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EC Number
BRENDA No.
Title
Journal
Volume
Pages
Year
Organism
PubMed ID
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
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
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
1.3.98.3
686237
The radical SAM superfamily
Crit. Rev. Biochem. Mol. Biol.
43
63-88
2008
Homo sapiens
18307109
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
713258
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
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