.14.11.17764499 Electrostatic perturbations in the substrate-binding pocket of taurine/alpha-ketoglutarate dioxygenase determine its selectivity Chemistry 28 e202104167 2022 Escherichia coli 34967481
Show all pathways known for 1.14.11.17Display the word mapDisplay the reaction diagram Show all sequences 1.14.11.17764499 Electrostatic perturbations in the substrate-binding pocket of taurine/alpha-ketoglutarate dioxygenase determine its selectivity Chemistry 28 e202104167 2022 Escherichia coli K12 34967481
Show all pathways known for 1.14.11.17Display the word mapDisplay the reaction diagram Show all sequences 1.14.11.17764167 Structure of a ferryl mimic in the archetypal iron(II)- and 2-(oxo)-glutarate-dependent dioxygenase, TauD Biochemistry 58 4218-4223 2019 Escherichia coli 31503454
Show all pathways known for 1.14.11.17Display the word mapDisplay the reaction diagram Show all sequences 1.14.11.17764167 Structure of a ferryl mimic in the archetypal iron(II)- and 2-(oxo)-glutarate-dependent dioxygenase, TauD Biochemistry 58 4218-4223 2019 Escherichia coli K12 31503454
Results 1 - 10 of 43 > >>
download as CSV
download all results as CSV