This enzyme catalyses the second of three steps leading to the formation of siroheme from uroporphyrinogen III. The first step involves the donation of two S-adenosyl-L-methionine-derived methyl groups to carbons 2 and 7 of uroporphyrinogen III to form precorrin-2 (EC 2.1.1.107, uroporphyrin-III C-methyltransferase) and the third step involves the chelation of ferrous iron to sirohydrochlorin to form siroheme (EC 4.99.1.4, sirohydrochlorin ferrochelatase). In Saccharomyces cerevisiae, the last two steps are carried out by a single bifunctional enzyme, Met8p. In some bacteria, steps 1-3 are catalysed by a single multifunctional protein called CysG, whereas in Bacillus megaterium, three separate enzymes carry out each of the steps, with SirC being responsible for the above reaction.
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
precorrin-2 + NAD+ = sirohydrochlorin + NADH + H+
first step; This enzyme catalyses the second of three steps leading to the formation of siroheme from uroporphyrinogen III. The first step involves the donation of two S-adenosyl-L-methionine-derived methyl groups to carbons 2 and 7 of uroporphyrinogen III to form precorrin-2 (EC 2.1.1.107, uroporphyrin-III C-methyltransferase) and the third step involves the chelation of ferrous iron to sirohydrochlorin to form siroheme (EC 4.99.1.4, sirohydrochlorin ferrochelatase). In Saccharomyces cerevisiae, the last two steps are carried out by a single bifunctional enzyme, Met8p. In some bacteria, steps 1-3 are catalysed by a single multifunctional protein called CysG, whereas in Bacillus megaterium, three separate enzymes carry out each of the steps, with SirC being responsible for the above reaction
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SYSTEMATIC NAME
IUBMB Comments
precorrin-2:NAD+ oxidoreductase
This enzyme catalyses the second of three steps leading to the formation of siroheme from uroporphyrinogen III. The first step involves the donation of two S-adenosyl-L-methionine-derived methyl groups to carbons 2 and 7 of uroporphyrinogen III to form precorrin-2 (EC 2.1.1.107, uroporphyrin-III C-methyltransferase) and the third step involves the chelation of ferrous iron to sirohydrochlorin to form siroheme (EC 4.99.1.4, sirohydrochlorin ferrochelatase). In Saccharomyces cerevisiae, the last two steps are carried out by a single bifunctional enzyme, Met8p. In some bacteria, steps 1-3 are catalysed by a single multifunctional protein called CysG, whereas in Bacillus megaterium, three separate enzymes carry out each of the steps, with SirC being responsible for the above reaction.
large multifunctional protein that catalyzes four diverse reactions, 2 S-adensyl-L-methionine-dependent methylations, NAD+-dependent tetrapyrrole dehydrogenation and metal chelation
multifunctional protein involved in S-adenosyl-L-methionine-dependent methylation, pyridine dinucleotide dependent dehydrogenation, and ferrochelation, second of three steps leading to formation of siroheme from uroporphyrinogen III
multifunctional protein involved in S-adenosyl-L-methionine-dependent methylation, pyridine dinucleotide dependent dehydrogenation, and ferrochelation, second of three steps leading to formation of siroheme from uroporphyrinogen III
precorrin-2 is the precursor of both siroheme and B12, first reaction specific to B12 synthesis, second of three steps leading to formation of siroheme from uroporphyrinogen III
multifunctional protein involved in S-adenosyl-L-methionine-dependent methylation, pyridine dinucleotide dependent dehydrogenation, and ferrochelation, second of three steps leading to formation of siroheme from uroporphyrinogen III
multifunctional protein involved in S-adenosyl-L-methionine-dependent methylation, pyridine dinucleotide dependent dehydrogenation, and ferrochelation, second of three steps leading to formation of siroheme from uroporphyrinogen III
precorrin-2 is the precursor of both siroheme and B12, first reaction specific to B12 synthesis, second of three steps leading to formation of siroheme from uroporphyrinogen III
Identification and functional analysis of enzymes required for precorrin-2 dehydrogenation and metal ion insertion in the biosynthesis of sirohaem and cobalamin in Bacillus megaterium