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EC Number
BRENDA No.
Title
Journal
Volume
Pages
Year
Organism
PubMed ID
1.3.98.3
763891
Revisiting the mechanism of the anaerobic coproporphyrinogen III oxidase HemN
Angew. Chem. Int. Ed. Engl.
58
6235-6238
2019
Escherichia coli
30884058
1.3.98.3
711084
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
1.3.98.3
724235
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
1.3.98.3
685280
Mechanistic study on the reaction of a radical SAM dehydrogenase BtrN by electron paramagnetic resonance spectroscopy
Biochemistry
47
8950-8960
2008
Niallia circulans
18672902
1.3.98.3
672473
Structural and functional comparison of HemN to other radical SAM enzymes
Biol. Chem.
386
971-980
2005
Cupriavidus necator
16218869
1.3.98.3
672473
Structural and functional comparison of HemN to other radical SAM enzymes
Biol. Chem.
386
971-980
2005
Bacillus subtilis
16218869
1.3.98.3
672473
Structural and functional comparison of HemN to other radical SAM enzymes
Biol. Chem.
386
971-980
2005
Escherichia coli
16218869
1.3.98.3
672473
Structural and functional comparison of HemN to other radical SAM enzymes
Biol. Chem.
386
971-980
2005
Cereibacter sphaeroides
16218869
1.3.98.3
672473
Structural and functional comparison of HemN to other radical SAM enzymes
Biol. Chem.
386
971-980
2005
Salmonella enterica subsp. enterica serovar Typhimurium
16218869
1.3.98.3
711348
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
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