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 15 > >>
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 3.6.1.54Display the word mapDisplay the reaction diagram Show all sequences 3.6.1.54758374 Crystal structures of the UDP-diacylglucosamine pyrophosphohydrase LpxH from Pseudomonas aeruginosa Sci. Rep. 6 32822 2016 Pseudomonas aeruginosa 27609419
Show all pathways known for 3.6.1.54Display the word mapDisplay the reaction diagram Show all sequences 3.6.1.54757780 Structure of the essential Haemophilus influenzae UDP-diacylglucosamine pyrophosphohydrolase LpxH in lipid A biosynthesis Nat. Microbiol. 1 16154 2016 Haemophilus influenzae 27780190
Show all pathways known for 3.6.1.54Display the word mapDisplay the reaction diagram Show all sequences 3.6.1.54755698 Structure-activity relationship of sulfonyl piperazine LpxH inhibitors analyzed by an LpxE-coupled malachite green assay ACS Infect. Dis. 5 641-651 2019 Escherichia coli 30721024
Show all pathways known for 3.6.1.54Display the word mapDisplay the reaction diagram Show all sequences 3.6.1.54757234 Substrate specificity of the pyrophosphohydrolase LpxH determines the asymmetry of Bordetella pertussis lipid A J. Biol. Chem. 294 7982-7989 2019 Neisseria meningitidis 30926608
Show all pathways known for 3.6.1.54Display the word mapDisplay the reaction diagram Show all sequences 3.6.1.54757216 The substrate-binding cap of the UDP-diacylglucosamine pyrophosphatase LpxH is highly flexible, enabling facile substrate binding and product release J. Biol. Chem. 293 7969-7981 2018 Escherichia coli 29626094
Show all pathways known for 3.6.1.54Display the word mapDisplay the reaction diagram Show all sequences 3.6.1.54758137 Toxic accumulation of lps pathway intermediates underlies the requirement of LpxH for growth of acinetobacter Baumannii ATCC 19606 PLoS ONE 11 e0160918 2016 Acinetobacter baumannii 27526195
Show all pathways known for 3.6.1.54Display the word mapDisplay the reaction diagram Show all sequences 3.6.1.54758137 Toxic accumulation of lps pathway intermediates underlies the requirement of LpxH for growth of acinetobacter Baumannii ATCC 19606 PLoS ONE 11 e0160918 2016 Acinetobacter baumannii ATCC 19606 27526195
Show all pathways known for 3.6.1.54Display the word mapDisplay the reaction diagram Show all sequences 3.6.1.54698721 Accumulation of the lipid A precursor UDP-2,3-diacylglucosamine in an Escherichia coli mutant lacking the lpxH gene J. Biol. Chem. 277 25947-25956 2002 Escherichia coli 12000771
Show all pathways known for 3.6.1.54Display the word mapDisplay the reaction diagram Show all sequences 3.6.1.54698721 Accumulation of the lipid A precursor UDP-2,3-diacylglucosamine in an Escherichia coli mutant lacking the lpxH gene J. Biol. Chem. 277 25947-25956 2002 Pseudomonas aeruginosa 12000771
Show all pathways known for 3.6.1.54Display the word mapDisplay the reaction diagram Show all sequences 3.6.1.54718879 An alternative route for UDP-diacylglucosamine hydrolysis in bacterial lipid A biosynthesis Biochemistry 49 6715-6726 2010 Caulobacter vibrioides 20608695
Results 1 - 10 of 15 > >>
download as CSV
download all results as CSV