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 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 7.1.1.3714885 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 7.1.1.3714129 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 7.1.1.3714285 Purification and properties of cytochrome bo-type ubiquinol oxidase from a marine bacterium Vibrio alginolyticus Biochim. Biophys. Acta 1141 283-287 1993 Vibrio alginolyticus 8443214
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
Show all pathways known for 7.1.1.3Display the word mapDisplay the reaction diagram Show all sequences 7.1.1.3714131 Site-directed mutagenesis of highly conserved residues in helix VIII of subunit I of the cytochrome bo ubiquinol oxidase from Escherichia coli: an amphipathic transmembrane helix that may be important in conveying protons to the binuclear center Biochemistry 32 11173-11180 1993 Escherichia coli 8218180
Show all pathways known for 7.1.1.3Display the word mapDisplay the reaction diagram Show all sequences 7.1.1.3714131 Site-directed mutagenesis of highly conserved residues in helix VIII of subunit I of the cytochrome bo ubiquinol oxidase from Escherichia coli: an amphipathic transmembrane helix that may be important in conveying protons to the binuclear center Biochemistry 32 11173-11180 1993 Escherichia coli GL101 8218180
Show all pathways known for 7.1.1.3Display the word mapDisplay the reaction diagram Show all sequences 7.1.1.3714132 Site-directed mutants of the cytochrome bo ubiquinol oxidase of Escherichia coli: amino acid substitutions for two histidines that are putative CuB ligands Biochemistry 32 11524-11529 1993 Escherichia coli 8218219
Results 1 - 10 of 61 > >>