1.3.98.3 2-deoxy-scyllo-inosamine + S-adenosyl-L-methionine - Niallia circulans 3-amino-2,3-dideoxy-scyllo-inosose + CO2 + L-methionine + 5'-deoxyadenosine - r 395504 1.3.98.3 2-deoxy-scyllo-inosamine + S-adenosyl-L-methionine 100% activity Niallia circulans 3-amino-2,3-dideoxy-scyllo-inosose + CO2 + L-methionine + 5'-deoxyadenosine - ? 395504 1.3.98.3 2-deoxystreptamine + S-adenosyl-L-methionine 14.4% activity compared to 2-deoxy-scyllo-inosamine Niallia circulans ? + CO2 + L-methionine + 5'-deoxyadenosine - ? 395505 1.3.98.3 coproporphyrinogen III + 2 S-adenosyl-L-methionine - Staphylococcus aureus protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine - ? 413336 1.3.98.3 coproporphyrinogen III + 2 S-adenosyl-L-methionine - Escherichia coli protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine - ? 413336 1.3.98.3 coproporphyrinogen III + 2 S-adenosyl-L-methionine - Homo sapiens protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine - ? 413336 1.3.98.3 coproporphyrinogen III + 2 S-adenosyl-L-methionine - Rubrivivax gelatinosus protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine - ? 413336 1.3.98.3 coproporphyrinogen III + 2 S-adenosyl-L-methionine sll1876 encodes HemN operating under micro-oxic conditions Synechocystis sp. protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine - ? 413336 1.3.98.3 coproporphyrinogen III + 2 S-adenosyl-L-methionine via reaction intermediate harderoporphyrinogen, not isoharderoporphyrinogen Escherichia coli protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine - ? 413336 1.3.98.3 coproporphyrinogen III + 2 S-adenosyl-L-methionine only Sll1876 shows CPO activity under anaerobic conditions, Sll1917 is inactive Synechocystis sp. protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine - ? 413336 1.3.98.3 coproporphyrinogen 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 ? 413336 1.3.98.3 coproporphyrinogen III + 2 S-adenosyl-L-methionine via reaction intermediate harderoporphyrinogen, not isoharderoporphyrinogen. During this reaction the propionate side chains on pyrrole rings A and B of coproporphyrinogen III are oxidatively decarboxylated to the corresponding vinyl groups of protoporphyrinogen IX. Two molecules of CO2 are released during the reaction and a final electron acceptor is required to take up two electrons from each side chain Escherichia coli protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine - ? 413336 1.3.98.3 coproporphyrinogen III + 2 S-adenosyl-L-methionine conversion of coproporphyrinogen III to protoporphyrinogen IX via the reaction intermediate harderoporphyrinogen Escherichia coli protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine - ? 413336 1.3.98.3 coproporphyrinogen III + S-adenosyl-L-methionine - Vibrio vulnificus protoporphyrinogen IX + CO2 + L-methionine + 5'-deoxyadenosine - ? 396779 1.3.98.3 coproporphyrinogen III + S-adenosyl-L-methionine - Vibrio vulnificus ATCC 29307 protoporphyrinogen IX + CO2 + L-methionine + 5'-deoxyadenosine - ? 396779 1.3.98.3 coproporphyrinogen-III + S-adenosyl-L-methionine - Escherichia coli protoporphyrinogen IX + CO2 + L-methionine + 5'-deoxyadenosine - ? 375097 1.3.98.3 coproporphyrinogen-III + S-adenosyl-L-methionine - Homo sapiens protoporphyrinogen IX + CO2 + L-methionine + 5'-deoxyadenosine - ? 375097 1.3.98.3 coproporphyrinogen-III + S-adenosyl-L-methionine - Cereibacter sphaeroides protoporphyrinogen IX + CO2 + L-methionine + 5'-deoxyadenosine - ? 375097 1.3.98.3 coproporphyrinogen-III + S-adenosyl-L-methionine HemN catalyzes the essential conversion of coproporphyrinogen-III to protoporphyrinogen IX during heme biosynthesis Escherichia coli protoporphyrinogen IX + CO2 + L-methionine + 5'-deoxyadenosine - ? 375097 1.3.98.3 coproporphyrinogen-III + S-adenosyl-L-methionine HemN catalyzes the prepenultimate step in anaerobic heme biosynthesis Escherichia coli protoporphyrinogen IX + CO2 + L-methionine + 5'-deoxyadenosine - ? 375097 1.3.98.3 coproporphyrinogen-III + S-adenosyl-L-methionine HemN catalyzes the oxygen-independent conversion of coproporphyrinogen-III to protoporphyrinogen IX, requires S-adenosyl-L-methionine, NAD(P)H and additional cytoplasmatic components for catalysis. Cys-62, Cys-66 and Cys-69 are part of the conserved CXXXCXXC motif and essential for iron-sulfur cluster formation and enzyme function. Gly-111 and Gly-113 are part of the potential GGGTP S-adenosyl-L-methionine binding motif and essential for enzymatic function, catalytic, radical mechanism Escherichia coli protoporphyrinogen IX + CO2 + L-methionine + 5'-deoxyadenosine - ? 375097 1.3.98.3 coproporphyrinogen-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 - ? 375097 1.3.98.3 coproporphyrinogen-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 - ? 375097 1.3.98.3 harderoporphyrinogen + 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 - ? 426471 1.3.98.3 harderoporphyrinogen + S-adenosyl-L-methionine chemical substrate sythesis, overview Escherichia coli protoporphyrinogen IX + CO2 + L-methionine + 5'-deoxyadenosine - ? 414688 1.3.98.3 additional information 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 ? - ? 89 1.3.98.3 additional information HemW shows no coproporphyrinogen III oxidase activity in vivo or in vitro Lactococcus lactis ? - ? 89 1.3.98.3 myo-inositol + S-adenosyl-L-methionine 0.9% activity compared to 2-deoxy-scyllo-inosamine Niallia circulans ? + CO2 + L-methionine + 5'-deoxyadenosine - ? 397813 1.3.98.3 scyllo-inositol + S-adenosyl-L-methionine 3.3% activity compared to 2-deoxy-scyllo-inosamine Niallia circulans ? + CO2 + L-methionine + 5'-deoxyadenosine - ? 398304