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 51 - 60 of 61 > >>
EC Number BRENDA No. Title Journal Volume Pages Year Organism PubMed ID
Show all pathways known for 7.1.1.3Display the word mapDisplay the reaction diagram Show all sequences 7.1.1.3715399 Substitutions of charged amino acid residues conserved in subunit I perturb the redox metal centers of the Escherichia coli bo-type ubiquinol oxidase J. Biochem. 122 422-429 1997 Escherichia coli ST4676 9378723
Show all pathways known for 7.1.1.3Display the word mapDisplay the reaction diagram Show all sequences 7.1.1.3714135 Proton transfer in cytochrome bo3 ubiquinol oxidase of Escherichia coli: second-site mutations in subunit I that restore proton pumping in the mutant Asp135-->Asn Biochemistry 34 4428-4433 1995 Escherichia coli 7703256
Show all pathways known for 7.1.1.3Display the word mapDisplay the reaction diagram Show all sequences 7.1.1.3714139 Oxidation of ubiquinol by cytochrome bo3 from Escherichia coli: Kinetics of electron and proton transfer Biochemistry 36 5425-5431 1997 Escherichia coli 9154924
Show all pathways known for 7.1.1.3Display the word mapDisplay the reaction diagram Show all sequences 7.1.1.3714129 Modified, large-scale purification of the cytochrome o complex (bo-type oxidase) of Escherichia coli yields a two heme/one copper terminal oxidase with high specific activity Biochemistry 31 6917-6924 1992 Escherichia coli 1322173
Show all pathways known for 7.1.1.3Display the word mapDisplay the reaction diagram Show all sequences 7.1.1.3714129 Modified, large-scale purification of the cytochrome o complex (bo-type oxidase) of Escherichia coli yields a two heme/one copper terminal oxidase with high specific activity Biochemistry 31 6917-6924 1992 Escherichia coli RG145 1322173
Show all pathways known for 7.1.1.3Display the word mapDisplay the reaction diagram Show all sequences 7.1.1.3714885 Orientation of the haems of the ubiquinol oxidase:O2 reductase, cytochrome bo of Escherichia coli Eur. J. Biochem. 198 789-792 1991 Escherichia coli 1646721
Show all pathways known for 7.1.1.3Display the word mapDisplay the reaction diagram Show all sequences 7.1.1.3714885 Orientation of the haems of the ubiquinol oxidase:O2 reductase, cytochrome bo of Escherichia coli Eur. J. Biochem. 198 789-792 1991 Escherichia coli RG145 1646721
Show all pathways known for 7.1.1.3Display the word mapDisplay the reaction diagram Show all sequences 7.1.1.3716311 The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site Nat. Struct. Biol. 7 910-917 2000 Escherichia coli 11017202
Show all pathways known for 7.1.1.3Display the word mapDisplay the reaction diagram Show all sequences 7.1.1.3714286 Reactions of the membrane-bound cytochrome bo terminal oxidase of Escherichia coli with carbon monoxide and oxygen Biochim. Biophys. Acta 1141 95-104 1993 Escherichia coli 8382081
Show all pathways known for 7.1.1.3Display the word mapDisplay the reaction diagram Show all sequences 7.1.1.3714286 Reactions of the membrane-bound cytochrome bo terminal oxidase of Escherichia coli with carbon monoxide and oxygen Biochim. Biophys. Acta 1141 95-104 1993 Escherichia coli RG145 8382081
<< < Results 51 - 60 of 61 > >>