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EC Number Substrates Commentary Substrates Organism Products Commentary (Products) Reversibility
Show all pathways known for 1.3.98.3Display the word mapDisplay the reaction diagram Show all sequences 1.3.98.3coproporphyrinogen-III + S-adenosyl-L-methionine HemN requires the juxtaposition of the [4Fe-4S] cluster and the cosubstrate S-adenosyl-L-methionine. The reaction involves the stereospecific hydrogen abstraction of the pro-S hydrogen from the propionate side chain beta-C of coproporphyrinogen-III, involvement of a coproporphyrinogenyl III radical, which is then decarboxylated releasing CO2 and forming the vinyl group, enzyme structure, two-domain enzyme consisting of the catalytic N- and an alpha-helical C-terminal domain, substrate binding mode Escherichia coli protoporphyrinogen IX + CO2 + L-methionine + 5'-deoxyadenosine - ?
Show all pathways known for 1.3.98.3Display the word mapDisplay the reaction diagram Show all sequences 1.3.98.3coproporphyrinogen-III + S-adenosyl-L-methionine mechanism, the S-adenosyl-L-methionine sulfonium sulfur is near both the Fe and neighboring sulfur of the cluster allowing single electron transfer from the 4Fe-4S cluster to the S-adenosyl-L-methionine sulfonium. S-adenosyl-L-methionine is cleaved yielding a highly oxidizing 5’-deoxyadenosyl radical, HemN binds a second S-adenosyl-L-methionine immediately adjacent to the first and may thus successively catalyze two propionate decarboxylations. Cofactor geometry required for Radical SAM catalysis, detailed enzyme structure, two distinct domains, domain structure, S-adenosyl-L-methionine binding mode Escherichia coli protoporphyrinogen IX + CO2 + L-methionine + 5'-deoxyadenosine - ?
Show all pathways known for 1.3.98.3Display the word mapDisplay the reaction diagram Show all sequences 1.3.98.3harderoporphyrinogen + 2 S-adenosyl-L-methionine HemN can utilize chemically synthesized harderoporphyrinogen as a substrate and converts it to protoporphyrinogen IX Escherichia coli protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine - ?
Show all pathways known for 1.3.98.3Display the word mapDisplay the reaction diagram Show all sequences 1.3.98.3harderoporphyrinogen + S-adenosyl-L-methionine chemical substrate sythesis, overview Escherichia coli protoporphyrinogen IX + CO2 + L-methionine + 5'-deoxyadenosine - ?
Show all pathways known for 1.3.98.3Display the word mapDisplay the reaction diagram Show all sequences 1.3.98.3more no activity with 1L-chiro-inositol, muco-inositol, allo-inositol, D-glucose, D-glucosamine, D-xylose, 1D-chiro-inositol, and 2,3-dideoxy-scyllo-inosose Niallia circulans ? - ?
Show all pathways known for 1.3.98.3Display the word mapDisplay the reaction diagram Show all sequences 1.3.98.3more HemW shows no coproporphyrinogen III oxidase activity in vivo or in vitro Lactococcus lactis ? - ?
Show all pathways known for 1.3.98.3Display the word mapDisplay the reaction diagram Show all sequences 1.3.98.3myo-inositol + S-adenosyl-L-methionine 0.9% activity compared to 2-deoxy-scyllo-inosamine Niallia circulans ? + CO2 + L-methionine + 5'-deoxyadenosine - ?
Show all pathways known for 1.3.98.3Display the word mapDisplay the reaction diagram Show all sequences 1.3.98.3scyllo-inositol + S-adenosyl-L-methionine 3.3% activity compared to 2-deoxy-scyllo-inosamine Niallia circulans ? + CO2 + L-methionine + 5'-deoxyadenosine - ?
Show all pathways known for 1.3.98.3Display the word mapDisplay the reaction diagram Show all sequences 1.3.98.3coproporphyrinogen III + 2 S-adenosyl-L-methionine reductive cleavage of S-adenosyl-L-methionine to produce methionine and a 5'-deoxyadenosyl radical intermediate, a reaction characteristic of the radical SAM superfamily, due to the presence of a CX3CX2C motif Homo sapiens protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine detection of the cleavage and degradation products and analysis by mass spectrometry, overview ?
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