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<< < Results 11 - 20 of 25 > >>
EC Number BRENDA No. Title Journal Volume Pages Year Organism PubMed ID
Show all pathways known for 1.3.98.3Display the word mapDisplay the reaction diagram Show all sequences 1.3.98.3687282 Characterization and mechanistic study of a radical SAM dehydrogenase in the biosynthesis of butirosin J. Am. Chem. Soc. 129 15147-15155 2007 Niallia circulans 18001019
Show all pathways known for 1.3.98.3Display the word mapDisplay the reaction diagram Show all sequences 1.3.98.3685280 Mechanistic study on the reaction of a radical SAM dehydrogenase BtrN by electron paramagnetic resonance spectroscopy Biochemistry 47 8950-8960 2008 Niallia circulans 18672902
Show all pathways known for 1.3.98.3Display the word mapDisplay the reaction diagram Show all sequences 1.3.98.3686237 The radical SAM superfamily Crit. Rev. Biochem. Mol. Biol. 43 63-88 2008 Homo sapiens 18307109
Show all pathways known for 1.3.98.3Display the word mapDisplay the reaction diagram Show all sequences 1.3.98.3713258 Functional differentiation of two analogous coproporphyrinogen III oxidases for heme and chlorophyll biosynthesis pathways in the cyanobacterium Synechocystis sp. PCC 6803 Plant Cell Physiol. 51 650-663 2010 Synechocystis sp. 20194361
Show all pathways known for 1.3.98.3Display the word mapDisplay the reaction diagram Show all sequences 1.3.98.3711084 Structural characterization reveals that viperin is a radical S-adenosyl-L-methionine (SAM) enzyme Biochem. Biophys. Res. Commun. 391 1390-1395 2010 Homo sapiens 20026307
Show all pathways known for 1.3.98.3Display the word mapDisplay the reaction diagram Show all sequences 1.3.98.3712016 The antiviral protein viperin is a radical SAM enzyme FEBS Lett. 584 1263-1267 2010 Homo sapiens 20176015
Show all pathways known for 1.3.98.3Display the word mapDisplay the reaction diagram Show all sequences 1.3.98.3711348 The oxygen-independent coproporphyrinogen III oxidase HemN utilizes harderoporphyrinogen as a reaction intermediate during conversion of coproporphyrinogen III to protoporphyrinogen IX Biol. Chem. 391 55-63 2010 Escherichia coli 19919179
Show all pathways known for 1.3.98.3Display the word mapDisplay the reaction diagram Show all sequences 1.3.98.3724235 Lactococcus lactis HemW (HemN) is a haem-binding protein with a putative role in haem trafficking Biochem. J. 442 335-343 2012 Lactococcus lactis 22142238
Show all pathways known for 1.3.98.3Display the word mapDisplay the reaction diagram Show all sequences 1.3.98.3745799 Coproporphyrin III excretion identifies the anaerobic coproporphyrinogen III oxidase HemN as a copper target in the Cu+-ATPase mutant copA- of Rubrivivax gelatinosus Mol. Microbiol. 88 339-351 2013 Rubrivivax gelatinosus 23448658
Show all pathways known for 1.3.98.3Display the word mapDisplay the reaction diagram Show all sequences 1.3.98.3726009 Coproporphyrin III excretion identifies the anaerobic coproporphyrinogen III oxidase HemN as a copper target in the Cu+-ATPase mutant copA- of Rubrivivax gelatinosus Mol. Microbiol. 88 339-351 2013 Rubrivivax gelatinosus 23448658
<< < Results 11 - 20 of 25 > >>